ArticleJournal of virology2011
The cellular protein lyric interacts with HIV-1 Gag.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Two Peas in a Pod: Retroviral RNA Dimers Organize Gag-RNA Nanoclusters with Novel Biophysical Properties.International journal of molecular sciences · 2025Article
- Two peas in a pod: retroviral RNA dimers organize Gag-RNA nanoclusters with novel biophysical properties.bioRxiv : the preprint server for biology · 2025Article
- Article
- Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome.Retrovirology · 2024Article
- Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome.bioRxiv : the preprint server for biology · 2024Article
- Review
- Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.Biomolecules · 2021Article
- HIV-1 Gag Forms Ribonucleoprotein Complexes with Unspliced Viral RNA at Transcription Sites.Viruses · 2020Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Elucidating the in vivo interactome of HIV-1 RNA by hybridization capture and mass spectrometry.Scientific reports · 2017Article
- Astrocyte elevated gene-1 (AEG-1) and the A(E)Ging HIV/AIDS-HAND.Progress in neurobiology · 2017Review
- The La-Related Proteins, a Family with Connections to Cancer.Biomolecules · 2015Review
- Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation.Virology journal · 2015Article
- Analysis of HIV-1 Gag protein interactions via biotin ligase tagging.Journal of virology · 2015Article
- Proteomics in the investigation of HIV-1 interactions with host proteins.Proteomics. Clinical applications · 2015Review
- Interplay between the alpharetroviral Gag protein and SR proteins SF2 and SC35 in the nucleus.Frontiers in microbiology · 2015Article
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- The role of AEG-1/MTDH/LYRIC in the pathogenesis of central nervous system disease.Advances in cancer research · 2013Review
- AEG-1/MTDH/LYRIC: signaling pathways, downstream genes, interacting proteins, and regulation of tumor angiogenesis.Advances in cancer research · 2013Article
- Budding of retroviruses utilizing divergent L domains requires nucleocapsid.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human immunodeficiency virus type 1 (HIV-1) Gag is the main structural protein driving assembly and release of virions from infected cells. Gag alone is capable of self-assembly in vitro, but host factors have been shown to play a role in efficient viral replication and particle morphogenesis within the living cell. In a series of affinity purification experiments, we identified the cellular protein Lyric to be an HIV-1 Gag-interacting protein. Lyric was previously described to be an HIV-inducible gene and is involved in various signaling pathways. Gag interacts with endogenous Lyric via its matrix (MA) and nucleocapsid (NC) domains. This interaction requires Gag multimerization and Lyric amino acids 101 to 289. Endogenous Lyric is incorporated into HIV-1 virions and is cleaved by the viral protease. Gag-Lyric interaction was also observed for murine leukemia virus and equine infectious anemia virus, suggesting that it represents a conserved feature among retroviruses. Expression of the Gag binding domain of Lyric increased Gag expression levels and viral infectivity, whereas expression of a Lyric mutant lacking the Gag binding site resulted in lower Gag expression and decreased viral infectivity. The results of the current study identify Lyric to be a cellular interaction partner of HIV-1 Gag and hint at a potential role in regulating infectivity. Further experiments are needed to elucidate the precise role of this interaction.
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