ArticleThe Journal of biological chemistry2010
Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 41 citations in OpenAlex.
- Quantitative and amino acid sequence analysis of soluble HIV-1 Vpu and calmodulin interactions.Protein science : a publication of the Protein Society · 2026Article
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.Biomolecules · 2021Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Differences and commonalities in plasma membrane recruitment of the two morphogenetically distinct retroviruses HIV-1 and MMTV.The Journal of biological chemistry · 2020Article
- Review
- 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
- KRAS Prenylation Is Required for Bivalent Binding with Calmodulin in a Nucleotide-Independent Manner.Biophysical journal · 2019Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- The Interplay between Calmodulin and Membrane Interactions with the Pleckstrin Homology Domain of Akt.The Journal of biological chemistry · 2017Article
- Article
- Structural and Biophysical Characterization of the Interactions between Calmodulin and the Pleckstrin Homology Domain of Akt.The Journal of biological chemistry · 2015Article
- Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.Frontiers in microbiology · 2015Article
- Roles played by acidic lipids in HIV-1 Gag membrane binding.Virus research · 2014Review
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- Tsg101 regulates PI(4,5)P2/Ca(2+) signaling for HIV-1 Gag assembly.Frontiers in microbiology · 2014Article
- Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages.Frontiers in microbiology · 2014Review
- Structural and biophysical characterization of the interactions between the death domain of Fas receptor and calmodulin.The Journal of biological chemistry · 2013Article
- The frantic play of the concealed HIV envelope cytoplasmic tail.Retrovirology · 2013Review
- Trio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Steady progress has been made in defining both the viral and cellular determinants of retroviral assembly and release. Although it is widely accepted that targeting of the Gag polypeptide to the plasma membrane is critical for proper assembly of HIV-1, the intracellular interactions and trafficking of Gag to its assembly sites in the infected cell are poorly understood. HIV-1 Gag was shown to interact and co-localize with calmodulin (CaM), a ubiquitous and highly conserved Ca(2+)-binding protein expressed in all eukaryotic cells, and is implicated in a variety of cellular functions. Binding of HIV-1 Gag to CaM is dependent on calcium and is mediated by the N-terminally myristoylated matrix (myr(+)MA) domain. Herein, we demonstrate that CaM binds to myr(+)MA with a dissociation constant (K(d)) of ∼2 μm and 1:1 stoichiometry. Strikingly, our data revealed that CaM binding to MA induces the extrusion of the myr group. However, in contrast to all known examples of CaM-binding myristoylated proteins, our data show that the myr group is exposed to solvent and not involved in CaM binding. The interactions between CaM and myr(+)MA are endothermic and entropically driven, suggesting that hydrophobic contacts are critical for binding. As revealed by NMR data, both CaM and MA appear to engage substantial regions and/or undergo significant conformational changes upon binding. We believe that our findings will provide new insights on how Gag may interact with CaM during the HIV replication cycle.
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