ArticleJournal of virology2009
A basic patch on alpha-adaptin is required for binding of human immunodeficiency virus type 1 Nef and cooperative assembly of a CD4-Nef-AP-2 complex.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
40 citing papers in PubMed, 51 citations in OpenAlex.
- HIV-1 Nef Uses a Conserved Pocket to Recruit the N-Terminal Cytoplasmic Tail of Serinc3.Viruses · 2025Article
- Viral Interactions with Adaptor-Protein Complexes: A Ubiquitous Trait among Viral Species.International journal of molecular sciences · 2021Review
- Nef Obtained from Individuals with HIV-1 Vary in Their Ability to Antagonize SERINC3- and SERINC5-Mediated HIV-1 Restriction.Viruses · 2021Article
- Identification of recombinant Fabs for structural and functional characterization of HIV-host factor complexes.PloS one · 2021Article
- Hijacking of endocytosis by HIV-1 Nef is becoming crystal clear.Nature structural & molecular biology · 2020Article
- Structural basis of CD4 downregulation by HIV-1 Nef.Nature structural & molecular biology · 2020Article
- Two Functional Variants of AP-1 Complexes Composed of either γ2 or γ1 Subunits Are Independently Required for Major Histocompatibility Complex Class I Downregulation by HIV-1 Nef.Journal of virology · 2020Article
- How HIV Nef Proteins Hijack Membrane Traffic To Promote Infection.Journal of virology · 2019Review
- TIM-mediated inhibition of HIV-1 release is antagonized by Nef but potentiated by SERINC proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Exosome Biogenesis and Biological Function in Response to Viral Infections.The open virology journal · 2018Review
- Endocytic activity of HIV-1 Vpu: Phosphoserine-dependent interactions with clathrin adaptors.Traffic (Copenhagen, Denmark) · 2017Article
- Cell-based Fluorescence Complementation Reveals a Role for HIV-1 Nef Protein Dimerization in AP-2 Adaptor Recruitment and CD4 Co-receptor Down-regulation.The Journal of biological chemistry · 2017Article
- HIV-1 Env and Nef Cooperatively Contribute to Plasmacytoid Dendritic Cell Activation via CD4-Dependent Mechanisms.Journal of virology · 2015Article
- The ap-2 clathrin adaptor mediates endocytosis of an inhibitory killer cell Ig-like receptor in human NK cells.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Interaction of HIV-1 Nef protein with the host protein Alix promotes lysosomal targeting of CD4 receptor.The Journal of biological chemistry · 2014Article
- Article
- HIV-1 Nef down-modulates C-C and C-X-C chemokine receptors via ubiquitin and ubiquitin-independent mechanism.PloS one · 2014Article
- Nef neutralizes the ability of exosomes from CD4+ T cells to act as decoys during HIV-1 infection.PloS one · 2014Article
- Cargo recognition in clathrin-mediated endocytosis.Cold Spring Harbor perspectives in biology · 2013Review
- Identification of a novel binding site between HIV type 1 Nef C-terminal flexible loop and AP2 required for Nef-mediated CD4 downregulation.AIDS research and human retroviruses · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
A critical function of the human immunodeficiency virus type 1 Nef protein is the downregulation of CD4 from the surfaces of infected cells. Nef is believed to act by linking the cytosolic tail of CD4 to the endocytic machinery, thereby increasing the rate of CD4 internalization. In support of this model, weak binary interactions between CD4, Nef, and the endocytic adaptor complex, AP-2, have been reported. In particular, dileucine and diacidic motifs in the C-terminal flexible loop of Nef have been shown to mediate binding to a combination of the alpha and sigma2 subunits of AP-2. Here, we report the identification of a potential binding site for the Nef diacidic motif on alpha-adaptin. This site comprises two basic residues, lysine-297 and arginine-340, on the alpha-adaptin trunk domain. The mutation of these residues specifically inhibits the ability of Nef to bind AP-2 and downregulate CD4. We also present evidence that the diacidic motif on Nef and the basic patch on alpha-adaptin are both required for the cooperative assembly of a CD4-Nef-AP-2 complex. This cooperativity explains how Nef is able to efficiently downregulate CD4 despite weak binary interactions between components of the tripartite complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.