000053708 001__ 53708
000053708 005__ 20180317095221.0
000053708 022__ $$a0261-4189
000053708 0247_ $$2doi$$a10.1093/emboj/17.9.2472
000053708 037__ $$aARTICLE
000053708 245__ $$aMechanism of Nef-induced CD4 endocytosis: Nef connects CD4 with the mu chain of adaptor complexes
000053708 269__ $$a1998
000053708 260__ $$c1998
000053708 336__ $$aJournal Articles
000053708 520__ $$aThe Nef protein of primate lentiviruses down-regulates the cell surface expression of CD4 and probably MHC I by connecting these receptors with the endocytic machinery. Here, we reveal that Nef interacts with the mu chains of adaptor complexes, key components of clathrin-coated pits. For human immunodeficiency virus type 2 (HIV-2) and simian immunodeficiency virus (SIV) Nef, this interaction occurs via tyrosine-based motifs reminiscent of endocytosis signals. Mutating these motifs prevents the binding of SIV Nef to the mu chain of plasma membrane adaptor complexes, abrogates its ability to induce CD4 internalization, suppresses the accelerated endocytosis of a chimeric integral membrane protein harboring Nef as its cytoplasmic domain and confers a dominant-negative phenotype to the viral protein. Taken together, these data identify mu adaptins as downstream mediators of the down-modulation of CD4, and possibly MHC I, by Nef.
000053708 700__ $$aPiguet, V
000053708 700__ $$aChen, Y L
000053708 700__ $$aMangasarian, A
000053708 700__ $$aFoti, M
000053708 700__ $$aCarpentier, J L
000053708 700__ $$0240083$$aTrono, Didier$$g167919
000053708 773__ $$j17$$k9$$q2472-81$$tEMBO J
000053708 909CO $$ooai:infoscience.tind.io:53708$$particle$$pSV
000053708 909C0 $$0252036$$pLVG$$xU11172
000053708 937__ $$aLVG-ARTICLE-1998-003
000053708 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000053708 970__ $$a9564030/LVG
000053708 980__ $$aARTICLE