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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:AAA + ATPase N-乙基马来酰亚胺敏感因子(NSF)的结构和分子机制的最新研究进展

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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)于1988年首次发现,是真核生物运输的关键因素,包括蛋白质和激素的分泌以及神经递质的释放。它是AAA +家族(与多种细胞活动相关的ATP酶)的成员。 NSF与可溶性N-乙基马来酰亚胺敏感因子附着蛋白(SNAP)一起分解可溶的N-乙基马来酰亚胺敏感因子附着蛋白受体(SNARE)复合物。 NSF及其与SNARE和SNAP的复合体(称为20S超复合体)的结构研究始于20年前。多年来,已经报道了NSF的各个N和D2域的晶体结构以及全长NSF和20S超复合物的低分辨率电子显微镜结构。然而,直到最近,20S超复合物的分子结构和NSF介导的SNARE复合物分解的分子机制仍不清楚。在这里,我们回顾了NSF和20S超复合物的近期原子拆分或近原子拆分结构,以及对NSF分子机理和能量需求的最新见解。我们还将NSF与其他已知的AAA +家族成员进行了比较。 (C)2015作者。由Elsevier Ltd.发布。这是CC BY-NC-ND许可(http://creativecommons.org/licenses/by-nc-nd/4.0/)下的开放获取文章。

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