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PROLINE-RICH (PXXP) MOTIFS IN HIV-1 NEF BIND TO SH3 DOMAINS OF A SUBSET OF SRC KINASES AND ARE REQUIRED FOR THE ENHANCED GROWTH OF NEF(+) VIRUSES BUT NOT FOR DOWN-REGULATION OF CD4
Author(s): SAKSELA K, CHENG GH, BALTIMORE D
Source: EMBO JOURNAL    Volume: 14    Issue: 3    Pages: 484-491    Published: FEB 1 1995  
Times Cited: 380     References: 42     
Abstract: Human immunodeficiency virus (HIV) and simian immunodeficiency virus Nef proteins contain a conserved motif with the minimal consensus (PxxP) site for Src homology region 3 (SH3)-mediated protein-protein interactions. Nef PxxP motifs show specific binding to biotinylated SH3 domains of Hck and Lyn, but not to those of other tested Src family kinases or less related proteins. A unique cooperative role of a distant proline is also observed. Endogenous Hck of monocytic U937 cells can be specifically precipitated by matrix-bound HIV-1 Nef, but not by mutant protein lacking PxxP. Intact Nef PxxP motifs are dispensable for Nef-induced CD4 down-regulation, but are required for the higher in vitro replicative potential of Nef(+) viruses. Thus, CD4 down-regulation and promotion of viral growth are two distinct functions of Nef, and the latter is mediated via SH3 binding.
Document Type: Article
Language: English
Reprint Address: SAKSELA, K (reprint author), ROCKEFELLER UNIV, 1230 YORK AVE, NEW YORK, NY 10021 USA
Addresses:
1. MIT, CAMBRIDGE, MA 02139 USA
Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: QF718
ISSN: 0261-4189
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