ArticleJournal of virology2002
The late-domain-containing protein p6 is the predominant phosphoprotein of human immunodeficiency virus type 1 particles.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- Trial
- Calcium and phosphorylation coordination is a novel mechanism that stabilises protein-complexes during HIV assembly.Journal of biomedical science · 2026Article
- The HIV-1 gag p6: a promising target for therapeutic intervention.Retrovirology · 2024Review
- The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity.International journal of molecular sciences · 2022Review
- ALV-miRNA-p19-01 Promotes Viral Replication via Targeting Dual Specificity Phosphatase 6.Viruses · 2022Article
- Subtype-specific differences in Gag-protease replication capacity of HIV-1 isolates from East and West Africa.Retrovirology · 2021Article
- Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role.International journal of molecular sciences · 2021Review
- Proteomic Approaches to Study SARS-CoV-2 Biology and COVID-19 Pathology.Journal of proteome research · 2021Article
- HIV-1Viruses · 2021Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Modulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesis.Nucleic acids research · 2018Article
- Glutamic Acid Residues in HIV-1 p6 Regulate Virus Budding and Membrane Association of Gag.Viruses · 2016Article
- Re-visiting the functional Relevance of the highly conserved Serine 40 Residue within HIV-1 p6(Gag).Retrovirology · 2014Article
- Article
- The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions.Retrovirology · 2014Article
- New findings in cleavage sites variability across groups, subtypes and recombinants of human immunodeficiency virus type 1.PloS one · 2014Article
- Comprehensive mutational analysis reveals p6Gag phosphorylation to be dispensable for HIV-1 morphogenesis and replication.Journal of virology · 2013Article
- The viral transactivator HBx protein exhibits a high potential for regulation via phosphorylation through an evolutionarily conserved mechanism.Infectious agents and cancer · 2012Article
- Phosphorylation events during viral infections provide potential therapeutic targets.Reviews in medical virology · 2012Article
- Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.Cellular and molecular life sciences : CMLS · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gag-derived protein p6 of human immunodeficiency virus type 1 (HIV-1) plays a crucial role in the release of virions from the membranes of infected cells. It is presumed that p6 and functionally related proteins from other viruses act as adapters, recruiting cellular factors to the budding site. This interaction is mediated by so-called late domains within the viral proteins. Previous studies had suggested that virus release from the plasma membrane shares elements with the cellular endocytosis machinery. Since protein phosphorylation is known to be a regulatory mechanism in these processes, we have investigated the phosphorylation of HIV-1 structural proteins. Here we show that p6 is the major phosphoprotein of HIV-1 particles. After metabolic labeling of infected cells with [ortho-32P]phosphate, we found that phosphorylated p6 from infected cells and from virus particles consisted of several forms, suggesting differential phosphorylation at multiple sites. Apparently, phosphorylation occurred shortly before or after the release of p6 from Gag and involved only a minor fraction of the total virion-associated p6 molecules. Phosphoamino acid analysis indicated phosphorylation at Ser and Thr, as well as a trace of Tyr phosphorylation, supporting the conclusion that multiple phosphorylation events do occur. In vitro experiments using purified virus revealed that endogenous or exogenously added p6 was efficiently phosphorylated by virion-associated cellular kinase(s). Inhibition experiments suggested that a cyclin-dependent kinase or a related kinase, most likely ERK2, was involved in p6 phosphorylation by virion-associated enzymes.
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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.