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Stimulation of NSF ATPase activity during t‐SNARE priming
Author(s) -
Haynes Lee P.,
Barnard Richard J.O.,
Morgan Alan,
Burgoyne Robert D.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01088-6
Subject(s) - snare complex , syntaxin , priming (agriculture) , chemistry , microbiology and biotechnology , stimulation , mutant , docking (animal) , lipid bilayer fusion , biophysics , biochemistry , biology , vesicle , neuroscience , membrane , medicine , germination , botany , nursing , gene
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.