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PMID: 8455721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

SNAP family of NSF attachment proteins includes a brain-specific isoform.

Nature ·Vol. 362 ·No. 6418 ·1993-03-25 ·Pages 353-5

Whiteheart SW, Griff IC, Brunner M, Clary DO, Mayer T, Buhrow SA, Rothman JE

Abstract

The soluble NSF attachment proteins (SNAPs) enable N-ethyl-maleimide-sensitive fusion protein (NSF) to bind to target membranes. Here we report the cloning and sequencing of complementary DNAs encoding alpha-, beta- and gamma-SNAPs. Two of these proteins, alpha and gamma, are found in a wide range of tissues, and act synergistically in intra-Golgi transport. The third, beta, is a brain-specific isoform of alpha-SNAP. Thus, NSF and SNAPs appear to be general components of the intracellular membrane fusion apparatus, and their action at specific sites of fusion must be controlled by SNAP receptors particular to the membranes being fused, as described in the accompanying article.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Northern Brain Chemistry Carrier Proteins/chemistry Cattle Cloning, Molecular Intracellular Membranes/chemistry Membrane Fusion Mice Molecular Sequence Data N-Ethylmaleimide-Sensitive Proteins Organ Specificity Recombinant Proteins/chemistry Vesicular Transport Proteins
Chemicals
Carrier Proteins Recombinant Proteins Vesicular Transport Proteins N-Ethylmaleimide-Sensitive Proteins Nsf protein, mouse
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Whiteheart S W
Rockefeller Research Laboratory, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
Griff I C
Brunner M
Clary D O
Mayer T
Buhrow S A
Rothman J E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1993-03-25
Pages
353-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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