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Monitoring the Effect of Osmotic Stress on Secretory Vesicles and Exocytosis
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Munc18/Syntaxin interaction kinetics control secretory vesicle dynamics.

Colin Rickman1, Rory R Duncan1

  • 1From the Centre for Integrative Physiology, University of Edinburgh, George Square, Edinburgh EH8 9XD, Scotland, United Kingdom.

The Journal of Biological Chemistry
|September 15, 2009
PubMed
Summary
This summary is machine-generated.

Phosphorylation of syntaxin 1 at Ser(14) regulates its interaction with Munc18-1, impacting vesicle dynamics and inhibiting exocytosis. This finding reveals a novel regulatory mechanism for regulated exocytosis.

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Molecular Biology

Background:

  • Regulated exocytosis relies on SNARE proteins (syntaxin 1, SNAP-25, VAMP) and Munc18.
  • Munc18-1 interacts with syntaxin 1 via inhibitory (mode 1) and direct N-terminal binding (mode 2/3) modes.
  • The N-terminal interaction is proposed to regulate fusion priming, but its regulation and dynamic effects are unknown.

Purpose of the Study:

  • Investigate the regulation of the Munc18-1/syntaxin 1 N-terminal interaction.
  • Determine the dynamic effects of this interaction at the molecular and vesicular levels in living cells.
  • Elucidate the role of syntaxin 1 phosphorylation in exocytosis.

Main Methods:

  • Real-time imaging of syntaxin 1 and Munc18-1 association in living cells.
  • Site-directed mutagenesis to alter syntaxin 1 phosphorylation at Ser(14).
  • Electrophysiological recordings and vesicle trafficking analysis.

Main Results:

  • Syntaxin 1 phosphorylation at Ser(14) was identified as a regulator of the N-terminal interaction with Munc18-1.
  • Modification of Ser(14) altered the dynamics of the Munc18-1/syntaxin 1 interaction at the plasma membrane.
  • Destabilization of this dynamic interaction led to vesicle immobilization and inhibited exocytosis.

Conclusions:

  • Syntaxin 1 phosphorylation at Ser(14) dynamically regulates its interaction with Munc18-1.
  • This regulation is crucial for controlling vesicle trafficking and exocytosis.
  • The findings uncover a novel molecular mechanism controlling regulated exocytosis.