ArticleJournal of virology2008
Human immunodeficiency virus type 1 Nef recruits the guanine exchange factor Vav1 via an unexpected interface into plasma membrane microdomains for association with p21-activated kinase 2 activity.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- HIV Nef amplifies mechanical heterogeneity to promote immune evasion.bioRxiv : the preprint server for biology · 2025Article
- The Role of Exogenous microRNAs on Human Health: The Plant-Human Trans-Kingdom Hypothesis.Nutrients · 2024Review
- Article
- Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage.PLoS pathogens · 2021Article
- Plant microRNAs fromFrontiers in pharmacology · 2020Article
- Coordinating Cytoskeleton and Molecular Traffic in T Cell Migration, Activation, and Effector Functions.Frontiers in cell and developmental biology · 2020Review
- Multifunctional Roles of the N-Terminal Region of HIV-1Journal of virology · 2019Article
- HIV-Nef Protein Persists in the Lungs of Aviremic Patients with HIV and Induces Endothelial Cell Death.American journal of respiratory cell and molecular biology · 2019Article
- Implications of HIV-1 Nef for "Shock and Kill" Strategies to Eliminate Latent Viral Reservoirs.Viruses · 2018Review
- All-Round Manipulation of the Actin Cytoskeleton by HIV.Viruses · 2018Review
- Subverting Host Cell P21-Activated Kinase: A Case of Convergent Evolution across Pathogens.Pathogens (Basel, Switzerland) · 2017Review
- The Antagonism of HIV-1 Nef to SERINC5 Particle Infectivity Restriction Involves the Counteraction of Virion-Associated Pools of the Restriction Factor.Journal of virology · 2016Article
- Article
- Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells.Journal of virology · 2015Article
- In vivo analysis of Nef's role in HIV-1 replication, systemic T cell activation and CD4(+) T cell loss.Retrovirology · 2015Article
- HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors, including tetraspanins.Journal of virology · 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
- 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
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alterations of T-cell receptor signaling by human immunodeficiency virus type 1 (HIV-1) Nef involve its association with a highly active subpopulation of p21-activated kinase 2 (PAK2) within a dynamic signalosome assembled in detergent-insoluble membrane microdomains. Nef-PAK2 complexes contain the GTPases Rac and Cdc42 as well as a factor providing guanine nucleotide exchange factor (GEF) activity for Rac/Cdc42. However, the identity of this GEF has remained controversial. Previous studies suggested the association of Nef with at least three independent GEFs, Vav, DOCK2/ELMO1, and betaPix. Here we used a broad panel of approaches to address which of these GEFs is involved in the functional interaction of Nef with PAK2 activity. Biochemical fractionation and confocal microscopy revealed that Nef recruits Vav1, but not DOCK2/ELMO1 or betaPix, to membrane microdomains. Transient RNAi knockdown, analysis of cell lines defective for expression of Vav1 or DOCK2 as well as use of a betaPix binding-deficient PAK2 variant confirmed a role for Vav1 but not DOCK2 or betaPix in Nef's association with PAK2 activity. Nef-mediated microdomain recruitment of Vav1 occurred independently of the Src homology 3 domain binding PxxP motif, which is known to connect Nef to many cellular signaling processes. Instead, a recently described protein interaction surface surrounding Nef residue F195 was identified as critical for Nef-mediated raft recruitment of Vav1. These results identify Vav1 as a relevant component of the Nef-PAK2 signalosome and provide a molecular basis for the role of F195 in formation of a catalytically active Nef-PAK2 complex.
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