Vesicle fusion probability is determined by the specific interactions of munc18

Research output: Contribution to journalArticle

Abstract

Mammalian-regulated secretion is absolutely dependent on four evolutionarily conserved proteins: three SNARE proteins and munc18. Dissecting the functional outcomes of the spatially organized protein interactions between these factors has been difficult because of the close interrelationship between different binding modes. Here, we investigated the spatial distribution of single munc18 molecules at the plasma membrane of cells and the underlying interactions between syntaxin and munc18. Disruption of munc18 binding to the N-terminal peptide motif of syntaxin did not alter munc18 localization on the plasma membrane but had a pronounced influence on the behavior of secretory vesicles and their likelihood to undergo fusion. We therefore conclude that interaction with the syntaxin N-peptide can confer differential release probabilities to secretory vesicles and may contribute to the delineation of secretory vesicle pools.

LanguageEnglish
Pages38141-38148
Number of pages8
JournalJournal of Biological Chemistry
Volume285
Issue number49
DOIs
Publication statusPublished - 3 Dec 2010

Fingerprint

Qa-SNARE Proteins
Secretory Vesicles
Cell Membrane
SNARE Proteins
Peptides
Plasma Cells
Cell Communication
Proteins

Keywords

  • Amino Acid Motifs
  • Animals
  • Cell Membrane
  • Membrane Fusion
  • Munc18 Proteins
  • PC12 Cells
  • Qa-SNARE Proteins
  • Rats
  • SNARE Proteins
  • Secretory Vesicles

Cite this

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title = "Vesicle fusion probability is determined by the specific interactions of munc18",
abstract = "Mammalian-regulated secretion is absolutely dependent on four evolutionarily conserved proteins: three SNARE proteins and munc18. Dissecting the functional outcomes of the spatially organized protein interactions between these factors has been difficult because of the close interrelationship between different binding modes. Here, we investigated the spatial distribution of single munc18 molecules at the plasma membrane of cells and the underlying interactions between syntaxin and munc18. Disruption of munc18 binding to the N-terminal peptide motif of syntaxin did not alter munc18 localization on the plasma membrane but had a pronounced influence on the behavior of secretory vesicles and their likelihood to undergo fusion. We therefore conclude that interaction with the syntaxin N-peptide can confer differential release probabilities to secretory vesicles and may contribute to the delineation of secretory vesicle pools.",
keywords = "Amino Acid Motifs, Animals, Cell Membrane, Membrane Fusion, Munc18 Proteins, PC12 Cells, Qa-SNARE Proteins, Rats, SNARE Proteins, Secretory Vesicles",
author = "Smyth, {Annya M} and Colin Rickman and Duncan, {Rory R}",
year = "2010",
month = "12",
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doi = "10.1074/jbc.M110.164038",
language = "English",
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pages = "38141--38148",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
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Vesicle fusion probability is determined by the specific interactions of munc18. / Smyth, Annya M; Rickman, Colin; Duncan, Rory R.

In: Journal of Biological Chemistry, Vol. 285, No. 49, 03.12.2010, p. 38141-38148.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Vesicle fusion probability is determined by the specific interactions of munc18

AU - Smyth, Annya M

AU - Rickman, Colin

AU - Duncan, Rory R

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N2 - Mammalian-regulated secretion is absolutely dependent on four evolutionarily conserved proteins: three SNARE proteins and munc18. Dissecting the functional outcomes of the spatially organized protein interactions between these factors has been difficult because of the close interrelationship between different binding modes. Here, we investigated the spatial distribution of single munc18 molecules at the plasma membrane of cells and the underlying interactions between syntaxin and munc18. Disruption of munc18 binding to the N-terminal peptide motif of syntaxin did not alter munc18 localization on the plasma membrane but had a pronounced influence on the behavior of secretory vesicles and their likelihood to undergo fusion. We therefore conclude that interaction with the syntaxin N-peptide can confer differential release probabilities to secretory vesicles and may contribute to the delineation of secretory vesicle pools.

AB - Mammalian-regulated secretion is absolutely dependent on four evolutionarily conserved proteins: three SNARE proteins and munc18. Dissecting the functional outcomes of the spatially organized protein interactions between these factors has been difficult because of the close interrelationship between different binding modes. Here, we investigated the spatial distribution of single munc18 molecules at the plasma membrane of cells and the underlying interactions between syntaxin and munc18. Disruption of munc18 binding to the N-terminal peptide motif of syntaxin did not alter munc18 localization on the plasma membrane but had a pronounced influence on the behavior of secretory vesicles and their likelihood to undergo fusion. We therefore conclude that interaction with the syntaxin N-peptide can confer differential release probabilities to secretory vesicles and may contribute to the delineation of secretory vesicle pools.

KW - Amino Acid Motifs

KW - Animals

KW - Cell Membrane

KW - Membrane Fusion

KW - Munc18 Proteins

KW - PC12 Cells

KW - Qa-SNARE Proteins

KW - Rats

KW - SNARE Proteins

KW - Secretory Vesicles

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