Haynes L P, Barnard R J, Morgan A, Burgoyne R D
The Physiological Laboratory, University of Liverpool, UK.
FEBS Lett. 1998 Sep 25;436(1):1-5. doi: 10.1016/s0014-5793(98)01088-6.
N-Ethylmaleimide-sensitive factor (NSF) plays a key role in vesicular traffic by disassembling and priming SNARE proteins for their function in docking and fusion. We demonstrate that the ATPase activity of NSF is activated by alpha-soluble NSF attachment protein (alpha-SNAP) in a complex with syntaxin 1A. In addition, we show that a construct consisting of the H3 domain of syntaxin IA (GST-synt(195-263), which does not support NSF disassembly in the presence of MgATP gave a larger stimulation. NSF ATPase activation was specific and did not occur using mutant alpha-SNAPs unable to bind GST-synt or with mutated C-termini. We suggest that activation of NSF ATPase activity in the SNARE complex may be essential to allow SNARE priming.
N - 乙基马来酰亚胺敏感因子（NSF）通过拆解和启动SNARE蛋白以使其在对接和融合中发挥作用，在囊泡运输中起关键作用。我们证明，NSF的ATP酶活性在与 syntaxin 1A形成的复合物中被α - 可溶性 NSF 附着蛋白（α - SNAP）激活。此外，我们表明，由 syntaxin IA的H3结构域组成的构建体（GST - synt(195 - 263)）在存在MgATP的情况下不支持NSF拆解，但能产生更大的刺激作用。NSF ATP酶激活具有特异性，使用无法结合GST - synt或具有突变C末端的突变α - SNAP时不会发生激活。我们认为，SNARE复合物中NSF ATP酶活性的激活对于SNARE启动可能至关重要。
