Abstract
The HIV-1 Nef-mediated downregulation of cell surface MHC-I molecules to the trans-Golgi network (TGN) enables HIV-1 to escape immune surveillance. However, the cellular pathway used by Nef to downregulate MHC-I is unknown. Here, we show that Nef and PACS-1 combine to usurp the ARF6 endocytic pathway by a PI3K-dependent process and downregulate cell surface MHC-I to the TGN. This mechanism requires the hierarchical actions of three Nef motifs-the acidic cluster 62EEEE(65), the SH3 domain binding site 72PXXP(75), and M(20)-in controlling PACS-1-dependent sorting to the TGN, ARF6 activation, and sequestering internalized MHC-I to the TGN, respectively. These data provide new insights into the cellular basis of HIV-1 immunoevasion.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ADP-Ribosylation Factor 6
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ADP-Ribosylation Factors / metabolism*
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Amino Acid Motifs
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Binding Sites
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Biological Transport
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CD4 Antigens / biosynthesis
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Carrier Proteins / metabolism*
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Cell Line
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Down-Regulation*
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Endocytosis*
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Gene Expression Regulation*
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Gene Products, nef / metabolism
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Gene Products, nef / physiology*
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Genes, MHC Class I / genetics*
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HeLa Cells
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Humans
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Kinetics
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Microscopy, Fluorescence
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Models, Biological
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Phosphatidylinositol 3-Kinases / metabolism*
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Protein Structure, Tertiary
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Temperature
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Time Factors
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Tumor Cells, Cultured
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Vesicular Transport Proteins
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src Homology Domains
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trans-Golgi Network / metabolism
Substances
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ADP-Ribosylation Factor 6
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CD4 Antigens
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Carrier Proteins
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Gene Products, nef
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PACS1 protein, human
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Vesicular Transport Proteins
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ADP-Ribosylation Factors
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ARF6 protein, human