Nuclear pore complexes (NPCs) are the sole gateways between the nucleus and the cytoplasm of eukaryotic cells and they mediate all macromolecular trafficking between these cellular compartments. Nucleocytoplasmic transport is highly selective and precisely regulated and as such an important aspect of normal cellular function. Defects in this process or in its machinery have been linked to various human diseases, including cancer. Nucleoporins, which are about 30 proteins that built up NPCs, are critical players in nucleocytoplasmic transport and have also been shown to be key players in numerous other cellular processes, such as cell cycle control and gene expression regulation. This review will focus on the three nucleoporins Nup98, Nup214, and Nup358. Common to them is their significance in nucleocytoplasmic transport, their multiple other functions, and being targets for chromosomal translocations that lead to haematopoietic malignancies, in particular acute myeloid leukaemia. The underlying molecular mechanisms of nucleoporin-associated leukaemias are only poorly understood but share some characteristics and are distinguished by their poor prognosis and therapy outcome. 1. Introduction 1.1. Nuclear Pore Complexes The nuclear envelope (NE) serves as a boundary that separates nuclear and cytoplasmic compartments to protect the genome. This compartmentalization necessitates the transport of RNAs and proteins across the NE and this bidirectional macromolecular trafficking occurs through nuclear pore complexes (NPCs) [1, 2]. NPCs are large multiprotein assemblies, which both in vertebrates and yeast consist of ~30 different proteins, known as nucleoporins or Nups, [3–5]. Nucleoporins assemble into repetitively arranged subcomplexes to form NPCs with the pseudo-8-fold rotational symmetry [6–10]. In total, NPCs are estimated to be formed from about 500–1000 individual proteins [10, 11], which account for a molecular weight of about 110？MDa in vertebrates, according to scanning transmission electron microscopy and proteomic analyses [4, 10, 12]. The principle structural organization of the NPC has been determined by distinct electron microscopy (EM) approaches, including cryo-EM tomography, mainly in Xenopus laevis oocyte nuclei, but also in yeast, amoebozoa, plants, and human and appears as evolutionary conserved [6, 9, 10, 13–19]. Overall, NPCs are characterized by a roughly tripartite architecture: a central framework (also known as spoke complex, spoke-ring complex, or scaffold-ring complex) that is decorated with eight cytoplasmic filaments and a
References
[1]
S. W？lde and R. H. Kehlenbach, “The part and the whole: functions of nucleoporins in nucleocytoplasmic transport,” Trends in Cell Biology, vol. 20, no. 8, pp. 461–469, 2010.
[2]
S. R. Wente and M. P. Rout, “The nuclear pore complex and nuclear transport,” Cold Spring Harbor Perspectives in Biology, vol. 2, no. 10, Article ID a000562, 2010.
[3]
J. M. Cronshaw, A. N. Krutchinsky, W. Zhang, B. T. Chait, and M. L. J. Matunis, “Proteomic analysis of the mammalian nuclear pore complex,” Journal of Cell Biology, vol. 158, no. 5, pp. 915–927, 2002.
[4]
A. Ori, N. Banterle, M. Iskar et al., “Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines,” Molecular Systems Biology, vol. 9, article 648, 2013.
[5]
M. P. Rout, J. D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B. T. Chait, “The yeast nuclear pore complex: composition, architecture, transport mechanism,” Journal of Cell Biology, vol. 148, no. 4, pp. 635–651, 2000.
[6]
B. Fahrenkrog and U. Aebi, “The nuclear pore complex: nucleocytoplasmic transport and beyond,” Nature Reviews Molecular Cell Biology, vol. 4, no. 10, pp. 757–766, 2003.
[7]
R. Y. H. Lim, U. Aebi, and B. Fahrenkrog, “Towards reconciling structure and function in the nuclear pore complex,” Histochemistry and Cell Biology, vol. 129, no. 2, pp. 105–116, 2008.
[8]
M. A. D'Angelo and M. W. Hetzer, “Structure, dynamics and function of nuclear pore complexes,” Trends in Cell Biology, vol. 18, no. 10, pp. 456–466, 2008.
[9]
T. Maimon, N. Elad, I. Dahan, and O. Medalia, “The human nuclear pore complex as revealed by cryo-electron tomography,” Structure, vol. 20, no. 6, pp. 998–1006, 2012.
[10]
K. H. Bui, A. von Appen, A. L. Diguilio et al., “Integrated structural analysis of the human nuclear pore complex scaffold,” Cell, vol. 155, pp. 1233–1243, 2013.
[11]
F. Alber, S. Dokudovskaya, L. M. Veenhoff et al., “The molecular architecture of the nuclear pore complex,” Nature, vol. 450, no. 7170, pp. 695–701, 2007.
[12]
R. Reichelt, A. Holzenburg, E. L. Buhle Jr., M. Jarnik, A. Engel, and U. Aebi, “Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components,” Journal of Cell Biology, vol. 110, no. 4, pp. 883–894, 1990.
[13]
M. Capelson, C. Doucet, and M. W. Hetzer, “Nuclear pore complexes: guardians of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 75, pp. 585–597, 2011.
[14]
D. Stoffler, B. Feja, B. Fahrenkrog, J. Walz, D. Typke, and U. Aebi, “Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport,” Journal of Molecular Biology, vol. 328, no. 1, pp. 119–130, 2003.
[15]
M. Beck, F. F？rster, M. Ecke et al., “Nuclear pore complex structure and dynamics revealed by cryoelectron tomography,” Science, vol. 306, no. 5700, pp. 1387–1390, 2004.
[16]
B. Fahrenkrog, E. C. Hurt, U. Aebi, and N. Panté, “Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes,” Journal of Cell Biology, vol. 143, no. 3, pp. 577–588, 1998.
[17]
J. Fiserova, E. Kiseleva, and M. W. Goldberg, “Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells,” Plant Journal, vol. 59, no. 2, pp. 243–255, 2009.
[18]
E. Kiseleva, T. D. Allen, S. Rutherford, M. Bucci, S. R. Wente, and M. W. Goldberg, “Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments,” Journal of Structural Biology, vol. 145, no. 3, pp. 272–288, 2004.
[19]
D. Frenkiel-Krispin, B. Maco, U. Aebi, and O. Medalia, “Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture,” Journal of Molecular Biology, vol. 395, no. 3, pp. 578–586, 2009.
[20]
M. Beck, V. Lǔí, F. F？rster, W. Baumeister, and O. Medalia, “Snapshots of nuclear pore complexes in action captured by cryo-electron tomography,” Nature, vol. 449, no. 7162, pp. 611–615, 2007.
[21]
N. Panté and M. Kann, “Nuclear pore complex is able to transport macromolecules with diameters of ~39？nm,” Molecular Biology of the Cell, vol. 13, no. 2, pp. 425–434, 2002.
[22]
K. Enss, T. Danker, A. Schlune, I. Buchholz, and H. Oberleithner, “Passive transport of macromolecules through xenopus laevis nuclear envelope,” Journal of Membrane Biology, vol. 196, no. 3, pp. 147–155, 2003.
[23]
O. Keminer and R. Peters, “Permeability of single nuclear pores,” Biophysical Journal, vol. 77, no. 1, pp. 217–228, 1999.
[24]
D. Mohr, S. Frey, T. Fischer, T. Güttler, and D. G？rlich, “Characterisation of the passive permeability barrier of nuclear pore complexes,” The EMBO Journal, vol. 28, no. 17, pp. 2541–2553, 2009.
[25]
N. Elad, T. Maimon, D. Frenkiel-Krispin, R. Y. Lim, and O. Medalia, “Structural analysis of the nuclear pore complex by integrated approaches,” Current Opinion in Structural Biology, vol. 19, no. 2, pp. 226–232, 2009.
[26]
M. Raices and M. A. D'Angelo, “Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions,” Nature Reviews Molecular Cell Biology, vol. 13, no. 11, pp. 687–699, 2012.
[27]
D. G？rlich and U. Kutay, “Transport between the cell nucleus and the cytoplasm,” Annual Review of Cell and Developmental Biology, vol. 15, pp. 607–660, 1999.
[28]
T. U. Schwartz, “Modularity within the architecture of the nuclear pore complex,” Current Opinion in Structural Biology, vol. 15, no. 2, pp. 221–226, 2005.
[29]
D. Devos, S. Dokudovskaya, R. Williams et al., “Simple fold composition and modular architecture of the nuclear pore complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 7, pp. 2172–2177, 2006.
[30]
A. Szymborska, A. de Marco, N. Daigle, V. C. Cordes, J. A. Briggs, and J. Ellenberg, “Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging,” Science, vol. 341, pp. 655–658, 2013.
[31]
K. Thierbach, A. von Appen, M. Thoms, M. Beck, D. Flemming, and E. Hurt, “Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy,” Structure, vol. 21, pp. 1672–1682, 2013.
[32]
B. Fahrenkrog, J. K？ser, and U. Aebi, “The nuclear pore complex: a jack of all trades?” Trends in Biochemical Sciences, vol. 29, no. 4, pp. 175–182, 2004.
