A minimal domain responsible for Munc13 activity

Nat Struct Mol Biol. 2005 Nov;12(11):1017-8. doi: 10.1038/nsmb1001.

Abstract

Munc13 proteins are essential in neurotransmitter release, controlling the priming of synaptic vesicles to a release-ready state. The sequences responsible for this priming activity are unknown. Here we identify a large alpha-helical domain of mammalian Munc13-1 that is autonomously folded and is sufficient to rescue the total arrest in neurotransmitter release observed in hippocampal neurons lacking Munc13s.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, Gel
  • Computational Biology
  • Excitatory Postsynaptic Potentials
  • Exocytosis / genetics
  • Exocytosis / physiology*
  • Gene Expression*
  • Hippocampus / metabolism*
  • Mice
  • Mice, Knockout
  • Nerve Tissue Proteins / genetics*
  • Nerve Tissue Proteins / metabolism
  • Neurons / drug effects
  • Neurons / metabolism*
  • Neurotransmitter Agents / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Folding
  • Protein Structure, Secondary / genetics
  • Protein Structure, Tertiary
  • Rats
  • Structure-Activity Relationship
  • Sucrose / pharmacology

Substances

  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Unc13h1 protein, rat
  • Sucrose