ArticleProtein science : a publication of the Protein Society2005
Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Review
- Protein lipidation in health and disease: molecular basis, physiological function and pathological implication.Signal transduction and targeted therapy · 2024Review
- HIV-1 Virus Interactions With Host Proteins: Interaction of the N-terminal Domain of the HIV-1 Capsid Protein With Human Calmodulin.Natural product communications · 2019Article
- Calmodulin and PI(3,4,5)P₃ cooperatively bind to the Itk pleckstrin homology domain to promote efficient calcium signaling and IL-17A production.Science signaling · 2014Article
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- HIV-1 Nef in macrophage-mediated disease pathogenesis.International reviews of immunology · 2012Review
- Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release.Biophysical journal · 2012Article
- Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Frontiers in microbiology · 2012Article
- NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2011Article
- Breaking down the barrier: the effects of HIV-1 on the blood-brain barrier.Brain research · 2011Review
- Article
- Sequence- and interactome-based prediction of viral protein hotspots targeting host proteins: a case study for HIV Nef.PloS one · 2011Article
- Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.The Journal of biological chemistry · 2010Article
- Calcium-dependent association of calmodulin with the rubella virus nonstructural protease domain.The Journal of biological chemistry · 2010Article
- N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010Review
- HIV-1 Nef dimerization is required for Nef-mediated receptor downregulation and viral replication.Journal of molecular biology · 2009Article
- Viral calciomics: interplays between Ca2+ and virus.Cell calcium · 2009Review
- Prediction of interactions between HIV-1 and human proteins by information integration.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2009Article
- Ortholog-based protein-protein interaction prediction and its application to inter-species interactions.BMC bioinformatics · 2008Article
- Altered gene expression in asymptomatic SHIV-infected rhesus macaques (Macacca mulatta).Virology journal · 2006Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human immunodeficiency virus Nef is a myristoylated protein expressed early in infection by HIV. In addition to the well known down-regulation of the cell surface receptors CD4 and MHCI, Nef is able to alter T-cell signaling pathways. The ability to alter the cellular signaling pathways suggests that Nef can associate with signaling proteins. In the present report, we show that Nef can interact with calmodulin, the major intracellular receptor for calcium. Coimmunoprecipitation analyses with lysates from the NIH3T3 cell line constitutively expressing the native HIV-1 Nef protein revealed the presence of a stable Nef-calmodulin complex. When lysates from NIH3T3 cells were incubated with calmodulin-agarose beads in the presence of CaCl(2) or EGTA, calcium ion drastically enhanced the interaction between Nef and calmodulin, suggesting that the binding is under the influence of Ca(2+) signaling. Glutathione S-transferase-Nef fusion protein bound directly to calmodulin with high affinity. Using synthetic peptides based on the N-terminal sequence of Nef, we determined that within a 20-amino-acid N-terminal basic domain was sufficient for calmodulin binding. Furthermore, the myristoylated peptide bound to calmodulin with higher affinity than nonmyris-toylated form. Thus, the N-terminal myristoylation domain of Nef plays an important role in interacting with calmodulin. This domain is highly conserved in several HIV-1 Nef variants and resembles the N-terminal domain of NAP-22/CAP23, a myristoylated calmodulin-binder. These results for the interaction between HIV Nef and calmodulin in the cells suggested that the Nef might interfere with intracellular Ca(2+) signaling through calmodulin-mediated interactions in infected cells.
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