[33]
M. Capelson and M. W. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” EMBO Reports, vol. 10, no. 7, pp. 697–705, 2009.
[34]
T. M. Franks and M. W. Hetzer, “The role of Nup98 in transcription regulation in healthy and diseased cells,” Trends in Cell Biology, vol. 23, no. 3, pp. 112–117, 2013.
[35]
Y. Liang, T. M. Franks, M. C. Marchetto, F. H. Gage, and M. W. Hetzer, “Dynamic association of NUP98 with the human genome,” PLoS Genetics, vol. 9, no. 2, Article ID e1003308, 2013.
[36]
B. Kalverda, H. Pickersgill, V. V. Shloma, and M. Fornerod, “Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm,” Cell, vol. 140, no. 3, pp. 360–371, 2010.
[37]
S. Mendjan, M. Taipale, J. Kind et al., “Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila,” Molecular Cell, vol. 21, no. 6, pp. 811–823, 2006.
[38]
J. M. Vaquerizas, R. Suyama, J. Kind, K. Miura, N. M. Luscombe, and A. Akhtar, “Nuclear pore proteins Nup153 and megator define transcriptionally active regions in the Drosophila genome,” PLoS Genetics, vol. 6, no. 2, Article ID e1000846, 2010.
[39]
G. Chatel and B. Fahrenkrog, “Nucleoporins: leaving the nuclear pore complex for a successful mitosis,” Cellular Signalling, vol. 23, no. 10, pp. 1555–1562, 2011.
[40]
R. Wozniak, B. Burke, and V. Doye, “Nuclear transport and the mitotic apparatus: an evolving relationship,” Cellular and Molecular Life Sciences, vol. 67, no. 13, pp. 2215–2230, 2010.
[41]
H. Nakano, W. Wang, C. Hashizume, T. Funasaka, H. Sato, and R. W. Wong, “Unexpected role of nucleoporins in coordination of cell cycle progression,” Cell Cycle, vol. 10, no. 3, pp. 425–433, 2011.
[42]
C. Plass, C. Oakes, W. Blum, and G. Marcucci, “Epigenetics in acute myeloid leukemia,” Seminars in Oncology, vol. 35, no. 4, pp. 378–387, 2008.
[43]
R. A. Alharbi, R. Pettengell, H. S. Pandha, and R. Morgan, “The role of HOX genes in normal hematopoiesis and acute leukemia,” Leukemia, vol. 27, no. 5, pp. 1000–1008, 2013.
[44]
D. G. Grier, A. Thompson, A. Kwasniewska, G. J. McGonigle, H. L. Halliday, and T. R. Lappin, “The pathophysiology of HOX genes and their role in cancer,” Journal of Pathology, vol. 205, no. 2, pp. 154–171, 2005.
[45]
G. G. Wang, L. Cai, M. P. Pasillas, and M. P. Kamps, “NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis,” Nature Cell Biology, vol. 9, no. 7, pp. 804–812, 2007.
[46]
A. R. Kumar, W. A. Hudson, W. Chen, R. Nishiuchi, Q. Yao, and J. H. Kersey, “Hoxa9 influences the phenotype but not the incidence of Mll-AF9 fusion gene leukemia,” Blood, vol. 103, no. 5, pp. 1823–1828, 2004.
[47]
H. Liu, E. H.-Y. Cheng, and J. J.-D. Hsieh, “MLL fusions: pathways to leukemia,” Cancer Biology and Therapy, vol. 8, no. 13, pp. 1204–1211, 2009.
[48]
M. Faretta, L. di Croce, and P. G. Pelicci, “Effects of the acute myeloid leukemia-associated fusion proteins on nuclear architecture,” Seminars in Hematology, vol. 38, no. 1, pp. 42–53, 2001.
[49]
J. Chen, O. Odenike, and J. D. Rowley, “Leukaemogenesis: more than mutant genes,” Nature Reviews Cancer, vol. 10, no. 1, pp. 23–36, 2010.
[50]
R. P. Hasserjian, “Acute myeloid leukemia: advances in diagnosis and classification,” International Journal of Laboratory Hematology, vol. 35, no. 3, pp. 358–366, 2013.
[51]
S. M. Gough, C. I. Slape, and P. D. Aplan, “NUP98 gene fusions and hematopoietic malignancies: common themes and new biologic insights,” Blood, vol. 118, no. 24, pp. 6247–6257, 2011.
[52]
L. Gar？on, M. Libura, E. Delabesse et al., “DEK-CAN molecular monitoring of myeloid malignancies could aid therapeutic stratification,” Leukemia, vol. 19, no. 8, pp. 1338–1344, 2005.
[53]
M. Andreeff, V. Ruvolo, S. Gadgil et al., “HOX expression patterns identify a common signature for favorable AML,” Leukemia, vol. 22, no. 11, pp. 2041–2047, 2008.
[54]
E. R. Griffis, N. Altan, J. Lippincott-Schwartz, and M. A. Powers, “Nup98 is a mobile nucleoporin with transcription-dependent dynamics,” Molecular Biology of the Cell, vol. 13, no. 4, pp. 1282–1297, 2002.
[55]
E. R. Griffis, B. Craige, C. Dimaano, K. S. Ullman, and M. A. Powers, “Distinct functional domains within nucleoporins Nup153 and Nup98 mediate transcription-dependent mobility,” Molecular Biology of the Cell, vol. 15, pp. 1991–2002, 2004.
[56]
B. M. A. Fontoura, G. Blobel, and M. J. Matunis, “A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96,” Journal of Cell Biology, vol. 144, no. 6, pp. 1097–1112, 1999.
[57]
M. Iwamoto, H. Asakawa, Y. Hiraoka, and T. Haraguchi, “Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms,” Genes to Cells, vol. 15, no. 7, pp. 661–669, 2010.
[58]
A. E. Hodel, M. R. Hodel, E. R. Griffis et al., “The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98,” Molecular Cell, vol. 10, no. 2, pp. 347–358, 2002.
[59]
J. S. Rosenblum and G. Blobel, “Autoproteolysis in nucleoporin biogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 20, pp. 11370–11375, 1999.
[60]
M. Oka, M. Asally, Y. Yasuda, Y. Ogawa, T. Tachibana, and Y. Yoneda, “The mobile FG nucleoporin Nup98 is a cofactor for Crm1-dependent protein export,” Molecular Biology of the Cell, vol. 21, no. 11, pp. 1885–1896, 2010.
[61]
A. Takeda, N. J. Sarma, A. M. Abdul-Nabi, and N. R. Yaseen, “Inhibition of CRM1-mediated nuclear export of transcription factors by leukemogenic NUP98 fusion proteins,” Journal of Biological Chemistry, vol. 285, no. 21, pp. 16248–16257, 2010.
[62]
M. B. Blevins, A. M. Smith, E. M. Phillips, and M. A. Powers, “Complex formation among the RNA export proteins Nup98, Rae1/Gle2, and TAP,” Journal of Biological Chemistry, vol. 278, no. 23, pp. 20979–20988, 2003.
[63]
A. Bachi, I. C. Braun, J. P. Rodrigues et al., “The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates,” RNA, vol. 6, no. 1, pp. 136–158, 2000.
[64]
Y. Ren, H. S. Seo, G. Blobel, and A. Hoelz, “Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 23, pp. 10406–10411, 2010.
[65]
C. E. J. Pritchard, M. Fornerod, L. H. Kasper, and J. M. A. van Deursen, “RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains,” Journal of Cell Biology, vol. 145, no. 2, pp. 237–253, 1999.
[66]
L. H. Kasper, P. K. Brindle, C. A. Schnabel, C. E. J. Pritchard, M. L. Cleary, and J. M. A. van Deursen, “CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity,” Molecular and Cellular Biology, vol. 19, no. 1, pp. 764–776, 1999.
[67]
E. R. Griffis, S. Xu, and M. A. Powers, “Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes,” Molecular Biology of the Cell, vol. 14, no. 2, pp. 600–610, 2003.
[68]
V. E. Gould, A. Orucevic, H. Zentgraf, P. Gattuso, N. Martinez, and A. Alonso, “Nup88 (karyoporin) in human malignant neoplasms and dysplasias: correlations of immunostaining of tissue sections, cytologic smears, and immunoblot analysis,” Human Pathology, vol. 33, no. 5, pp. 536–544, 2002.
[69]
S. Xu and M. A. Powers, “Nuclear pore proteins and cancer,” Seminars in Cell and Developmental Biology, vol. 20, no. 5, pp. 620–630, 2009.
[70]
K. S. Ullman, S. Shah, M. A. Powers, and D. J. Forbes, “The nucleoporin Nup153 plays a critical role in multiple types of nuclear export,” Molecular Biology of the Cell, vol. 10, no. 3, pp. 649–664, 1999.
[71]
E. Voronina and G. Seydoux, “The C. elegans homolog of nucleoporin Nup98 is required for the integrity and function of germline P granules,” Development, vol. 137, no. 9, pp. 1441–1450, 2010.
