N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex.

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 (alpha-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 alpha-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 alpha-SNAP or NSF alone has no effect on the GS28-syntaxin 5 complex, a concerted action of alpha-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 alpha-SNAP when the GS28-syntaxin 5 complex is dissociated.
Mesh Terms:
Animals, Carrier Proteins, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, Indirect, Golgi Apparatus, Macromolecular Substances, Membrane Proteins, Microscopy, Fluorescence, N-Ethylmaleimide-Sensitive Proteins, Nerve Tissue Proteins, Qa-SNARE Proteins, Rabbits, SNARE Proteins, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins, Vesicular Transport Proteins
J. Biol. Chem.
Date: Oct. 10, 1997
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