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Vol. 273, Issue 3, 1334-1338, January 16, 1998

N-Ethylmaleimide-Sensitive Factor-dependent -SNAP Release, an Early Event in the Docking/Fusion Process, Is Not Regulated by Rab GTPases

Maria I. Colombo, S. Courtney Gelberman, Sidney W. Whiteheart^¶, and Philip D. Stahl

From the  Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110 and the ^¶ Department of Biochemistry, University of Kentucky College of Medicine, Chandler Medical Center, Lexington, Kentucky 40536

The N-ethylmaleimide-sensitive factor (NSF) is required for multiple intracellular vesicle transport events. In vitro biochemical studies have demonstrated that NSF, soluble NSF attachment proteins (SNAPs), and SNAP receptors form a 20 S particle. This complex is disassembled by the ATPase activity of NSF. We have studied particle disassembly in a membrane environment by examining the binding of recombinant SNAPs and NSF to endosomal membranes. We present evidence that -SNAP is released from the membranes in a temperature- and time-dependent manner and that this release is mediated by the ATPase activity of NSF. Our results indicate that NSF mutants in the first ATP binding domain completely abrogate -SNAP release, whereas no inhibitory effect is observed with a mutant in the second ATP binding domain. Interestingly, neither -SNAP nor -SNAP are released by the ATPase activity of NSF, indicating that these proteins are retained on the membranes by interactions that differ from those that retain -SNAP. Although the small Rab GTPases are known to play a role in SNARE complex assembly, our results indicate that these GTPases do not regulate the NSF-dependent release of -SNAP.

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