Phorbol esters and neurotransmitter release: More than just protein kinase C?

Eugene M. Silinsky*, Timothy J. Searl

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

75 Scopus citations


This review focuses on the effects of phorbol esters and the role of phorbol ester receptors in the secretion of neurotransmitter substances. We begin with a brief background on the historical use of phorbol esters as tools to decipher the role of the enzyme protein kinase C in signal transduction cascades. Next, we illustrate the structural differences between active and inactive phorbol esters and the mechanism by which the binding of phorbol to its recognition sites (C1 domains) on a particular protein acts to translocate that protein to the membrane. We then discuss the evidence that the most important nerve terminal receptor for phorbol esters (and their endogenous counterpart diacylglycerol) is likely to be Munc13. Indeed, Munc13 and its invertebrate homologues are the main players in priming the secretory apparatus for its critical function in the exocytosis process.

Original languageEnglish (US)
Pages (from-to)1191-1201
Number of pages11
JournalBritish journal of pharmacology
Issue number7
StatePublished - Apr 2003


  • Munc13
  • Neurotransmitter release
  • Phorbol esters
  • Protein kinase C

ASJC Scopus subject areas

  • Pharmacology


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