%0 Journal Article
%T An MHC-I Cytoplasmic Domain/HIV-1 Nef Fusion Protein Binds Directly to the ¦Ì Subunit of the AP-1 Endosomal Coat Complex
%A Rajendra Kumar Singh
%A David Lau
%A Colleen M. Noviello
%A Partho Ghosh
%A John C. Guatelli
%J PLOS ONE
%D 2012
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0008364
%X The down-regulation of the major histocompatibility complex class I (MHC-I) from the surface of infected cells by the Nef proteins of primate immunodeficiency viruses likely contributes to pathogenesis by providing evasion of cell-mediated immunity. HIV-1 Nef-induced down-regulation involves endosomal trafficking and a cooperative interaction between the cytoplasmic domain (CD) of MHC-I, Nef, and the clathrin adaptor protein complex-1 (AP-1). The CD of MHC-I contains a key tyrosine within the sequence YSQA that is required for down-regulation by Nef, but this sequence does not conform to the canonical AP-binding tyrosine-based motif Yxx¦Õ, which mediates binding to the medium (¦Ì) subunits of AP complexes. We previously proposed that Nef allows the MHC-I CD to bind the ¦Ì subunit of AP-1 (¦Ì1) as if it contained a Yxx¦Õmotif.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008364