Volume 272, Number 41, Issue of October 10, 1997 pp. 25441-25444
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
N-Ethylmaleimide-sensitive Factor (NSF) and -Soluble NSF Attachment Proteins (SNAP) Mediate Dissociation of GS28-Syntaxin 5 Golgi SNAP Receptors (SNARE) Complex

(Received for publication, July 22, 1997, and in revised form, August 19, 1997)

From the Membrane Biology Laboratory, Institute of Molecular and Cell Biology, 15 Lower Kent Ridge Road, Singapore 119076, Singapore

Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) GS28 and syntaxin 5 can be reciprocally coimmunoprecipitated from Golgi extracts, suggesting that they exist in a protein complex. When Golgi extract is preincubated with soluble NSF attachment proteins (-SNAP) and N-ethylmaleimide-sensitive factor (NSF) under conditions that allow ATP hydrolysis by NSF, GS28 and syntaxin 5 become dissociated. GS28 and syntaxin 5 remain in a protein complex when Golgi extract is preincubated with similar amounts of -SNAP and NSF under conditions that prevent ATP hydrolysis by NSF, suggesting that ATP hydrolysis by NSF is necessary for dissociating the GS28-syntaxin 5 complex. Since preincubation of Golgi extract with either -SNAP or NSF alone has no effect on the GS28-syntaxin 5 complex, a concerted action of -SNAP and NSF therefore mediates the dissociation of the GS28-syntaxin 5 complex. Furthermore, GS28 but not syntaxin 5 is capable of binding to immobilized -SNAP when the GS28-syntaxin 5 complex is dissociated.

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