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A dynamic template complex mediates Munc18-chaperoned SNARE assembly.

Jie Yang1, Huaizhou Jin1, Yihao Liu1

  • 1Department of Cell Biology, Yale School of Medicine, New Haven, CT 06511.

Proceedings of the National Academy of Sciences of the United States of America
|December 1, 2022
PubMed
Summary
This summary is machine-generated.

Munc18 proteins chaperone SNARE complex assembly for membrane fusion. This study reveals how Munc18-1 and Munc18-3 form dynamic template complexes, ensuring specific and efficient protein interactions for exocytosis.

Keywords:
Munc18 proteinsSNARE assemblymembrane fusionoptical tweezerstemplate complexes

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biophysics

Background:

  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediate membrane fusion, crucial for exocytosis.
  • Munc18 proteins act as chaperones in SNARE complex assembly, but the mechanism remains unclear.
  • Template complexes involving Munc18 and SNAREs are proposed to facilitate assembly.

Purpose of the Study:

  • To investigate the structure, dynamics, and function of Munc18-chaperoned SNARE template complexes.
  • To elucidate the molecular mechanisms underlying specific SNARE assembly.
  • To understand the role of Munc18-1 and Munc18-3 in synaptic vesicle and GLUT4 vesicle fusion.

Main Methods:

  • Utilized optical tweezers to study the dynamics of SNARE template complexes.
  • Analyzed the structural contributions of syntaxin-1 and Munc18-1 regions.
  • Compared the binding specificities of different SNARE-binding proteins (SNAP-25, SNAP-23).

Main Results:

  • The synaptic template complex transitions to an activated state for efficient SNAP-25 binding.
  • Syntaxin-1's linker region and Munc18-1's disordered loop are critical for template complex function and stability.
  • The GLUT4 template complex shows a strong preference for SNAP-23 over SNAP-25.

Conclusions:

  • Munc18-chaperoned template complexes are dynamic and mediate efficient, specific SNARE assembly.
  • The observed specificity in binding suggests distinct roles for Munc18-1 and Munc18-3 in different exocytotic pathways.
  • This work provides mechanistic insights into the regulation of membrane fusion.