{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dick RA"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["18761-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3503231"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(46)"],"pubmed_abstract":["Membrane binding of the HIV-1 group-specific antigen (Gag) structural protein, a critical step in viral assembly at the plasma membrane, is mediated by the myristoylated, highly basic matrix (MA) domain, which interacts with negatively charged lipids in the inner leaflet. According to a popular model, virus particles bud from membrane rafts, microdomains enriched in cholesterol and high-melting phospholipids with higher order than found outside rafts. How Gag might recognize membrane rafts, if they exist in the inner leaflet, is unknown. Using a liposome flotation assay with proteins translated in vitro, we investigated whether Gag can sense the composition of the hydrophobic part of the bilayer, by fixing lipid head group composition and varying hydrophobic properties. In liposomes compos"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes."],"pmcid":["PMC3503231"],"funding_grant_id":["CA20081","R01 CA020081","R01 GM107013"],"pubmed_authors":["Feigenson GW","Vogt VM","Dick RA","Goh SL"],"additional_accession":[]},"is_claimable":false,"name":"HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes.","description":"Membrane binding of the HIV-1 group-specific antigen (Gag) structural protein, a critical step in viral assembly at the plasma membrane, is mediated by the myristoylated, highly basic matrix (MA) domain, which interacts with negatively charged lipids in the inner leaflet. According to a popular model, virus particles bud from membrane rafts, microdomains enriched in cholesterol and high-melting phospholipids with higher order than found outside rafts. How Gag might recognize membrane rafts, if they exist in the inner leaflet, is unknown. Using a liposome flotation assay with proteins translated in vitro, we investigated whether Gag can sense the composition of the hydrophobic part of the bilayer, by fixing lipid head group composition and varying hydrophobic properties. In liposomes compos","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Nov","modification":"2025-05-29T21:01:32.914Z","creation":"2025-05-29T21:01:32.914Z"},"accession":"S-EPMC3503231","cross_references":{"pubmed":["23010924"],"doi":["10.1073/pnas.1209408109"]}}