[72]
S. Krull, J. Thyberg, B. Bj？rkroth, H. R. Rackwitz, and V. C. Cordes, “Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket,” Molecular Biology of the Cell, vol. 15, no. 9, pp. 4261–4277, 2004.
[73]
G. Chatel, S. H. Desai, A. L. Mattheyses, M. A. Powers, and B. Fahrenkrog, “Domain topology of nucleoporin Nup98 within the nuclear pore complex,” Journal of Structural Biology, vol. 177, no. 1, pp. 81–89, 2012.
[74]
D. P. Denning, S. S. Patel, V. Uversky, A. L. Fink, and M. Rexach, “Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 5, pp. 2450–2455, 2003.
[75]
D. P. Denning, V. Uversky, S. S. Patel, A. L. Fink, and M. Rexach, “The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein,” Journal of Biological Chemistry, vol. 277, no. 36, pp. 33447–33455, 2002.
[76]
S. S. Patel, B. J. Belmont, J. M. Sante, and M. F. Rexach, “Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex,” Cell, vol. 129, no. 1, pp. 83–96, 2007.
[77]
V. V. Krishnan, E. Y. Lau, J. Yamada et al., “Intramolecular cohesion of coils mediated by phenylalanine-glycine motifs in the natively unfolded domain of a nucleoporin,” PLoS Computational Biology, vol. 4, no. 8, Article ID e1000145, 2008.
[78]
J. Yamada, J. L. Phillips, S. Patel et al., “A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins,” Molecular and Cellular Proteomics, vol. 9, no. 10, pp. 2205–2224, 2010.
[79]
B. Fahrenkrog, B. Maco, A. M. Fager et al., “Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex,” Journal of Structural Biology, vol. 140, no. 1–3, pp. 254–267, 2002.
[80]
S. M. Paulillo, E. M. Phillips, J. K？ser et al., “Nucleoporin domain topology is linked to the transport status of the nuclear pore complex,” Journal of Molecular Biology, vol. 351, no. 4, pp. 784–798, 2005.
[81]
S. M. Paulillo, M. A. Powers, K. S. Ullman, and B. Fahrenkrog, “Changes in nucleoporin domain topology in response to chemical effectors,” Journal of Molecular Biology, vol. 363, no. 1, pp. 39–50, 2006.
[82]
K. Schwarz-Herion, B. Maco, U. Sauder, and B. Fahrenkrog, “Domain topology of the p62 complex within the 3-D architecture of the nuclear pore complex,” Journal of Molecular Biology, vol. 370, no. 4, pp. 796–806, 2007.
[83]
X. Wu, L. H. Kasper, R. T. Mantcheva, G. T. Mantchev, M. J. Springett, and J. M. A. van Deursen, “Disruption of the FG nucleoporin Nup98 causes selective changes in nuclear pore complex stoichiometry and function,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 6, pp. 3191–3196, 2001.
[84]
M. A. Powers, D. J. Forbes, J. E. Dahlberg, and E. Lund, “The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways,” The Journal of Cell Biology, vol. 136, pp. 241–250, 1997.
[85]
M. A. Powers, C. Macaulay, F. R. Masiarz, and D. J. Forbes, “Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication,” Journal of Cell Biology, vol. 128, no. 5, pp. 721–736, 1995.
[86]
B. M. A. Fontoura, G. Blobel, and N. R. Yaseen, “The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin β2-mediated nuclear import,” Journal of Biological Chemistry, vol. 275, no. 40, pp. 31289–31296, 2000.
[87]
A. Radu, M. S. Moore, and G. Blobel, “The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex,” Cell, vol. 81, no. 2, pp. 215–222, 1995.
[88]
A. S. Zolotukhin and B. K. Felber, “Nucleoporins Nup98 and Nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev,” Journal of Virology, vol. 73, no. 1, pp. 120–127, 1999.
[89]
C. P. C. de Souza, K. P. Horn, K. Masker, and S. A. Osmani, “The SONBNUP98 nucleoporin interacts with the NIMA Kinase in aspergillus nidulans,” Genetics, vol. 165, no. 3, pp. 1071–1081, 2003.
[90]
B. B. Hülsmann, A. A. Labokha, and D. G？rlich, “The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model,” Cell, vol. 150, no. 4, pp. 738–751, 2012.
[91]
M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. W. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” Cell, vol. 140, no. 3, pp. 372–383, 2010.
[92]
W. H. Light, J. Freaney, V. Sood et al., “A conserved role for human Nup98 in altering chromatin structure and promoting epigenetic transcriptional memory,” PLoS Biology, vol. 11, no. 3, Article ID e1001524, 2013.
[93]
S. Singer, R. Zhao, A. M. Barsotti et al., “Nuclear pore component Nup98 is a potential tumor suppressor and regulates posttranscriptional expression of select p53 target genes,” Molecular Cell, vol. 48, no. 5, pp. 799–810, 2012.
[94]
C. P. C. de Souza, S. B. Hashmi, K. P. Horn, and S. A. Osmani, “A point mutation in the Aspergillus nidulans sonBNup98 nuclear pore complex gene causes conditional DNA damage sensitivity,” Genetics, vol. 174, no. 4, pp. 1881–1893, 2006.
[95]
M. K. Cross and M. A. Powers, “Nup98 regulates bipolar spindle assembly through association with microtubules and opposition of MCAK,” Molecular Biology of the Cell, vol. 22, no. 5, pp. 661–672, 2011.
[96]
K. B. Jeganathan, D. J. Baker, and J. M. van Deursen, “Securin associates with APCCdh1 in prometaphase but its destruction is delayed by Rae1 and Nup98 until the metaphase/anaphase transition,” Cell Cycle, vol. 5, no. 4, pp. 366–370, 2006.
[97]
K. B. Jeganathan, L. Malureanu, and J. M. van Deursen, “The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation,” Nature, vol. 438, no. 7070, pp. 1036–1039, 2005.
[98]
S. Xu and M. A. Powers, “Nup98-homeodomain fusions interact with endogenous Nup98 during interphase and localize to kinetochores and chromosome arms during mitosis,” Molecular Biology of the Cell, vol. 21, no. 9, pp. 1585–1596, 2010.
[99]
J. Borrow, A. M. Shearman, V. P. Stanton Jr. et al., “The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9,” Nature Genetics, vol. 12, pp. 159–167, 1996.
[100]
T. Nakamura, D. A. Largaespada, M. P. Lee et al., “Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia,” Nature Genetics, vol. 12, pp. 154–158, 1996.
[101]
D. H. Lam and P. D. Aplan, “NUP98 gene fusions in hematologic malignancies,” Leukemia, vol. 15, no. 11, pp. 1689–1695, 2001.
[102]
J. M. Scandura, P. Boccuni, J. Cammenga, and S. D. Nimer, “Transcription factor fusions in acute leukemia: variations on a theme,” Oncogene, vol. 21, pp. 3422–3444, 2002.
[103]
M. A. S. Moore, K. Y. Chung, M. Plasilova et al., “NUP98 dysregulation in myeloid leukemogenesis,” Annals of the New York Academy of Sciences, vol. 1106, pp. 114–142, 2007.
[104]
W. C. Chou, C. Y. Chen, H. A. Hou et al., “Acute myeloid leukemia bearing t(7;11)(p15;p15) is a distinct cytogenetic entity with poor outcome and a distinct mutation profile: comparative analysis of 493 adult patients,” Leukemia, vol. 23, pp. 1303–1310, 2009.
[105]
P. Gorello, V. Nofrini, L. Brandimarte et al., “Inv(11)(p15q22)/NUP98-DDX10 fusion and isoforms in a new case of de novo acute myeloid leukemia,” Cancer Genetics, vol. 206, no. 3, pp. 92–96, 2013.
[106]
N. Shah and S. Sukumar, “The Hox genes and their roles in oncogenesis,” Nature Reviews Cancer, vol. 10, no. 5, pp. 361–371, 2010.
[107]
K. R. Calvo, D. B. Sykes, M. P. Pasillas, and M. P. Kamps, “Nup98-Hoxa9 immortalizes myeloid progenitors, enforces expression of Hoxa9, Hoxa7 and Meis1, and alters cytokine-specific responses in a manner similar to that induced by retroviral co-expression of Hoxa9 and Meis1,” Oncogene, vol. 21, no. 27, pp. 4247–4256, 2002.
[108]
K. Y. Chung, G. Morrone, J. J. Schuringa et al., “Enforced expression of NUP98-HOXA9 in human CD34+ cells enhances stem cell proliferation,” Cancer Research, vol. 66, no. 24, pp. 11781–11791, 2006.
[109]
K. Hirose, C. Abramovich, B. Argiropoulos, and R. K. Humphries, “Leukemogenic properties of NUP98-PMX1 are linked to NUP98 and homeodomain sequence functions but not to binding properties of PMX1 to serum response factor,” Oncogene, vol. 27, no. 46, pp. 6056–6067, 2008.
