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Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA plus ATPase N-Ethylmaleimide-Sensitive Factor (NSF)

机译:解入AAA加上ATP酶N-乙基马来酰亚胺敏感因子(NSF)的结构和分子机制的最新进展

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摘要

N-ethylmaleimide-sensitive factor (NSF), first discovered in 1988, is a key factor for eukaryotic trafficking, including protein and hormone secretion and neurotransmitter release. It is a member of the AAA+ family (ATPases associated with diverse cellular activities). NSF disassembles soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes in conjunction with soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP). Structural studies of NSF and its complex with SNAREs and SNAPs (known as 20S supercomplex) started about 20 years ago. Crystal structures of individual N and D2 domains of NSF and low-resolution electron microscopy structures of full-length NSF and 20S supercomplex have been reported over the years. Nevertheless, the molecular architecture of the 20S supercomplex and the molecular mechanism of NSF-mediated SNARE complex disassembly remained unclear until recently. Here we review recent atomic-resolution or near-atomic resolution structures of NSF and of the 20S supercomplex, as well as recent insights into the molecular mechanism and energy requirements of NSF. We also compare NSF with other known AAA+ family members. (C) 2015 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
机译:N-乙基马来酰亚胺敏感因子(NSF)首次于1988年发现,是真核贩运的关键因素,包括蛋白质和激素分泌和神经递质释放。它是AAA +家族的成员(与多种细胞活动相关的ATPASE)。 NSF拆卸可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体(圈套)配合物与可溶性的N-乙基马来酰亚胺敏感因子附着蛋白(SNAP)结合。 NSF的结构研究及其复合物与捕获和捕获(称为20S超级复合)大约20年前。多年来,已经报道了多年来NSF的NSF和低分辨率电子显微镜结构的单个N和D2结构域的晶体结构已经报告了全长NSF和20S超复杂。然而,20S超复杂的分子结构和NSF介导的纳雷复合物拆卸拆卸的分子结构仍不清楚,直至最近。在这里,我们审查了NSF的最近原子分辨率或近似原子分辨率结构,以及20S超复合物的最新洞察,以及NSF的分子机制和能量要求。我们还将NSF与其他已知的AAA +家族成员进行比较。 (c)2015年作者。由elsevier有限公司出版。这是CC By-NC-ND许可下的开放式访问文章(http://creativecommons.org/licenses/by-nc-nd/4.0/)。

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