{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu H"],"funding":["NIGMS NIH HHS"],"pagination":["39359-65"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2998153"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["285(50)"],"pubmed_abstract":["Phosphatidylinositol 3-phosphate (PI(3)P) and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) are essential for rapid SNARE-dependent fusion of yeast vacuoles and other organelles. These phosphoinositides also regulate the fusion of reconstituted proteoliposomes. The reconstituted reaction allows separate analysis of phosphoinositide-responsive subreactions: fusion with SNAREs alone, with the addition of the HOPS tethering factor, and with the further addition of the SNARE complex disassembly chaperones Sec17p and Sec18p. Using assays of membrane tethering, trans-SNARE pairing, and lipid mixing, we found that PI(3)P and PI(4,5)P(2) have distinct functions that are asymmetric with respect to R-SNARE (Nyv1p) and the 3Q-SNAREs (Vam3p, Vti1p, and Vam7p). Fusion reactions with the Q-SNAREs "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly."],"pmcid":["PMC2998153"],"funding_grant_id":["GM23377-35","R01 GM023377"],"pubmed_authors":["Wickner W","Xu H"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly.","description":"Phosphatidylinositol 3-phosphate (PI(3)P) and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) are essential for rapid SNARE-dependent fusion of yeast vacuoles and other organelles. These phosphoinositides also regulate the fusion of reconstituted proteoliposomes. The reconstituted reaction allows separate analysis of phosphoinositide-responsive subreactions: fusion with SNAREs alone, with the addition of the HOPS tethering factor, and with the further addition of the SNARE complex disassembly chaperones Sec17p and Sec18p. Using assays of membrane tethering, trans-SNARE pairing, and lipid mixing, we found that PI(3)P and PI(4,5)P(2) have distinct functions that are asymmetric with respect to R-SNARE (Nyv1p) and the 3Q-SNAREs (Vam3p, Vti1p, and Vam7p). Fusion reactions with the Q-SNAREs ","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2025-04-04T20:12:59.202Z","creation":"2019-03-27T00:37:14Z"},"accession":"S-EPMC2998153","cross_references":{"pubmed":["20937838"],"doi":["10.1074/jbc.m110.183111","10.1074/jbc.M110.183111"]}}