ArticleCell host & microbe2017
Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.
Article in Cell host & microbe, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
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- HIV-1 matrix-tRNA complex structure reveals basis for host control of Gag localization.Cell host & microbe · 2021Article
- Host metabolic reprogramming in response to SARS-CoV-2 infection: A systems biology approach.Microbial pathogenesis · 2021Article
- Protein N-myristoylation: functions and mechanisms in control of innate immunity.Cellular & molecular immunology · 2021Review
- Across the Hall from Pioneers.Viruses · 2021Article
- Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site.The Journal of biological chemistry · 2020Article
- Myristoylation of EV71 VP4 is Essential for Infectivity and Interaction with Membrane Structure.Virologica Sinica · 2020Article
- N-myristoylation: from cell biology to translational medicine.Acta pharmacologica Sinica · 2020Review
- Intrinsic properties and plasma membrane trafficking route of Src family kinase SH4 domains sensitive to retargeting by HIV-1 Nef.The Journal of biological chemistry · 2018Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
N-myristoylation is the covalent attachment of myristic acid to the N terminus of proteins in eukaryotic cells. The matrix domain (MA) of HIV-1 Gag protein is N-myristoylated and plays an important role in virus budding. In screening for host factors that interact with HIV-1 MA, we found that heme oxygenase (HO-2) specifically binds the myristate moiety of Gag. HO-2 was also found to bind TRAM, an adaptor protein for Toll-like receptor 4 (TLR4), and thereby impact both virus replication and cellular inflammatory responses. A crystal structure revealed that HO-2 binds myristate via a hydrophobic channel adjacent to the heme-binding pocket. Inhibiting HO-2 expression, or blocking myristate binding with a heme analog, led to marked increases in virus production. HO-2 deficiency caused hyperresponsive TRAM-dependent TLR4 signaling and hypersensitivity to the TLR4 ligand lipopolysaccharide. Thus, HO-2 is a cellular myristate-binding protein that negatively regulates both virus replication and host inflammatory responses.
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