ArticleJournal of virology2006
A hydrophobic binding surface on the human immunodeficiency virus type 1 Nef core is critical for association with p21-activated kinase 2.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- HIV-1 Balances the Fitness Costs and Benefits of Disrupting the Host Cell Actin Cytoskeleton Early after Mucosal Transmission.Cell host & microbe · 2019Article
- Intrinsic properties and plasma membrane trafficking route of Src family kinase SH4 domains sensitive to retargeting by HIV-1 Nef.The Journal of biological chemistry · 2018Article
- Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource.Database : the journal of biological databases and curation · 2016Article
- Article
- A Conserved GPG-Motif in the HIV-1 Nef Core Is Required for Principal Nef-Activities.PloS one · 2015Article
- Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody.Retrovirology · 2014Article
- The activity of Nef on HIV-1 infectivity.Frontiers in microbiology · 2014Review
- Primate lentiviral Nef proteins deregulate T-cell development by multiple mechanisms.Retrovirology · 2013Article
- HIV-1 Nef and T-cell activation: a history of contradictions.Future virology · 2013Article
- Article
- HIV-1 Nef interferes with T-lymphocyte circulation through confined environments in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Proteomic analysis of HIV-1 Nef cellular binding partners reveals a role for exocyst complex proteins in mediating enhancement of intercellular nanotube formation.Retrovirology · 2012Article
- Optimization of magnetic nanoparticle-assisted lentiviral gene transfer.Pharmaceutical research · 2012Article
- Magnetically enhanced nucleic acid delivery. Ten years of magnetofection-progress and prospects.Advanced drug delivery reviews · 2011Review
- Nef-mediated enhancement of cellular activation and human immunodeficiency virus type 1 replication in primary T cells is dependent on association with p21-activated kinase 2.Retrovirology · 2011Article
- Mechanisms of HIV-1 Nef function and intracellular signaling.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011Review
- Review
- CD4 and MHC class 1 down-modulation activities of nef alleles from brain- and lymphoid tissue-derived primary HIV-1 isolates.Journal of neurovirology · 2011Article
- Trans-cellular introduction of HIV-1 protein Nef induces pathogenic response in Caenorhabditis elegans.PloS one · 2010Article
- Lentiviral Nef proteins utilize PAK2-mediated deregulation of cofilin as a general strategy to interfere with actin remodeling.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The interaction of human immunodeficiency virus type 1 (HIV-1) Nef with p21-activated kinase 2 (Pak2) has been proposed to play an important role in T-cell activation and disease progression during viral infection. However, the mechanism by which Nef activates Pak2 is poorly understood. Mutations in most Nef motifs previously reported to be required for Pak2 activation (G2, PxxP72, and RR105) also affect other Nef functions, such as CD4 or major histocompatibility complex class I (MHC-I) downregulation. To better understand Nef interactions with Pak2, we performed mutational analysis of three primary HIV-1 Nef clones that exhibited similar capacities for downregulation of CD4 and MHC-I but variable abilities to associate with activated Pak2. Our results demonstrate that Nef amino acids at positions 85, 89, 187, 188, and 191 (L, H, S, R, and F in the clade B consensus, respectively) are critical for Pak2 association. Mutation of these Nef residues dramatically altered association with Pak2 without affecting Nef expression levels or CD4 and MHC-I downregulation. Furthermore, compensation occurred at positions 89 and 191 when both amino acids were substituted. Since residues 85, 89, 187, 188, and 191 cluster on the surface of the Nef core domain in a region distinct from the dimerization and SH3-binding domains, we propose that these Nef residues form part of a unique binding surface specifically involved in association with Pak2. This binding surface includes exposed and recessed hydrophobic residues and may participate in an as-yet-unidentified protein-protein interaction to facilitate Pak2 activation.
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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.