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One structure corresponds to a prefusion state, in which ATL molecules in apposing membranes interact through their GTPase domains to form a dimer with the nucleotides bound at the interface. The other structure corresponds to a postfusion state generated after GTP hydrolysis and phosphate release. Compared with the prefusion structure, the three-helix bundles of the two ATL molecules undergo a major conformational change relative to the GTPase domains, which could pull the membranes together. The proposed fusion mechanism is supported by biochemical experiments and fusion assays with wild-type and mutant full-length\n                    <jats:italic>Drosophila<\/jats:italic>\n                    ATL. These experiments also show that membrane fusion is facilitated by the C-terminal cytosolic tails following the two transmembrane segments. Finally, our results show that mutations in ATL1 causing hereditary spastic paraplegia compromise homotypic ER fusion.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1101643108","type":"journal-article","created":{"date-parts":[[2011,2,22]],"date-time":"2011-02-22T22:52:57Z","timestamp":1298415177000},"page":"3976-3981","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":235,"title":["Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes"],"prefix":"10.1073","volume":"108","author":[{"given":"Xin","family":"Bian","sequence":"first","affiliation":[{"name":"Departments of aGenetics and Cell Biology and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robin W.","family":"Klemm","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cell Biology, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tina Y.","family":"Liu","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cell Biology, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miao","family":"Zhang","sequence":"additional","affiliation":[{"name":"Departments of aGenetics and Cell Biology and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sha","family":"Sun","sequence":"additional","affiliation":[{"name":"Departments of aGenetics and Cell Biology and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuewu","family":"Sui","sequence":"additional","affiliation":[{"name":"Departments of aGenetics and Cell Biology and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinqi","family":"Liu","sequence":"additional","affiliation":[{"name":"Biochemistry and Molecular Biology, College of Life Sciences, and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom A.","family":"Rapoport","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cell Biology, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junjie","family":"Hu","sequence":"additional","affiliation":[{"name":"Departments of aGenetics and Cell Biology and"},{"name":"Tianjin Key Laboratory of Protein Sciences, Nankai University, Tianjin 300071, China; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,2,22]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0074-7696(01)05004-5","article-title":"Endoplasmic reticulum of animal cells and its organization into structural and functional domains","volume":"205","author":"Baumann O","year":"2001","unstructured":"O Baumann, B Walz, Endoplasmic reticulum of animal cells and its organization into structural and functional domains. 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