[110]
D. Jankovic, P. Gorello, T. Liu et al., “Leukemogenic mechanisms and targets of a NUP98/HHEX fusion in acute myeloid leukemia,” Blood, vol. 111, no. 12, pp. 5672–5682, 2008.
[111]
L. Palmqvist, N. Pineault, C. Wasslavik, and R. K. Humphries, “Candidate genes for expansion and transformation of hematopoietic stem cells by NUP98-HOX fusion genes,” PLoS ONE, vol. 2, no. 8, article e768, 2007.
[112]
A. Takeda, C. Goolsby, and N. R. Yaseen, “NUP98-HOXA9 induces long-term proliferation and blocks differentiation of primary human CD34+ hematopoietic cells,” Cancer Research, vol. 66, no. 13, pp. 6628–6637, 2006.
[113]
G. G. Wang, J. Song, Z. Wang et al., “Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger,” Nature, vol. 459, no. 7248, pp. 847–851, 2009.
[114]
T. Taketani, T. Taki, T. Nakamura et al., “High frequencies of simultaneous FLT3-ITD, WT1 and KIT mutations in hematological malignancies with NUP98-fusion genes,” Leukemia, vol. 24, no. 11, pp. 1975–1977, 2010.
[115]
A. Fasan, C. Haferlach, T. Alpermann, W. Kern, T. Haferlach, and S. Schnittger, “A rare but specific subset of adult AML patients can be defined by the cytogenetically cryptic NUP98-NSD1 fusion gene,” Leukemia, vol. 27, no. 1, pp. 245–248, 2013.
[116]
S. Akiki, S. A. Dyer, D. Grimwade et al., “NUP98-NSD1 fusion in association with FLT3-ITD mutation identifies a prognostically relevant subgroup of pediatric acute myeloid leukemia patients suitable for monitoring by real time quantitative PCR,” Genes Chromosomes Cancer, vol. 52, pp. 1053–1064, 2013.
[117]
S. Kaltenbach, G. Soler, C. Barin et al., “NUP98-MLL fusion in human acute myeloblastic leukemia,” Blood, vol. 116, no. 13, pp. 2332–2335, 2010.
[118]
J. Saw, D. J. Curtis, D. J. Hussey, A. Dobrovic, P. D. Aplan, and C. I. Slape, “The fusion partner specifies the oncogenic potential of NUP98 fusion proteins,” Leukemia Research, vol. 37, pp. 1668–1673, 2013.
[119]
E. R. Yassin, N. J. Sarma, A. M. Abdul-Nabi et al., “Dissection of the transformation of primary human hematopoietic cells by the oncogene NUP98-HOXA9,” PLoS ONE, vol. 4, no. 8, Article ID e6719, 2009.
[120]
T. Funasaka, H. Nakano, Y. Wu et al., “RNA export factor RAE1 contributes to NUP98-HOXA9-mediated leukemogenesis,” Cell Cycle, vol. 10, no. 9, pp. 1456–1467, 2010.
[121]
V. Salsi, S. Ferrari, P. Gorello et al., “NUP98 fusion oncoproteins promote aneuploidy by attenuating the mitotic spindle checkpoint,” Cancer Research, vol. 74, pp. 1079–1090, 2014.
[122]
A. M. Forrester, C. Grabher, E. R. Mcbride et al., “NUP98-HOXA9-transgenic zebrafish develop a myeloproliferative neoplasm and provide new insight into mechanisms of myeloid leukaemogenesis,” British Journal of Haematology, vol. 155, no. 2, pp. 167–181, 2011.
[123]
J. van Deursen, J. Boer, L. Kasper, and G. Grosveld, “G2 arrest and impaired nucleocytoplasmic transport in mouse embryos lacking the proto-oncogene CAN/Nup214,” The EMBO Journal, vol. 15, pp. 5574–5583, 1996.
[124]
R. Bernad, D. Engelsma, H. Sanderson, H. Pickersgill, and M. Fornerod, “Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear export,” Journal of Biological Chemistry, vol. 281, no. 28, pp. 19378–19386, 2006.
[125]
S. Hutten and R. H. Kehlenbach, “Nup214 is required for CRM1-dependent nuclear protein export in vivo,” Molecular and Cellular Biology, vol. 26, no. 18, pp. 6772–6785, 2006.
[126]
J. Boer, J. Bonten-Surtel, and G. Grosveld, “Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis,” Molecular and Cellular Biology, vol. 18, no. 3, pp. 1236–1247, 1998.
[127]
D. Kraemer, R. W. Wozniak, G. Blobel, and A. Radu, “The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 4, pp. 1519–1523, 1994.
[128]
N. Panté, R. Bastos, I. McMorrow, B. Burke, and U. Aebi, “Interactions and three-dimensional localization of a group of nuclear pore complex proteins,” Journal of Cell Biology, vol. 126, no. 3, pp. 603–617, 1994.
[129]
T. C. Walther, M. Fornerod, H. Pickersgill, M. Goldberg, T. D. Allen, and I. W. Mattaj, “The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins,” The EMBO Journal, vol. 20, no. 20, pp. 5703–5714, 2001.
[130]
M. Fornerod, J. van Deursen, S. van Baal et al., “The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88,” The EMBO Journal, vol. 16, pp. 807–816, 1997.
[131]
R. Bastos, L. R. de Pouplana, M. Enarson, K. Bodoor, and B. Burke, “Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex,” The Journal of Cell Biology, vol. 137, pp. 989–1000, 1997.
[132]
N. Xylourgidis, P. Roth, N. Sabri, V. Tsarouhas, and C. Samakovlis, “The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates NFκB activation in Drosophila,” Journal of Cell Science, vol. 119, no. 21, pp. 4409–4419, 2006.
[133]
P. Roth, N. Xylourgidis, N. Sabri, A. Uv, M. Fornerod, and C. Samakovlis, “The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the nuclear envelope and attenuates NES-mediated nuclear export,” Journal of Cell Biology, vol. 163, no. 4, pp. 701–706, 2003.
[134]
R. Bernad, H. van der Velde, M. Fornerod, and H. Pickersgill, “Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export,” Molecular and Cellular Biology, vol. 24, no. 6, pp. 2373–2384, 2004.
[135]
U. Stochaj, P. Bański, M. Kodiha, and N. Matusiewicz, “The N-terminal domain of the mammalian nucleoporin p62 interacts with other nucleoporins of the FXFG family during interphase,” Experimental Cell Research, vol. 312, no. 13, pp. 2490–2499, 2006.
[136]
J. Napetschnig, G. Blobel, and A. Hoelz, “Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 6, pp. 1783–1788, 2007.
[137]
B. Montpetit, N. D. Thomsen, K. J. Helmke, M. A. Seeliger, J. M. Berger, and K. Weis, “A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export,” Nature, vol. 472, no. 7342, pp. 238–244, 2011.
[138]
H. von Moeller, C. Basquin, and E. Conti, “The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner,” Nature Structural and Molecular Biology, vol. 16, no. 3, pp. 247–254, 2009.
[139]
C. S. Weirich, J. P. Erzberger, J. M. Berger, and K. Weis, “The N-terminal domain of Nup159 forms a β-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore,” Molecular Cell, vol. 16, no. 5, pp. 749–760, 2004.
[140]
J. Napetschnig, S. A. Kassube, E. W. Debler, R. W. Wong, G. Blobel, and A. Hoelz, “Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 9, pp. 3089–3094, 2009.
[141]
S. Kuersten, G. J. Arts, T. C. Walther, L. Englmeier, and I. W. Mattaj, “Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains,” Molecular and Cellular Biology, vol. 22, no. 16, pp. 5708–5720, 2002.
[142]
J. Katahira, K. Str？？er, A. Podtelejnikov, M. Mann, J. U. Jung, and E. Hurt, “The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human,” The EMBO Journal, vol. 18, no. 9, pp. 2593–2609, 1999.
[143]
S. Roloff, C. Spillner, and R. H. Kehlenbach, “Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1,” Journal of Biological Chemistry, vol. 288, no. 6, pp. 3952–3963, 2013.
[144]
C. Rollenhagen, P. Mühlh？usser, U. Kutay, and N. Panté, “Importin β-depending nuclear import pathways: role of the adapter proteins in the docking and releasing steps,” Molecular Biology of the Cell, vol. 14, no. 5, pp. 2104–2115, 2003.
[145]
L. Xu, Y. Kang, S. ？？l, and J. Massagué, “Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus,” Molecular Cell, vol. 10, no. 2, pp. 271–282, 2002.
[146]
J. A. Carman and S. G. Nadler, “Direct association of tristetraprolin with the nucleoporin CAN/Nup214,” Biochemical and Biophysical Research Communications, vol. 315, no. 2, pp. 445–449, 2004.
[147]
C. G. Besirli, E. F. Wagner, and E. M. Johnson Jr., “The limited role of NH2-terminal c-Jun phosphorylation in neuronal apoptosis: identification of the nuclear pore complex as a potential target of the JNK pathway,” Journal of Cell Biology, vol. 170, no. 3, pp. 401–411, 2005.
