{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiang Y"],"funding":["Josie Robertson Investigators Program Searle Scholars Program","U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke","U.S. Department of Health & Human Services | NIH | National Center for Complementary and Integrative Health (NCCIH)","U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS)","NCI NIH HHS","Kavli Foundation","U.S. Department of Health & Human Services | NIH | National Center for Complementary and Integrative Health","U.S. Department of Health & Human Services | NIH | NCI | Division of Cancer Epidemiology and Genetics, National Cancer Institute"],"pagination":["7373"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9712761"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["The plasma membrane's main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents."],"journal":["Nature communications"],"pubmed_title":["Membrane-mediated protein interactions drive membrane protein organization."],"pmcid":["PMC9712761"],"funding_grant_id":["R01NS110790","R01NS116747","P30 CA008748","DP1AT010874"],"pubmed_authors":["Jiang Y","Sturgis JN","Thienpont B","Scheuring S","Hite RK","Dittman JS","Sapuru V"],"additional_accession":[]},"is_claimable":false,"name":"Membrane-mediated protein interactions drive membrane protein organization.","description":"The plasma membrane's main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-27T22:56:22.969Z","creation":"2025-04-06T12:14:08.179Z"},"accession":"S-EPMC9712761","cross_references":{"pubmed":["36450733"],"doi":["10.1038/s41467-022-35202-8"]}}