α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Recent experiments showed that α-SNAP also dramatical...
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doaj-4208b9f7419140b883c7f46f504fa1622020-11-24T21:21:04ZengElsevierCell Reports2211-12472016-04-0115353153910.1016/j.celrep.2016.03.050α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix BundleLu Ma0Yuhao Kang1Junyi Jiao2Aleksander A. Rebane3Hyo Keun Cha4Zhiqun Xi5Hong Qu6Yongli Zhang7Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USADepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USAIntracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Recent experiments showed that α-SNAP also dramatically enhances SNARE assembly and membrane fusion. How α-SNAP is involved in these opposing activities is not known. Here, we examine the effect of α-SNAP on the stepwise assembly of the synaptic SNARE complex using optical tweezers. We found that α-SNAP destabilized the linker domain (LD) of the SNARE complex but stabilized its C-terminal domain (CTD) through a conformational selection mechanism. In contrast, α-SNAP minimally affected assembly of the SNARE N-terminal domain (NTD), indicating that α-SNAP barely bound the partially assembled trans-SNARE complex. Thus, α-SNAP recognizes the folded CTD for SNARE disassembly with NSF and subtly modulates membrane fusion by altering the stabilities of the SNARE CTD and LD.http://www.sciencedirect.com/science/article/pii/S2211124716303217 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lu Ma Yuhao Kang Junyi Jiao Aleksander A. Rebane Hyo Keun Cha Zhiqun Xi Hong Qu Yongli Zhang |
spellingShingle |
Lu Ma Yuhao Kang Junyi Jiao Aleksander A. Rebane Hyo Keun Cha Zhiqun Xi Hong Qu Yongli Zhang α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle Cell Reports |
author_facet |
Lu Ma Yuhao Kang Junyi Jiao Aleksander A. Rebane Hyo Keun Cha Zhiqun Xi Hong Qu Yongli Zhang |
author_sort |
Lu Ma |
title |
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle |
title_short |
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle |
title_full |
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle |
title_fullStr |
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle |
title_full_unstemmed |
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle |
title_sort |
α-snap enhances snare zippering by stabilizing the snare four-helix bundle |
publisher |
Elsevier |
series |
Cell Reports |
issn |
2211-1247 |
publishDate |
2016-04-01 |
description |
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion. Recent experiments showed that α-SNAP also dramatically enhances SNARE assembly and membrane fusion. How α-SNAP is involved in these opposing activities is not known. Here, we examine the effect of α-SNAP on the stepwise assembly of the synaptic SNARE complex using optical tweezers. We found that α-SNAP destabilized the linker domain (LD) of the SNARE complex but stabilized its C-terminal domain (CTD) through a conformational selection mechanism. In contrast, α-SNAP minimally affected assembly of the SNARE N-terminal domain (NTD), indicating that α-SNAP barely bound the partially assembled trans-SNARE complex. Thus, α-SNAP recognizes the folded CTD for SNARE disassembly with NSF and subtly modulates membrane fusion by altering the stabilities of the SNARE CTD and LD. |
url |
http://www.sciencedirect.com/science/article/pii/S2211124716303217 |
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