Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release

Neuron. 1998 Jul;21(1):123-36. doi: 10.1016/s0896-6273(00)80520-6.


Munc13-1, a mammalian homolog of C. elegans unc-13p, is thought to be involved in the regulation of synaptic transmission. We now demonstrate that Munc13-1 is a presynaptic high-affinity phorbol ester and diacylglycerol receptor with ligand affinities similar to those of protein kinase C. Munc13-1 associates with the plasma membrane in response to phorbol ester binding and acts as a phorbol ester-dependent enhancer of transmitter release when overexpressed presynaptically in the Xenopus neuromuscular junction. These observations establish Munc13-1 as a novel presynaptic target of the diacylglycerol second messenger pathway that acts in parallel with protein kinase C to regulate neurotransmitter secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport / drug effects
  • Brain / metabolism
  • Caenorhabditis elegans Proteins*
  • Carrier Proteins
  • Cell Line
  • Female
  • Humans
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Nerve Tissue Proteins / physiology
  • Neuromuscular Junction / metabolism
  • Neurotransmitter Agents / metabolism*
  • Phorbol Esters / metabolism*
  • Phorbol Esters / pharmacology
  • Presynaptic Terminals / metabolism*
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Drug / metabolism*
  • Synaptic Transmission / physiology
  • Tissue Distribution
  • Xenopus / metabolism


  • Caenorhabditis elegans Proteins
  • Carrier Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Phorbol Esters
  • Receptors, Drug
  • UNC13B protein, human
  • Unc13a protein, rat
  • phorbol ester binding protein
  • phorbol ester receptor
  • Protein Kinase C