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Guiding AlphaFold to predict how Munc13-1 opens Syntaxin-1.

Madhurima Chattopadhyay1,2,3, Junjie Xu1,2,3, Josep Rizo1,2,3

  • 1Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.

FEBS Open Bio
|May 28, 2026
PubMed
Summary
This summary is machine-generated.

Munc13-1 opens syntaxin-1, a key step in neurotransmitter release, but the mechanism was unclear. Using AlphaFold with a destabilized syntaxin-1 fragment revealed its open conformation, suggesting a novel mechanism for this crucial process.

Keywords:
AlphaFoldMunc13SNAREsSyntaxinconformational changeneurotransmitter release

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Structural Biology

Background:

  • SNARE proteins (syntaxin-1, synaptobrevin, SNAP-25) mediate neurotransmitter release via SNARE complex formation.
  • Munc18-1 and Munc13-1 regulate SNARE complex assembly, a process critical for synaptic vesicle fusion.
  • Munc13-1's role in opening syntaxin-1 is essential for neurotransmitter release but mechanistically undefined.

Purpose of the Study:

  • To elucidate the molecular mechanism by which Munc13-1 opens syntaxin-1.
  • To obtain structural insights into the Munc13-1-syntaxin-1 interaction.
  • To explore the utility of AlphaFold in predicting structures of kinetic intermediates.

Main Methods:

  • Computational modeling using AlphaFold.
  • Analysis of Munc13-1-syntaxin-1 complexes using full-length and truncated syntaxin-1 fragments.
  • Structural prediction of protein-protein interactions.

Main Results:

  • AlphaFold initially predicted Munc13-1-syntaxin-1 complexes with syntaxin-1 in a closed conformation.
  • Using a syntaxin-1 fragment destabilizing the closed conformation, AlphaFold generated a model of Munc13-1 bound to an open syntaxin-1.
  • This model provides a potential mechanism for Munc13-1-mediated syntaxin-1 opening and aligns with experimental data.

Conclusions:

  • The judicious selection of protein fragments can enable AlphaFold to predict structures of transient states in complex biological processes.
  • The predicted open syntaxin-1 conformation offers a testable hypothesis for Munc13-1's catalytic function in neurotransmitter release.
  • This study highlights a strategy for advancing structural understanding of dynamic protein interactions.