{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu TY"],"funding":["Howard Hughes Medical Institute","National Natural Science Foundation of China","National Science Foundation"],"pagination":["E1851-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4403200"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(15)"],"pubmed_abstract":["Atlastin (ATL), a membrane-anchored GTPase that mediates homotypic fusion of endoplasmic reticulum (ER) membranes, is required for formation of the tubular network of the peripheral ER. How exactly ATL mediates membrane fusion is only poorly understood. Here we show that fusion is preceded by the transient tethering of ATL-containing vesicles caused by the dimerization of ATL molecules in opposing membranes. Tethering requires GTP hydrolysis, not just GTP binding, because the two ATL molecules are pulled together most strongly in the transition state of GTP hydrolysis. Most tethering events are futile, so that multiple rounds of GTP hydrolysis are required for successful fusion. Supported lipid bilayer experiments show that ATL molecules sitting on the same (cis) membrane can also undergo "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Cis and trans interactions between atlastin molecules during membrane fusion."],"pmcid":["PMC4403200"],"funding_grant_id":["N/A","31225006"],"pubmed_authors":["Liu TY","Shemesh T","Hu J","Romano FB","Bian X","Rapoport TA"],"additional_accession":[]},"is_claimable":false,"name":"Cis and trans interactions between atlastin molecules during membrane fusion.","description":"Atlastin (ATL), a membrane-anchored GTPase that mediates homotypic fusion of endoplasmic reticulum (ER) membranes, is required for formation of the tubular network of the peripheral ER. How exactly ATL mediates membrane fusion is only poorly understood. Here we show that fusion is preceded by the transient tethering of ATL-containing vesicles caused by the dimerization of ATL molecules in opposing membranes. Tethering requires GTP hydrolysis, not just GTP binding, because the two ATL molecules are pulled together most strongly in the transition state of GTP hydrolysis. Most tethering events are futile, so that multiple rounds of GTP hydrolysis are required for successful fusion. Supported lipid bilayer experiments show that ATL molecules sitting on the same (cis) membrane can also undergo ","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2026-04-13T08:26:12.789Z","creation":"2026-04-07T13:29:03.64Z"},"accession":"S-EPMC4403200","cross_references":{"pubmed":["25825753"],"doi":["10.1073/pnas.1504368112"]}}