Stimulation of NSF ATPase activity during t‐SNARE priming

FEBS Letters

Burgoyne, Robert D.¹  Haynes, Lee P.¹  Barnard, Richard J.O.¹  Morgan, Alan¹ 

[1] The Physiological Laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, UK

关键词: Syntaxin;    N-Ethylmaleimide-sensitive factor;    ATPase;    Vesicular traffic;    Soluble NSF attachment protein receptor;    GST;    glutathione-S-transferase;    NSF;    N-ethylmaleimide-sensitive factor;    SNAP;    soluble NSF attachment protein;    SNARE;    SNAP receptor;   

DOI  :  10.1016/S0014-5793(98)01088-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-soluble NSF attachment protein (α-SNAP) in a complex with syntaxin 1A. In addition, we show that a construct consisting of the H3 domain of syntaxin 1A (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 α-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.

【 授权许可】

Unknown