FEBS Letters
Volume 436, Issue 1 , Pages 1-5, 25 September 1998

Stimulation of NSF ATPase activity during t-SNARE priming

  • Lee P. Haynes
    • ,
  • Richard J.O. Barnard

      Affiliations

    • Present address: Department of Genetics, University of Wisconsin, Madison, Wisconsin, USA.
    • Present address: Department of Genetics, University of Wisconsin, Madison, Wisconsin, USA.
    • ,
  • Alan Morgan
    • ,
  • Robert D. Burgoyne

      Affiliations

    • Corresponding Author InformationCorresponding author. Fax: (44) (151) 794-5337. E-mail: burgoyne@liverpool.ac.uk

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

Received 20 July 1998

Abstract 

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.

Keywords:  Syntaxin, N-Ethylmaleimide-sensitive factor, ATPase, Vesicular traffic, Soluble NSF attachment protein receptor

Abbreviations:  GST, glutathione-S-transferase, NSF, N-ethylmaleimide-sensitive factor, SNAP, soluble NSF attachment protein, SNARE, SNAP receptor

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PII: S0014-5793(98)01088-6

FEBS Letters
Volume 436, Issue 1 , Pages 1-5, 25 September 1998

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