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PMID: 8108733 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking.

Science (New York, N.Y.) ·Vol. 263 ·No. 5150 ·1994-02-25 ·Pages 1146-9

Calakos N, Bennett MK, Peterson KE, Scheller RH

Abstract

Intracellular vesicles destined to fuse with the plasma membrane and secrete their contents must have a mechanism for specifically interacting with the appropriate target membrane. Such a mechanism is now suggested by the demonstration of specific interaction between vesicular proteins and plasma membrane proteins. The vesicle-associated membrane proteins (VAMPs) 1 and 2 specifically bind the acceptor membrane proteins syntaxin 1A and 4 but not syntaxin 2 or 3. The binding site is within amino acids 194 to 267 of syntaxin 1A, and the approximate equilibrium dissociation constants is 4.7 x 10(-6) molar. These data suggest a physical basis for the specificity of intracellular vesicular transport.

MeSH Terms
Amino Acid Sequence Animals Antigens, Surface/metabolism Binding Sites Cell Line Cell Membrane/metabolism Cytoplasm/metabolism Haplorhini Kinetics Membrane Proteins/metabolism Molecular Sequence Data Nerve Tissue Proteins/metabolism R-SNARE Proteins Recombinant Fusion Proteins/metabolism Synaptic Vesicles/metabolism Syntaxin 1
Chemicals
Antigens, Surface Membrane Proteins Nerve Tissue Proteins R-SNARE Proteins Recombinant Fusion Proteins Syntaxin 1
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Calakos N
Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305.
Bennett M K
Peterson K E
Scheller R H
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1994-02-25
Pages
1146-9
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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