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Science 25 February 1994: Vol. 263. no. 5150, pp. 1146 - 1149 DOI: 10.1126/science.8108733
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Articles
Science, Vol 263, Issue 5150, 1146-1149
Copyright © 1994 by American Association for the Advancement of Science
Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
N Calakos,
MK Bennett,
KE Peterson,
and
RH Scheller
Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305.
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.
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J. Biol. Chem.
271, 13300-13303
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- Evidence That Syntaxin 1A Is Involved in Storage in the Secretory Pathway.
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271, 11214-11221
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- Mammalian Vesicle Trafficking Proteins of the Endoplasmic Reticulum and Golgi Apparatus.
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J. Biol. Chem.
271, 5671-5679
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- Patch-clamp capacitance analysis of the effects of alpha-SNAP on exocytosis in adrenal chromaffin cells.
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J. Cell Sci.
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- Functional Diversity of C2 Domains of Synaptotagmin Family.
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J. Biol. Chem.
270, 26523-26527
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- Ca[IMAGE] Regulates the Interaction between Synaptotagmin and Syntaxin 1.
- E. R. Chapman, P. I. Hanson, S. An, and R. Jahn (1995)
J. Biol. Chem.
270, 23667-23671
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- Inhibition of Neurotransmitter Release by Synthetic Proline-rich Peptides Shows That the N-terminal Domain of Vesicle-associated Membrane Protein/Synaptobrevin Is Critical for Neuro-exocytosis.
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270, 16826-16832
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- The N-Ethylmaleimide-sensitive Fusion Protein and [IMAGE]-SNAP Induce a Conformational Change in Syntaxin.
- P. I. Hanson, H. Otto, N. Barton, and R. Jahn (1995)
J. Biol. Chem.
270, 16955-16961
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- Syntaxin 1 (HPC-1) Is Associated with Chromaffin Granules.
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270, 15930-15933
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- A Novel Ubiquitous Form of Munc-18 Interacts with Multiple Syntaxins.
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J. Biol. Chem.
270, 13022-13028
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- Botulinum Neurotoxin Type C Cleaves a Single Lys-Ala Bond within the Carboxyl-terminal Region of Syntaxins.
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270, 10566-10570
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- Molecular Identification of Two Novel Munc-18 Isoforms Expressed in Non-neuronal Tissues.
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270, 5857-5863
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- The Biochemistry of Neurotransmitter Secretion.
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270, 1971-1974
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- Vesicle-associated Membrane Protein (VAMP)/Synaptobrevin-2 Is Associated with Dense Core Secretory Granules in PC12 Neuroendocrine Cells.
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270, 1332-1336
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- SNAREs Involved in Traffic through the Golgi Complex.
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Cold Spring Harb Symp Quant Biol
60, 105-111
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- Control of Exocytosis in Yeast.
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Cold Spring Harb Symp Quant Biol
60, 171-177
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- Botulinum and Tetanus Neurotoxins: Emerging Tools for the Study of Membrane Fusion.
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Cold Spring Harb Symp Quant Biol
60, 329-335
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