{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alpadi K"],"funding":["Swiss National Science Foundation","Medical Research Council","Biotechnology and Biological Sciences Research Council","NIGMS NIH HHS"],"pagination":["1704"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3630463"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4"],"pubmed_abstract":["The fundamental processes of membrane fission and fusion determine size and copy numbers of intracellular organelles. Although SNARE proteins and tethering complexes mediate intracellular membrane fusion, fission requires the presence of dynamin or dynamin-related proteins. Here we study these reactions in native yeast vacuoles and find that the yeast dynamin homologue Vps1 is not only an essential part of the fission machinery, but also controls membrane fusion by generating an active Qa SNARE-tethering complex pool, which is essential for trans-SNARE formation. Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins."],"journal":["Nature communications"],"pubmed_title":["Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion."],"pmcid":["PMC3630463"],"funding_grant_id":["GM087333","128661","BB/K002511/1","G0601600","R01 GM087333","GM088803","R01 GM088803"],"pubmed_authors":["Peters C","Kulkarni A","Ayscough K","Sippel KH","Evangelista M","Quiocho FA","Schmidt A","Zieger M","Srinivasan S","Namjoshi S","Mayer A","Alpadi K"],"additional_accession":[]},"is_claimable":false,"name":"Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion.","description":"The fundamental processes of membrane fission and fusion determine size and copy numbers of intracellular organelles. Although SNARE proteins and tethering complexes mediate intracellular membrane fusion, fission requires the presence of dynamin or dynamin-related proteins. Here we study these reactions in native yeast vacuoles and find that the yeast dynamin homologue Vps1 is not only an essential part of the fission machinery, but also controls membrane fusion by generating an active Qa SNARE-tethering complex pool, which is essential for trans-SNARE formation. Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins.","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2025-04-25T22:17:04.29Z","creation":"2019-03-27T01:07:38Z"},"accession":"S-EPMC3630463","cross_references":{"pubmed":["23591871"],"doi":["10.1038/ncomms2724"]}}