[148]
S. Strunze, M. F. Engelke, I.-H. Wang et al., “Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection,” Cell Host and Microbe, vol. 10, no. 3, pp. 210–223, 2011.
[149]
S. Strunze, L. C. Trotman, K. Boucke, and U. F. Greber, “Nuclear targeting of adenovirus type 2 requires CRM1-mediated nuclear export,” Molecular Biology of the Cell, vol. 16, no. 6, pp. 2999–3009, 2005.
[150]
M. von Lindern, D. Breems, S. van Baal, H. Adriaansen, and G. Grosveld, “Characterization of the translocation breakpoint sequences of two DEK-CAN fusion genes present in t(6;9) acute myeloid leukemia and a SET-CAN fusion gene found in a case of acute undifferentiated leukemia,” Genes Chromosomes and Cancer, vol. 5, no. 3, pp. 227–234, 1992.
[151]
C. Graux, J. Cools, C. Melotte et al., “Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia,” Nature Genetics, vol. 36, no. 10, pp. 1084–1089, 2004.
[152]
P. Gorello, R. la Starza, D. di Giacomo et al., “SQSTM1-NUP214: a new gene fusion in adult T-cell acute lymphoblastic leukemia,” Haematologica, vol. 95, no. 12, pp. 2161–2163, 2010.
[153]
S. Saito, M. Miyaji-Yamaguchi, and K. Nagata, “Aberrant intracellular localization of set-can fusion protein, associated with a leukemia, disorganizes nuclear export,” International Journal of Cancer, vol. 111, no. 4, pp. 501–507, 2004.
[154]
K. de Keersmaecker, J. L. Rocnik, R. Bernad et al., “Kinase activation and transformation by NUP214-ABL1 is dependent on the context of the nuclear pore,” Molecular Cell, vol. 31, no. 1, pp. 134–142, 2008.
[155]
K. de Keersmaecker, M. Versele, J. Cools, G. Superti-Furga, and O. Hantschel, “Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases,” Leukemia, vol. 22, no. 12, pp. 2208–2216, 2008.
[156]
M. Fornerod, J. Boer, S. van Baal et al., “Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements,” Oncogene, vol. 10, no. 9, pp. 1739–1748, 1995.
[157]
P. van Vlierberghe, M. van Grotel, J. Tchinda et al., “The recurrent SET-NUP214 fusion as a new HOXA activation mechanism in pediatric T-cell acute lymphoblastic leukemia,” Blood, vol. 111, no. 9, pp. 4668–4680, 2008.
[158]
U. ？zbek, A. Kandilci, S. van Baal et al., “SET-CAN, the product of the t(9;9) in acute undifferentiated leukemia, causes expansion of early hematopoietic progenitors and hyperproliferation of stomach mucosa in transgenic mice,” The American Journal of Pathology, vol. 171, no. 2, pp. 654–666, 2007.
[159]
M. von Lindern, M. Fornerod, S. van Baal et al., “The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA,” Molecular and Cellular Biology, vol. 12, no. 4, pp. 1687–1697, 1992.
[160]
R. ben Abdelali, A. Roggy, T. Leguay et al., “SET-NUP214 is a recurrent gammadelta lineage specific fusion transcript associated with cortico/chemoresistance in adult T-ALL,” Blood, vol. 123, no. 12, pp. 1860–1863, 2014.
[161]
J. D. Sandahl, E. A. Coenen, E. Forestier et al., “t(6;9)(p22;q34)/DEK-NUP214 rearranged pediatric myeloid leukemia: an international study on 62 patients,” Haematologica, vol. 99, no. 5, pp. 865–872, 2014.
[162]
M. Ageberg, K. Drott, T. Olofsson, U. Gullberg, and A. Lindmark, “Identification of a novel and myeloid specific role of the leukemia-associated fusion protein DEK-NUP214 leading to increased protein synthesis,” Genes Chromosomes and Cancer, vol. 47, no. 4, pp. 276–287, 2008.
[163]
C. Sanden, M. Ageberg, J. Petersson, A. Lennartsson, and U. Gullberg, “Forced expression of the DEK-NUP214 fusion protein promotes proliferation dependent on upregulation of mTOR,” BMC Cancer, vol. 13, article 440, 2013.
[164]
C. Graux, M. Stevens-Kroef, M. Lafage et al., “Heterogeneous patterns of amplification of the NUP214-ABL1 fusion gene in T-cell acute lymphoblastic leukemia,” Leukemia, vol. 23, no. 1, pp. 125–133, 2009.
[165]
P. Ballerini, M. Busson, S. Fasola et al., “NUP214-ABL1 amplification in t(5;14)/HOX11L2-positive ALL present with several forms and may have a prognostic significance,” Leukemia, vol. 19, no. 3, pp. 468–470, 2005.
[166]
K. de Keersmaecker, M. Porcu, L. Cox et al., “NUP214-ABL1-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK kinase and various interacting proteins,” Haematologica, vol. 99, pp. 85–93, 2014.
[167]
H. Quentmeier, B. Schneider, S. R？hrs et al., “SET-NUP214 fusion in acute myeloid leukemia-and T-cell acute lymphoblastic leukemia-derived cell lines,” Journal of Hematology and Oncology, vol. 2, article 3, 2009.
[168]
J. Wu, M. J. Matunis, D. Kraemer, G. Blobel, and E. Coutavas, “Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran- GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region,” Journal of Biological Chemistry, vol. 270, no. 23, pp. 14209–14213, 1995.
[169]
T. C. Walther, H. S. Pickersgill, V. C. Cordes et al., “The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import,” Journal of Cell Biology, vol. 158, no. 1, pp. 63–77, 2002.
[170]
N. Yokoyama, H. Hayashi, T. Seki et al., “A giant nucleopore protein that binds Ran/TC4,” Nature, vol. 376, no. 6536, pp. 184–188, 1995.
[171]
S. Hutten, A. Flotho, F. Melchior, and R. H. Kehlenbach, “The Nup358-RanGAP complex is required for efficient importin α/β-dependent nuclear import,” Molecular Biology of the Cell, vol. 19, no. 5, pp. 2300–2310, 2008.
[172]
S. Hutten, S. W？lde, C. Spillner, J. Hauber, and R. H. Kehlenbach, “The nuclear pore component Nup358 promotes transportin-dependent nuclear import,” Journal of Cell Science, vol. 122, no. 8, pp. 1100–1110, 2009.
[173]
S. W？lde, K. Thakar, S. Hutten et al., “The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner,” Traffic, vol. 13, no. 2, pp. 218–233, 2012.
[174]
B. B. Singh, H. H. Patel, R. Roepman, D. Schick, and P. A. Ferreira, “The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1,” Journal of Biological Chemistry, vol. 274, no. 52, pp. 37370–37378, 1999.
[175]
M. Hamada, A. Haeger, K. B. Jeganathan et al., “Ran-dependent docking of importin β- to RanBP2/Nup358 filaments is essential for protein import and cell viability,” Journal of Cell Biology, vol. 194, no. 4, pp. 597–612, 2011.
[176]
D. Salina, P. Enarson, J. B. Rattner, and B. Burke, “Nup358 integrates nuclear envelope breakdown with kinetochore assembly,” Journal of Cell Biology, vol. 162, no. 6, pp. 991–1001, 2003.
[177]
A. Arnaoutov, Y. Azuma, K. Ribbeck et al., “Crm1 is a mitotic effector of Ran-GTP in somatic cells,” Nature Cell Biology, vol. 7, no. 6, pp. 626–632, 2005.
[178]
J. Joseph, S.-T. Liu, S. A. Jablonski, T. J. Yen, and M. Dasso, “The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo,” Current Biology, vol. 14, no. 7, pp. 611–617, 2004.
[179]
C. Hashizume, A. Kobayashi, and R. W. Wong, “Down-modulation of nucleoporin RanBP2/Nup358 impaired chromosomal alignment and induced mitotic catastrophe,” Cell Death and Disease, vol. 4, article e854, 2013.
[180]
A. Pichler, A. Gast, J. S. Seeler, A. Dejean, and F. Melchior, “The nucleoporin RanBP2 has SUMO1 E3 ligase activity,” Cell, vol. 108, no. 1, pp. 109–120, 2002.
[181]
U. R. Klein, M. Haindl, E. A. Nigg, and S. Muller, “RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on borealin,” Molecular Biology of the Cell, vol. 20, no. 1, pp. 410–418, 2009.
[182]
O. Kirsh, J.-S. Seeler, A. Pichler et al., “The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase,” The EMBO Journal, vol. 21, no. 11, pp. 2682–2691, 2002.
[183]
M. M. Dawlaty, L. Malureanu, K. B. Jeganathan et al., “Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha,” Cell, vol. 133, no. 1, pp. 103–115, 2008.
[184]
A. Werner, A. Flotho, and F. Melchior, “The RanBP2/RanGAP1*SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase,” Molecular Cell, vol. 46, no. 3, pp. 287–298, 2012.
