可溶性 NSF 附着蛋白/可溶性 NSF 附着蛋白受体复合物对 NSF ATP 酶的影响。

The effects of SNAP/SNARE complexes on the ATPase of NSF.

作者信息

Matveeva E, Whiteheart S W

机构信息

Department of Biochemistry, Chandler Medical Center, University of Kentucky College of Medicine, Lexington 40536-0084, USA.

出版信息

FEBS Lett. 1998 Sep 18;435(2-3):211-4. doi: 10.1016/s0014-5793(98)01071-0.

DOI:10.1016/s0014-5793(98)01071-0

PMID:9762911

Abstract

The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, alpha-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all alpha-SNAP-containing complexes, only the alpha-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more alpha-SNAP but did not stimulate the ATPase of NSF.

摘要

N - 乙基马来酰亚胺敏感因子（NSF）的ATP酶似乎在囊泡与靶膜融合最终发生的一系列事件中起着核心作用。重新构建了包含NSF、α - SNAP、Vamp - 2（突触小泡蛋白2）、 syntaxin 1和SNAP - 25不同组合的复合物，然后测试它们对NSF的ATP酶的影响。虽然NSF与所有含α - SNAP的复合物相互作用，但只有α - SNAP/t - SNARE复合物能显著刺激ATP酶活性。这种刺激依赖于增加的SNAP/t - SNARE复合物，并且具有饱和性。ATP酶活性的明显刺激是由于初始水解速率增加了10倍。同时包含v - SNARE和t - SNARE的复合物结合的α - SNAP明显更多，但并未刺激NSF的ATP酶活性。