Distinct Roles for N-Ethylmaleimide-sensitive Fusion Protein (NSF) Suggested by the Identification of a Second Drosophila NSF Homolog

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The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins.

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A critical role for N-ethylmaleimide-sensitive fusion protein (NSF) in platelet granule secretion.

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Non-standard abbreviations: N-ethylmaleimide sensitive factor (NSF) Soluble NSF Attachment protein Receptor (SNARE) Soluble NSF Attachment Proteins (SNAP) Transactivating regulatory protein (Tat) von Willebrand factor (vWF)

Transactivating regulatory protein (Tat) von Willebrand factor (vWF) This article has not been copyedited and formatted. The final version may differ from this version. Abstract N-ethylmaleimide sensitive factor (NSF) plays a critical role in the regulation of exocytosis. NSF regulates exocytosis by interacting with a complex containing SNARE molecules, hydrolyzing ATP, and disassembling the SN...

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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY A Critical Role for N-ethylmaleimide–Sensitive Fusion Protein (NSF) in Platelet Granule Secretion

The molecular mechanisms that regulate membrane targeting/fusion during platelet granule secretion are not yet understood. N-ethylmaleimide-sensitive fusion protein (NSF), soluble NSF attachment proteins (SNAPs), and SNAREs (SNAP receptors) are elements of a conserved molecular machinery for membrane targeting/fusion that have been detected in platelets. We examined whether NSF, an ATPase that ...

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Processive ATP-driven Substrate Disassembly by the N-Ethylmaleimide-sensitive Factor (NSF) Molecular Machine*♦

SNARE proteins promote membrane fusion by forming a four-stranded parallel helical bundle that brings the membranes into close proximity. Post-fusion, the complex is disassembled by an AAA+ ATPase called N-ethylmaleimide-sensitive factor (NSF). We present evidence that NSF uses a processive unwinding mechanism to disassemble SNARE proteins. Using a real-time disassembly assay based on fluoresce...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1995

ISSN: 0021-9258

DOI: 10.1074/jbc.270.32.18742