[185]
K. Mahadevan, H. Zhang, A. Akef et al., “RanBP2/Nup358 potentiates the translation of a subset of mRNAs encoding secretory proteins,” PLoS Biology, vol. 11, no. 4, Article ID e1001545, 2013.
[186]
K.-I. Cho, H. Yi, N. Tserentsoodol, K. Searle, and P. A. Ferreira, “Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress,” DMM Disease Models and Mechanisms, vol. 3, no. 9-10, pp. 595–604, 2010.
[187]
K.-I. Cho, H. Yi, A. Yeh et al., “Haploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neurons,” Cell Death and Differentiation, vol. 16, no. 2, pp. 287–297, 2009.
[188]
Y. Cai, B. B. Singh, A. Aslanukov, H. Zhao, and P. A. Ferreira, “The docking of kinesins, KIF5B and KIF5C, to ran-binding protein 2 (RanBP2) is mediated via a novel RanBP2 domain,” Journal of Biological Chemistry, vol. 276, no. 45, pp. 41594–41602, 2001.
[189]
T. A. Mavlyutov, Y. Cai, and P. A. Ferreira, “Identification of RanBP2- and kinesin-mediated transport pathways with restricted neuronal and subcellular localization,” Traffic, vol. 3, no. 9, pp. 630–640, 2002.
[190]
D. Splinter, M. E. Tanenbaum, A. Lindqvist et al., “Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry,” PLoS Biology, vol. 8, no. 4, 2010.
[191]
M. Asally, Y. Yasuda, M. Oka et al., “Nup358, a nucleoporin, functions as a key determinant of the nuclear pore complex structure remodeling during skeletal myogenesis,” The FEBS Journal, vol. 278, no. 4, pp. 610–621, 2011.
[192]
K. I. Cho, M. Haque, J. Wang et al., “Distinct and atypical intrinsic and extrinsic cell death pathways between photoreceptor cell types upon specific ablation of Ranbp2 in cone photoreceptors,” PLoS Genetics, vol. 9, Article ID e1003555, 2013.
[193]
C. Frohnert, S. Hutten, S. Walde, A. Nath, and R. H. Kehlenbach, “Importin 7 and nup358 promote nuclear import of the protein component of human telomerase,” PLoS ONE, vol. 9, Article ID e88887, 2014.
[194]
J. Joseph and M. Dasso, “The nucleoporin Nup358 associates with and regulates interphase microtubules,” The FEBS Letters, vol. 582, no. 2, pp. 190–196, 2008.
[195]
P. Murawala, M. M. Tripathi, P. Vyas, A. Salunke, and J. Joseph, “Nup358 interacts with APC and plays a role in cell polarization,” Journal of Cell Science, vol. 122, no. 17, pp. 3113–3122, 2009.
[196]
M. Gloerich, M. J. Vliem, E. Prummel et al., “The nucleoporin RanBP2 tethers the cAMP effector Epac1 and inhibits its catalytic activity,” Journal of Cell Biology, vol. 193, no. 6, pp. 1009–1020, 2011.
[197]
M. Gloerich and J. L. Bos, “Epac: defining a new mechanism for cAMP action,” Annual Review of Pharmacology and Toxicology, vol. 50, pp. 355–375, 2010.
[198]
P. A. Ferreira, T. A. Nakayama, W. L. Pak, and G. H. Travis, “Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin,” Nature, vol. 383, pp. 637–640, 1996.
[199]
P. A. Ferreira, T. A. Nakayama, and G. H. Travis, “Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ran-binding protein 2,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, pp. 1556–1561, 1997.
[200]
A. Aslanukov, R. Bhowmick, M. Guruju et al., “RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism,” PLoS Genetics, vol. 2, no. 10, p. e177, 2006.
[201]
K.-I. Cho, Y. Cai, H. Yi, A. Yeh, A. Aslanukov, and P. A. Ferreira, “Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function,” Traffic, vol. 8, no. 12, pp. 1722–1735, 2007.
[202]
K.-I. Cho, H. Yi, R. Desai, A. R. Hand, A. L. Haas, and P. A. Ferreira, “RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system,” EMBO Reports, vol. 10, no. 5, pp. 480–486, 2009.
[203]
C. Gervais, L. Dano, N. Perrusson et al., “A translocation t(2;8)(q12;p11) fuses FGFR1 to a novel partner gene, RANBP2/NUP358, in a myeloproliferative/myelodysplastic neoplasm,” Leukemia, vol. 27, no. 5, pp. 1186–1188, 2013.
[204]
J. H. Lim, S. Jang, C. J. Park et al., “RANBP2-ALK fusion combined with monosomy 7 in acute myelomonocytic leukemia,” Cancer Genetics, vol. 207, no. 1-2, pp. 40–45, 2014.
[205]
S. E. Lee, S. Y. Kang, K. Takeuchi, and Y. H. Ko, “Identification of RANBP2-ALK fusion in ALK positive diffuse large B-cell lymphoma,” Hematological Oncology, 2014.
[206]
Z. Ma, D. A. Hill, M. H. Collins et al., “Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor,” Genes Chromosomes and Cancer, vol. 37, no. 1, pp. 98–105, 2003.
[207]
A. Mari？o-Enríquez, W.-L. Wang, A. Roy et al., “Epithelioid inflammatory myofibroblastic sarcoma: an aggressive intra-abdominal variant of inflammatory myofibroblastic tumor with nuclear membrane or perinuclear alk,” The American Journal of Surgical Pathology, vol. 35, no. 1, pp. 135–144, 2011.
[208]
S.-T. Chen and J.-C. Lee, “An inflammatory myofibroblastic tumor in liver with ALK and RANBP2 gene rearrangement: combination of distinct morphologic, immunohistochemical, and genetic features,” Human Pathology, vol. 39, no. 12, pp. 1854–1858, 2008.
[209]
J. Li, W. H. Yin, K. Takeuchi, H. Guan, Y. H. Huang, and J. K. Chan, “Inflammatory myofibroblastic tumor with RANBP2 and ALK gene rearrangement: a report of two cases and literature review,” Diagnostic Pathology, vol. 8, article 147, 2013.
[210]
A. S. Patel, K. M. Murphy, A. L. Hawkins et al., “RANBP2 and CLTC are involved in ALK rearrangements in inflammatory myofibroblastic tumors,” Cancer Genetics and Cytogenetics, vol. 176, no. 2, pp. 107–114, 2007.
[211]
Y. Maesako, K. Izumi, S. Okamori et al., “inv(2)(p23q13)/RAN-binding protein 2 (RANBP2)-ALK fusion gene in myeloid leukemia that developed in an elderly woman,” International Journal of Hematology, vol. 99, pp. 202–207, 2014.
[212]
S. Hutten and R. H. Kehlenbach, “CRM1-mediated nuclear export: to the pore and beyond,” Trends in Cell Biology, vol. 17, no. 4, pp. 193–201, 2007.
[213]
P. Ranganathan, X. Yu, C. Na et al., “Preclinical activity of a novel CRM1 inhibitor in acute myeloid leukemia,” Blood, vol. 120, no. 9, pp. 1765–1773, 2012.
[214]
G. Ghannam, A. Takeda, T. Camarata, M. A. Moore, A. Viale, and N. R. Yaseen, “The oncogene Nup98-HOXA9 induces gene transcription in myeloid cells,” Journal of Biological Chemistry, vol. 279, no. 2, pp. 866–875, 2004.
[215]
T. Fujino, A. Suzuki, Y. Ito et al., “Single-translocation and double-chimeric transcripts: detection of NUP98-HOXA9 in myeloid leukemias with hOXA11 or HOXA13 breaks of the chromosomal translocation t(7;11)(p15;p15),” Blood, vol. 99, no. 4, pp. 1428–1433, 2002.
[216]
Y. Mizoguchi, N. Fujita, T. Taki, Y. Hayashi, and K. Hamamoto, “Juvenile myelomonocytic leukemia with t(7;11)(p15;p15) and NUP98-HOXA11 fusion,” The American Journal of Hematology, vol. 84, no. 5, pp. 295–297, 2009.
[217]
A. Suzuki, Y. Ito, G. Sashida et al., “t(7;11)(p15;p15) chronic myeloid leukaemia developed into blastic transformation showing a novel NUP98/HOXA11 fusion,” British Journal of Haematology, vol. 116, no. 1, pp. 170–172, 2002.
[218]
J. Nakahara, K. Kanekura, M. Nawa, S. Aiso, and N. Suzuki, “Abnormal expression of TIP30 and arrested nucleocytoplasmic transport within oligodendrocyte precursor cells in multiple sclerosis,” Journal of Clinical Investigation, vol. 119, no. 1, pp. 169–181, 2009.
[219]
T. Taketani, T. Taki, R. Ono, Y. Kobayashi, K. Ida, and Y. Hayashi, “The chromosome translocation t(7;11)(p15;15) in acute myeloid leukemia results in fusion of the NUP98 gene with a HOXA cluster gene, HOXA13, but not HOXA9,” Genes Chromosomes and Cancer, vol. 34, no. 4, pp. 437–443, 2002.
