SNAP family of NSF attachment proteins includes a brain-specific isoform
Article Abstract:
N-ethylmaleimide-sensitive fusion protein (NSF) is a membrane fusion protein which interact with soluble NSF attachment proteins (SNAPs) during membrane fusion events. A bovine brain cDNA library was screened for clones coding for alpha- beta- and gamma-SNAPs. Sequence analysis showed that the cDNA clones corresponding to alpha- beta- and gamma-SNAP code for proteins with molecular weights of 33K, 34K and 36K, respectively. Southern blot analysis showed that these proteins are encoded by a single gene. Northern blotanalysis localized the expression of alpha- and gamma-SNAP in the intra-Golgi compartment of various tissues, while beta-SNAP was localized to the brain.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Bridging the gap
Article Abstract:
The proper fusion of vesicles and membrane compartments requires a docking mechanism whichdetermines the precise binding of vesicles to membranes. Investigations seekingto elucidate the fusion machinery have isolated specific factors involved in the docking mechanism. The general fusion factors are the N-ethylmaleimide sensitive factor (NSF) and the soluble, NSF accessory proteins (SNAPs). Syntaxin and synaptobrevin-2 have been identified as SNAP receptors which are hypothesized to be responsible for fusion specificity.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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P47 is a cofactor for p97-mediated membrane fusion
Article Abstract:
ATPases NSF and p97 are known to have an affect on the heterotypic fusion of transport vesicles with the target membranes. Many components of the NSF-mediated fusion pathway have been indentified. The first component of the P97 mediated fusion pathway has been identified. It is a protein, forming a tight, stoichiometric complex and is necessary for the p97-mediated regrowth of Golgi cisternae from mitotic Golgi fragments.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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