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Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion

DOI: 10.1083/jcb.201502078 DOI Help
PMID: 26370501 PMID Help

Authors: L. Yan (Tsinghua University) , S. Sun (Nankai University) , W. Wang (Tsinghua University) , J. Shi (Nankai University) , X. Hu (Nankai University) , S. Wang (Henan University) , D. Su (Sichuan University) , Z. Rao (Tsinghua University) , J. Hu (Nankai University) , Z. Lou (Tsinghua University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Journal Of Cell Biology , VOL 210 (6) , PAGES 961 - 972

State: Published (Approved)
Published: September 2015

Abstract: Homotypic membrane fusion of the endoplasmic reticulum is mediated by dynamin-like guanosine triphosphatases (GTPases), which include atlastin (ATL) in metazoans and Sey1p in yeast. In this paper, we determined the crystal structures of the cytosolic domain of Sey1p derived from Candida albicans. The structures reveal a stalk-like, helical bundle domain following the GTPase, which represents a previously unidentified configuration of the dynamin superfamily. This domain is significantly longer than that of ATL and critical for fusion. Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AlF4− but is monomeric with GDP. Surprisingly, Sey1p could mediate fusion without GTP hydrolysis, even though fusion was much more efficient with GTP. Sey1p was able to replace ATL in mammalian cells, and the punctate localization of Sey1p was dependent on its GTPase activity. Despite the common function of fusogenic GTPases, our results reveal unique features of Sey1p.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Other Facilities: SSRF

Added On: 30/10/2015 15:21

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