Munc18-1 and syntaxin1: unraveling the interactions between the dynamic duo

Research output: Contribution to journalArticle

Abstract

All neurotransmitter and hormone regulated secretory events involve the action of three soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, syntaxin, SNAP-25, and synaptobrevin. The SNARE proteins interact to form a four alpha-helical complex, involving syntaxin and SNAP-25 on the plasma membrane and synaptobrevin on the vesicular membrane, bringing the opposing membranes together, promoting bilayer merger and membrane fusion. The process of regulated secretion is an adaptation of the membrane fusion events which occur at multiple steps throughout the intracellular trafficking pathway, in each case catalyzed by SNARE protein isoforms. At all of these locations, the SNAREs are joined by a member of the Sec1p/Munc18 (SM) protein family which selectively bind to syntaxin isoforms. From their initial identification, the SM proteins were known to be essential for membrane fusion, however, over the intervening decades, deciphering the precise mechanism of action of the SM proteins has proved problematic. Recent studies, investigating the interactions of munc18-1 and syntaxin1, provide an explanation for previous, apparently conflicting, observations yielding a new understanding of their cellular functions.
LanguageEnglish
Pages1309-13
Number of pages5
JournalCellular and Molecular Neurobiology
Volume30
Issue number8
DOIs
Publication statusPublished - 2010

Fingerprint

SNARE Proteins
Munc18 Proteins
Qa-SNARE Proteins
Membrane Fusion
R-SNARE Proteins
Protein Isoforms
Membranes
Secretory Pathway
Neurotransmitter Agents
Cell Membrane
Hormones

Keywords

  • Animals
  • Models, Molecular
  • Munc18
  • Protein Binding
  • Syntaxin 1
  • Exocytosis
  • SNARE

Cite this

@article{189118f7d849481c908d8ebf190b7cf2,
title = "Munc18-1 and syntaxin1: unraveling the interactions between the dynamic duo",
abstract = "All neurotransmitter and hormone regulated secretory events involve the action of three soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, syntaxin, SNAP-25, and synaptobrevin. The SNARE proteins interact to form a four alpha-helical complex, involving syntaxin and SNAP-25 on the plasma membrane and synaptobrevin on the vesicular membrane, bringing the opposing membranes together, promoting bilayer merger and membrane fusion. The process of regulated secretion is an adaptation of the membrane fusion events which occur at multiple steps throughout the intracellular trafficking pathway, in each case catalyzed by SNARE protein isoforms. At all of these locations, the SNAREs are joined by a member of the Sec1p/Munc18 (SM) protein family which selectively bind to syntaxin isoforms. From their initial identification, the SM proteins were known to be essential for membrane fusion, however, over the intervening decades, deciphering the precise mechanism of action of the SM proteins has proved problematic. Recent studies, investigating the interactions of munc18-1 and syntaxin1, provide an explanation for previous, apparently conflicting, observations yielding a new understanding of their cellular functions.",
keywords = "Animals, Models, Molecular, Munc18 , Protein Binding, Syntaxin 1, Exocytosis, SNARE",
author = "Smyth, {Annya M} and Duncan, {Rory R} and Colin Rickman",
year = "2010",
doi = "10.1007/s10571-010-9581-1",
language = "English",
volume = "30",
pages = "1309--13",
journal = "Cellular and Molecular Neurobiology",
issn = "0272-4340",
publisher = "Springer",
number = "8",

}

Munc18-1 and syntaxin1: unraveling the interactions between the dynamic duo. / Smyth, Annya M; Duncan, Rory R; Rickman, Colin.

In: Cellular and Molecular Neurobiology, Vol. 30, No. 8, 2010, p. 1309-13.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Munc18-1 and syntaxin1: unraveling the interactions between the dynamic duo

AU - Smyth, Annya M

AU - Duncan, Rory R

AU - Rickman, Colin

PY - 2010

Y1 - 2010

N2 - All neurotransmitter and hormone regulated secretory events involve the action of three soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, syntaxin, SNAP-25, and synaptobrevin. The SNARE proteins interact to form a four alpha-helical complex, involving syntaxin and SNAP-25 on the plasma membrane and synaptobrevin on the vesicular membrane, bringing the opposing membranes together, promoting bilayer merger and membrane fusion. The process of regulated secretion is an adaptation of the membrane fusion events which occur at multiple steps throughout the intracellular trafficking pathway, in each case catalyzed by SNARE protein isoforms. At all of these locations, the SNAREs are joined by a member of the Sec1p/Munc18 (SM) protein family which selectively bind to syntaxin isoforms. From their initial identification, the SM proteins were known to be essential for membrane fusion, however, over the intervening decades, deciphering the precise mechanism of action of the SM proteins has proved problematic. Recent studies, investigating the interactions of munc18-1 and syntaxin1, provide an explanation for previous, apparently conflicting, observations yielding a new understanding of their cellular functions.

AB - All neurotransmitter and hormone regulated secretory events involve the action of three soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, syntaxin, SNAP-25, and synaptobrevin. The SNARE proteins interact to form a four alpha-helical complex, involving syntaxin and SNAP-25 on the plasma membrane and synaptobrevin on the vesicular membrane, bringing the opposing membranes together, promoting bilayer merger and membrane fusion. The process of regulated secretion is an adaptation of the membrane fusion events which occur at multiple steps throughout the intracellular trafficking pathway, in each case catalyzed by SNARE protein isoforms. At all of these locations, the SNAREs are joined by a member of the Sec1p/Munc18 (SM) protein family which selectively bind to syntaxin isoforms. From their initial identification, the SM proteins were known to be essential for membrane fusion, however, over the intervening decades, deciphering the precise mechanism of action of the SM proteins has proved problematic. Recent studies, investigating the interactions of munc18-1 and syntaxin1, provide an explanation for previous, apparently conflicting, observations yielding a new understanding of their cellular functions.

KW - Animals

KW - Models, Molecular

KW - Munc18

KW - Protein Binding

KW - Syntaxin 1

KW - Exocytosis

KW - SNARE

U2 - 10.1007/s10571-010-9581-1

DO - 10.1007/s10571-010-9581-1

M3 - Article

VL - 30

SP - 1309

EP - 1313

JO - Cellular and Molecular Neurobiology

T2 - Cellular and Molecular Neurobiology

JF - Cellular and Molecular Neurobiology

SN - 0272-4340

IS - 8

ER -