%0 Journal Article
%T Proteins recruited by SH3 domains of Ruk/CIN85 adaptor identified by LC-MS/MS
%A Serhiy Havrylov
%A Yuriy Rzhepetskyy
%A Agata Malinowska
%A Lyudmyla Drobot
%A Maria Redowicz
%J Proteome Science
%D 2009
%I BioMed Central
%R 10.1186/1477-5956-7-21
%X In the present study we employed a LC-MS/MS-based experimental pipeline to identify a considerable number (over 100) of proteins recruited by the SH3 domains of Ruk/CIN85 in vitro. Most of these identifications are novel Ruk/CIN85 interaction candidates. The identified proteins have diverse molecular architectures and can interact with other proteins, as well as with lipids and nucleic acids. Some of the identified proteins possess enzymatic activities. Functional profiling analyses and literature mining demonstrate that many of the proteins recruited by the SH3 domains of Ruk/CIN85 identified in this work were involved in the regulation of membranes and cytoskeletal structures necessary for vesicle-mediated transport and cancer cell invasiveness. Several groups of the proteins were also associated with few other cellular processes not previously related to Ruk/CIN85, most prominently with cell division.Obtained data support the notion that Ruk/CIN85 regulates vesicle-mediated transport and cancer cell invasiveness through the assembly of multimeric protein complexes governing coordinated remodelling of membranes and underlying cytoskeletal structures, and imply its important roles in formation of coated vesicles and biogenesis of invadopodia. In addition, this study points to potential involvement of Ruk/CIN85 in other cellular processes, chiefly in cell division.Ruk/CIN85 is a mammalian adaptor molecule with three SH3 domains. In addition to the SH3 domains located at the N-terminal part of the protein, Ruk/CIN85 contains other protein interaction modules, namely proline-rich sequences and a coiled-coil region (see Additional file 1). By sequence homology and domain architecture Ruk/CIN85 is closely related to another mammalian adaptor molecule CD2AP/CMS [1]. Due to the similarity of their SH3 domains, Ruk/CIN85 and CD2AP/CMS recognise the same atypical proline-arginine PX(P/A)XXR motif and reveal partially overlapping specificity towards interaction partners [2,3
%U http://www.proteomesci.com/content/7/1/21