[220]
B.-W. Gu, Q. Wang, J.-M. Wang et al., “Major form of NUP98/HOXC11 fusion in adult AMLwith t(11;12)(p15;q13) translocation exhibits aberrant trans-regulatory activity,” Leukemia, vol. 17, no. 9, pp. 1858–1864, 2003.
[221]
T. Taketani, T. Taki, N. Shibuya, A. Kikuchi, R. Hanada, and Y. Hayashi, “Novel NUP98-HOXC11 fusion gene resulted from a chromosomal break within exon 1 of HOXC11 in acute myeloid leukemia with t(11;12)(p15;q13),” Cancer Research, vol. 62, no. 16, pp. 4571–4574, 2002.
[222]
R. La Starza, M. Trubia, B. Crescenzi et al., “Human homeobox gene HOXCI3 is the partner of NUP98 in adult acute myeloid leukemia with t(11;12)(p15;q13),” Genes Chromosomes and Cancer, vol. 36, no. 4, pp. 420–423, 2003.
[223]
I. Panagopoulos, M. Isaksson, R. Billstr？m, B. Str？mbeck, F. Mitelman, and B. Johansson, “Fusion of the NUP98 gene and the homeobox gene HOXC13 in acute myeloid leukemia with t(11;12)(p15;q13),” Genes Chromosomes and Cancer, vol. 36, no. 1, pp. 107–112, 2003.
[224]
N. To？i？, M. Stojiljkovi？, N. Colovi？, M. ？olovi？, and S. Pavlovi？, “Acute myeloid leukemia with NUP98-HOXC13 fusion and FLT3 internal tandem duplication mutation: case report and literature review,” Cancer Genetics and Cytogenetics, vol. 193, no. 2, pp. 98–103, 2009.
[225]
K. Terui, J. Kitazawa, Y. Takahashi et al., “Successful treatment of acute myelomonocytic leukaemia with NUP98-HOXD11 fusion transcripts and monitoring of minimal residual disease,” British Journal of Haematology, vol. 120, no. 2, pp. 274–276, 2003.
[226]
Y. Arai, T. Kyo, H. Miwa et al., “Heterogeneous fusion transcripts involving the NUP98 gene and HOXD13 gene activation in a case of acute myeloid leukemia with the t(2;11)(q31;p15) translocation,” Leukemia, vol. 14, no. 9, pp. 1621–1629, 2000.
[227]
M. Emerenciano, C. Meyer, M. L. MacEdo-Silva et al., “Backtracking to birth of the NUP98-HOXD13 gene fusion in an infant acute myeloid leukemia,” Leukemia, vol. 25, no. 7, pp. 1192–1194, 2011.
[228]
S. Z. Raza-Egilmez, S. N. Jani-Sait, M. Grossi, M. J. Higgins, T. B. Shows, and P. D. Aplan, “NUP98-HOXD13 gene fusion in therapy-related acute myelogenous leukemia,” Cancer Research, vol. 58, no. 19, pp. 4269–4273, 1998.
[229]
H. Shimada, Y. Arai, S. Sekiguchi, T. Ishii, S. Tanitsu, and M. Sasaki, “Generation of the NUP98-HOXD13 fusion transcript by a rare translocation, t(2;11)(q31;p15), in a case of infant leukaemia,” British Journal of Haematology, vol. 110, no. 1, pp. 210–213, 2000.
[230]
Y. N. Kobzev, J. Martinez-Climent, S. Lee, J. Chen, and J. D. Rowley, “Analysis of translocations that involve the NUP98 gene in patients with 11p15 chromosomal rearrangements,” Genes Chromosomes and Cancer, vol. 41, no. 4, pp. 339–352, 2004.
[231]
T. Nakamura, Y. Yamazaki, Y. Hatano, and I. Miura, “NUP98 is fused to PMX1 homeobox gene in human acute myelogenous leukemia with chromosome translocation t(1;11)(q23;p15),” Blood, vol. 94, no. 2, pp. 741–747, 1999.
[232]
L. Zhang, R. Alsabeh, C. Mecucci et al., “Rare t(1;11)(q23;p15) in therapy-related myelodysplastic syndrome evolving into acute myelomonocytic leukemia: a case report and review of the literature,” Cancer Genetics and Cytogenetics, vol. 178, no. 1, pp. 42–48, 2007.
[233]
C. Gervais, L. Mauvieux, N. Perrusson et al., “A new translocation t(9;11)(q34;p15) fuses NUP98 to a novel homeobox partner gene, PRRX2, in a therapy-related acute myeloid leukemia,” Leukemia, vol. 19, no. 1, pp. 145–148, 2005.
[234]
S. Lisboa, N. Cerveira, S. Bizarro et al., “POU1F1 is a novel fusion partner of NUP98 in acute myeloid leukemia with t(3;11)(p11;p15),” Molecular Cancer, vol. 12, no. 1, article 5, 2013.
[235]
G. Soler, S. Kaltenbach, S. Dobbelstein et al., “Identification of GSX2 and AF10 as NUP98 partner genes in myeloid malignancies,” Blood Cancer Journal, vol. 3, article e124, 2013.
[236]
J. C. Reader, J. S. Meekins, I. Gojo, and Y. Ning, “A novel NUP98-PHF23 fusion resulting from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia,” Leukemia, vol. 21, no. 4, pp. 842–844, 2007.
[237]
J. D. E. de Rooij, I. H. I. M. Hollink, S. T. C. J. M. Arentsen-Peters et al., “NUP98/JARID1A is a novel recurrent abnormality in pediatric acute megakaryoblastic leukemia with a distinct HOX gene expression pattern,” Leukemia, 2013.
[238]
L. J. C. M. van Zutven, E. ？nen, S. C. J. M. Velthuizen et al., “Identification of NUP98 abnormalities in acute leukemia: JARIDIA (12p13) as a new partner gene,” Genes Chromosomes and Cancer, vol. 45, no. 5, pp. 437–446, 2006.
[239]
I. H. I. M. Hollink, M. M. van den Heuvel-Eibrink, S. T. C. J. M. Arentsen-Peters et al., “NUP98/NSD1 characterizes a novel poor prognostic group in acute myeloid leukemia with a distinct HOX gene expression pattern,” Blood, vol. 118, no. 13, pp. 3645–3656, 2011.
[240]
R. J. Jaju, C. Fidler, O. A. Haas et al., “A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia,” Blood, vol. 98, no. 4, pp. 1264–1267, 2001.
[241]
R. La Starza, P. Gorello, R. Rosati et al., “Cryptic insertion producing two NUP98/NSD1 chimeric transcripts in adult refractory anemia with an excess of blasts,” Genes Chromosomes and Cancer, vol. 41, no. 4, pp. 395–399, 2004.
[242]
C. Panarello, C. Rosanda, and C. Morerio, “Cryptic translocation t(5;11)(q35;p15.5) with involvement of the NSD1 and NUP98 genes without 5q deletion in childhood acute myeloid leukemia,” Genes Chromosomes and Cancer, vol. 35, no. 3, pp. 277–281, 2002.
[243]
A. Petit, I. Radford, M.-C. Waill, S. Romana, and R. Berger, “NUP98-NSD1 fusion by insertion in acute myeloblastic leukemia,” Cancer Genetics and Cytogenetics, vol. 180, no. 1, pp. 43–46, 2008.
[244]
F. Thol, B. K？lking, I. H. I. Hollink et al., “Analysis of NUP98/NSD1 translocations in adult AML and MDS patients,” Leukemia, vol. 27, no. 3, pp. 750–754, 2013.
[245]
R. Rosati, R. La Starza, A. Veronese et al., “NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15),” Blood, vol. 99, no. 10, pp. 3857–3860, 2002.
[246]
T. Taketani, T. Taki, H. Nakamura, M. Taniwaki, J. Masuda, and Y. Hayashi, “NUP98-NSD3 fusion gene in radiation-associated myelodysplastic syndrome with t(8;11)(p11;p15) and expression pattern of NSD family genes,” Cancer Genetics and Cytogenetics, vol. 190, no. 2, pp. 108–112, 2009.
[247]
I. Panagopoulos, G. Kerndrup, N. Carlsen, B. Str？mbeck, M. Isaksson, and B. Johansson, “Fusion of NUP98 and the SET binding protein 1 (SETBP1) gene in a paediatric acute T cell lymphoblastic leukaemia with t(11;18)(p15;q12),” British Journal of Haematology, vol. 136, no. 2, pp. 294–296, 2007.
[248]
A. Petit, C. Ragu, V. Della-Valle et al., “NUP98-HMGB3: a novel oncogenic fusion,” Leukemia, vol. 24, no. 3, pp. 654–658, 2010.
[249]
H. G. Ahuja, C. A. Felix, and P. D. Aplan, “Potential role for DNA topoisomerase II poisons in the generation of t(11;20)(p15;q11) translocations,” Genes Chromosomes Cancer, vol. 29, pp. 96–105, 2000.
