Abstract
The human immunodeficiency virus type 1 (HIV-1) Vpu protein interacts with CD4 within the endoplasmic reticula of infected cells and targets CD4 for degradation through interaction with beta-TrCP1. Mammals possess a homologue of beta-TrCP1, HOS, which is also named beta-TrCP2. We show by coimmunoprecipitation experiments that beta-TrCP2 binds Vpu and is able to induce CD4 down-modulation as efficiently as beta-TrCP1. In two different cell lines, HeLa CD4+ and Jurkat, Vpu-mediated CD4 down-modulation could not be reversed through the individual silencing of endogenous beta-TrCP1 or beta-TrCP2 but instead required the two genes to be silenced simultaneously.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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CD4 Antigens / biosynthesis*
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Down-Regulation
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Gene Expression Regulation, Viral
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Gene Silencing / physiology*
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HIV-1 / genetics
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HIV-1 / immunology*
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HeLa Cells
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Human Immunodeficiency Virus Proteins
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Humans
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T-Lymphocytes / immunology*
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T-Lymphocytes / virology
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Ubiquitin-Protein Ligases / deficiency
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Ubiquitin-Protein Ligases / genetics*
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Viral Regulatory and Accessory Proteins / physiology*
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beta-Transducin Repeat-Containing Proteins / deficiency
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beta-Transducin Repeat-Containing Proteins / genetics*
Substances
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BTRC protein, human
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CD4 Antigens
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FBXW11 protein, human
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Human Immunodeficiency Virus Proteins
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Viral Regulatory and Accessory Proteins
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beta-Transducin Repeat-Containing Proteins
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vpu protein, Human immunodeficiency virus 1
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Ubiquitin-Protein Ligases