Selective stimulation of the D1 ATPase domain ofN-ethylmaleimide-sensitive fusion protein (NSF) by soluble NSF attachment proteins
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چکیده
منابع مشابه
The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins.
N-Ethylmaleimide-sensitive fusion protein (NSF) is an ATPase required in multiple stages of the secretory and endocytic pathways. NSF requires other proteins for its action in vesicular transport including the soluble NSF attachment proteins (SNAPs), which act to bind NSF to integral membrane proteins. We have investigated the ATPase activity of NSF and its modulation by alpha- and gamma-SNAPs ...
متن کاملNon-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...
متن کاملAssociation of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6.
PDZ domains are involved in the scaffolding and assembly of multi-protein complexes at various subcellular sites. We describe here the isolation and characterization of a novel PDZ domain-containing protein that localizes to the Golgi apparatus. Using an in silico cloning approach, we have identified and isolated a cDNA encoding a ubiquitously expressed 59-kDa protein that we call FIG. It is co...
متن کاملThe activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (alpha SNAP) during vesicle formation
An assay designed to measure the formation of functional transport vesicles was constructed by modifying a cell-free assay for protein transport between compartments of the Golgi (Balch, W. E., W. G. Dunphy, W. A. Braell, and J. E. Rothman. 1984. Cell. 39:405-416). A 35-kD cytosolic protein that is immunologically and functionally indistinguishable from alpha SNAP (soluble NSF attachment protei...
متن کاملA 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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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1998
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(98)00072-6