SNAP receptors implicated in vesicle targeting and fusion Journal Article


Authors: Söllner, T.; Whiteheart, S. W.; Brunner, M.; Erdjument-Bromage, H.; Geromanos, S.; Tempst, P.; Rothman, J. E.
Article Title: SNAP receptors implicated in vesicle targeting and fusion
Abstract: The N-ethylmaleimide-sensitive fusion protein (NSF) and the soluble NSF attachment proteins (SNAPs) appear to be essential components of the intracellular membrane fusion apparatus. An affinity purification procedure based on the natural binding of these proteins to their targets was used to isolate SNAP receptors (SNAREs) from bovine brain. Remarkably, the four principal proteins isolated were all proteins associated with the synapse, with one type located in the synaptic vesicle and another in the plasma membrane, suggesting a simple mechanism for vesicle docking. The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicle or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesicle-to-target specificity. © 1993 Nature Publishing Group.
Keywords: nonhuman; animal; animal tissue; models, biological; protein targeting; nerve tissue proteins; animalia; amino acid sequence; molecular sequence data; hybrid protein; brain; protein purification; carrier proteins; cell membrane; cattle; receptor; adenosine triphosphate; hydrolysis; bovinae; membrane fusion; synaptic vesicles; bos taurus; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; n ethylmaleimide
Journal Title: Nature
Volume: 362
Issue: 6418
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1993-03-25
Start Page: 318
End Page: 324
Language: English
DOI: 10.1038/362318a0
PUBMED: 8455717
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 1 March 2019 -- Source: Scopus
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  1. Thomas H Sollner
    65 Sollner
  2. James E Rothman
    120 Rothman
  3. Paul J Tempst
    324 Tempst