[250]
H. G. Ahuja, C. A. Felix, and P. D. Aplan, “The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion,” Blood, vol. 94, no. 9, pp. 3258–3261, 1999.
[251]
S. Chen, Y. Xue, Z. Chen, Y. Guo, Y. Wu, and J. Pan, “Generation of the NUP98-TOP1 fusion transcript by the t(11;20) (p15;q11) in a case of acute monocytic leukemia,” Cancer Genetics and Cytogenetics, vol. 140, no. 2, pp. 153–156, 2003.
[252]
S. Iwase, N. Akiyama, T. Sekikawa et al., “Both NUP98/TOP1 and TOP1/NUP98 transcripts are detected in a de novo AML with t(11;20)(p15;q11),” Genes Chromosomes and Cancer, vol. 38, no. 1, pp. 102–105, 2003.
[253]
I. Panagopoulos, T. Fioretos, M. Isaksson et al., “Expression of NUP98/TOP1, but not of TOP1/NUP98, in a treatment-related myelodysplastic syndrome with t(10;20;11)(q24;q11;p15),” Genes Chromosomes and Cancer, vol. 34, no. 2, pp. 249–254, 2002.
[254]
K. Nebral, H. H. Schmidt, O. A. Haas, and S. Strehl, “NUP98 is fused to topoisomerase (DNA) IIβ 180？kDa (TOP2B) in a patient with acute myeloid leukemia with a new t(3;11)(p24;p15),” Clinical Cancer Research, vol. 11, no. 18, pp. 6489–6494, 2005.
[255]
K. Nakao, M. Nishino, K. Takeuchi et al., “Fusion of the nucleoporin gene, NUP98, and the putative RNA helicase gene, DDX10, by inversion 11 (p15q22) chromosome translocation in a patient with etoposide-related myelodysplastic syndrome,” Internal Medicine, vol. 39, no. 5, pp. 412–415, 2000.
[256]
T. Ikeda, K. Ikeda, K. Sasaki, K. Kawakami, and J. Takahara, “The inv(11)(p15q22) chromosome translocation of therapy-related myelodysplasia with NUP98-DDX10 and DDX10-NUP98 fusion transcripts,” International Journal of Hematology, vol. 69, no. 3, pp. 160–164, 1999.
[257]
C. Morerio, M. Acquila, A. Rapella, E. Tassano, C. Rosanda, and C. Panarello, “Inversion (11)(p15q22) with NUP98-DDX10 fusion gene in pediatric acute myeloid leukemia,” Cancer Genetics and Cytogenetics, vol. 171, no. 2, pp. 122–125, 2006.
[258]
M. Yamamoto, K. Kakihana, T. Kurosu, N. Murakami, and O. Miura, “Clonal evolution with inv(11)(p15q22) and NUP98/DDX10 fusion gene in imatinib-resistant chronic myelogenous leukemia,” Cancer Genetics and Cytogenetics, vol. 157, no. 2, pp. 104–108, 2005.
[259]
G. Cimino, T. Sprovieri, M. C. Rapanotti, R. Foà, C. Mecucci, and F. Mandelli, “Molecular evaluation of the NUP98/RAP1GDS1 gene frequency in adults with T-acute lymphoblastic leukemia,” Haematologica, vol. 86, no. 4, pp. 436–437, 2001.
[260]
D. J. Hussey, M. Nicola, S. Moore, G. B. Peters, and A. Dobrovic, “The (4;11)(q21;p15) translocation fuses the NUP98 and RAP1GDS1 genes and is recurrent in T-cell acute lymphocytic leukemia,” Blood, vol. 94, no. 6, pp. 2072–2079, 1999.
[261]
C. Mecucci, R. La Starza, M. Negrini et al., “t(4;11)(q21;p15) translocation involving NUP98 and RAP1GDS1 genes: characterization of a new subset of T acute lymphoblastic leukaemia,” British Journal of Haematology, vol. 109, no. 4, pp. 788–793, 2000.
[262]
I. Lahortiga, J. L. Vizmanos, X. Agirre et al., “NUP98 is fused to Adducin 3 in a patient with T-cell acute lymphoblastic leukemia and myeloid markers, with a new translocation t(10;11)(q25;p15),” Cancer Research, vol. 63, no. 12, pp. 3079–3083, 2003.
[263]
M. Ishikawa, F. Yagasaki, D. Okamura et al., “A novel gene, ANKRD28 on 3p25, is fused with NUP98 on 11p15 in a cryptic 3-way translocation of t(3;5;11)(p25;q35;p15) in an adult patient with myelodysplastic syndrome/acute myelogenous leukemia,” International Journal of Hematology, vol. 86, no. 3, pp. 238–245, 2007.
[264]
H. G. Ahuja, J. Hong, P. D. Aplan, L. Tcheurekdjian, S. J. Forman, and M. L. Slovak, “t(9;11)(p22;p15) in acute myeloid leukemia results in a fusion between NUP98 and the gene encoding transcriptional coactivators p52 and p75-lens epithelium-derived growth factor (LEDGF),” Cancer Research, vol. 60, no. 22, pp. 6227–6229, 2000.
[265]
F. H. Grand, P. Koduru, N. C. P. Cross, and S. L. Allen, “NUP98-LEDGF fusion and t(9;11) in transformed chronic myeloid leukemia,” Leukemia Research, vol. 29, no. 12, pp. 1469–1472, 2005.
[266]
D. J. Hussey, S. Moore, M. Nicola, and A. Dobrovic, “Fusion of the NUP98 gene with the LEDGF/p52 gene defines a recurrent acute myeloid leukemia translocation,” BMC Genetics, vol. 2, article 20, 2001.
[267]
C. Morerio, M. Acquila, C. Rosanda et al., “t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia,” Leukemia Research, vol. 29, no. 4, pp. 467–470, 2005.
[268]
Q. Pan, Y.-J. Zhu, B.-W. Gu et al., “A new fusion gene NUP98-IQCG identified in an acute T-lymphoid/myeloid leukemia with a t(3;11)(q29q13;p15)del(3)(q29) translocation,” Oncogene, vol. 27, no. 24, pp. 3414–3423, 2008.
[269]
E. Such, J. Cervera, A. Valencia et al., “A novel NUP98/RARG gene fusion in acute myeloid leukemia resembling acute promyelocytic leukemia,” Blood, vol. 117, no. 1, pp. 242–245, 2011.
[270]
A. Petit, C. Ragu, G. Soler et al., “Functional analysis of the NUP98-CCDC28A fusion protein,” Haematologica, vol. 97, no. 3, pp. 379–387, 2012.
[271]
S. Tosi, E. Ballabio, A. Teigler-Schlegel, J. Boultwood, J. Bruch, and J. Harbott, “Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia,” Genes Chromosomes and Cancer, vol. 44, no. 3, pp. 225–232, 2005.
[272]
P. Gorello, L. Brandimarte, R. La Starza et al., “t(3;11)(q12;p15)/NUP98-LOC348801 fusion transcript in acute myeloid leukemia,” Haematologica, vol. 93, no. 9, pp. 1398–1401, 2008.
[273]
S. Saito, K. Nouno, R. Shimizu, M. Yamamoto, and K. Nagata, “Impairment of erythroid and megakaryocytic differentiation by a leukemia-associated and t(9;9)-derived fusion gene product, SET/TAF-Iβ-CAN/ Nup214,” Journal of Cellular Physiology, vol. 214, no. 2, pp. 322–333, 2008.
[274]
M. von Lindern, S. van Baal, J. Wiegant, A. Raap, A. Hagemeijer, and G. Grosveld, “can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene,” Molecular and Cellular Biology, vol. 12, no. 8, pp. 3346–3355, 1992.
[275]
M. von Lindern, M. Fornerod, N. Soekarman et al., “Translocation t(6;9) in acute non-lymphocytic leukaemia results in the formation of a DEK-CAN fusion gene,” Bailliere's Clinical Haematology, vol. 5, no. 4, pp. 857–879, 1992.
[276]
W. Deenik, H. B. Beverloo, S. C. P. A. M. van der Poel-van de Luytgaarde et al., “Rapid complete cytogenetic remission after upfront dasatinib monotherapy in a patient with a NUP214-ABL1-positive T-cell acute lymphoblastic leukemia,” Leukemia, vol. 23, no. 3, pp. 627–629, 2009.
[277]
N. Kawamata, L. Zhang, S. Ogawa et al., “Double minute chromosomes containing MYB gene and NUP214-ABL1 fusion gene in T-cell leukemia detected by single nucleotide polymorphism DNA microarray and fluorescence in situ hybridization,” Leukemia Research, vol. 33, no. 4, pp. 569–571, 2009.
[278]
A. Quintás-Cardama, W. Tong, T. Manshouri et al., “Activity of tyrosine kinase inhibitors against human NUP214-ABL1-positive T cell malignancies,” Leukemia, vol. 22, no. 6, pp. 1117–1124, 2008.
