{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tao M"],"funding":["NINDS NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["5301"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7093510"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Membrane protein oligomerization mediates a wide range of biological events including signal transduction, viral infection and membrane curvature induction. However, the relative contributions of protein-protein and protein-membrane interactions to protein oligomerization remain poorly understood. Here, we used the Ca<sup>2+</sup>-dependent membrane-binding protein ANXB12 as a model system to determine the relative contributions of protein-protein and protein-membrane interactions toward trimer formation. Using an EPR-based detection method, we find that some protein-protein interactions are essential for trimer formation. Surprisingly, these interactions are largely hydrophobic, and they do not include the previously identified salt bridges, which are less important. Interfering with memb"],"journal":["Scientific reports"],"pubmed_title":["Annexin B12 Trimer Formation is Governed by a Network of Protein-Protein and Protein-Lipid Interactions."],"pmcid":["PMC7093510"],"funding_grant_id":["R01 NS084345","R01NS084345","R01 GM115736"],"pubmed_authors":["Tao M","Isas JM","Langen R"],"additional_accession":[]},"is_claimable":false,"name":"Annexin B12 Trimer Formation is Governed by a Network of Protein-Protein and Protein-Lipid Interactions.","description":"Membrane protein oligomerization mediates a wide range of biological events including signal transduction, viral infection and membrane curvature induction. However, the relative contributions of protein-protein and protein-membrane interactions to protein oligomerization remain poorly understood. Here, we used the Ca<sup>2+</sup>-dependent membrane-binding protein ANXB12 as a model system to determine the relative contributions of protein-protein and protein-membrane interactions toward trimer formation. Using an EPR-based detection method, we find that some protein-protein interactions are essential for trimer formation. Surprisingly, these interactions are largely hydrophobic, and they do not include the previously identified salt bridges, which are less important. Interfering with memb","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2026-06-07T08:01:56.494Z","creation":"2025-05-29T21:25:40.136Z"},"accession":"S-EPMC7093510","cross_references":{"pubmed":["32210350"],"doi":["10.1038/s41598-020-62343-x"]}}