Regulation of exocytosis by protein kinase C

A Morgan, R D Burgoyne, J W Barclay, T J Craig, G R Prescott, L F Ciufo, G J O Evans, M E Graham

Research output: Contribution to journalArticlepeer-review

81 Citations (Scopus)

Abstract

PKC (protein kinase C) has been known for many years to modulate regulated exocytosis in a wide variety of cell types. in neurons and neuroendocrine cells, PKC regulates several different stages of the exocytotic process, suggesting that these multiple actions of PKC are mediated by phosphorylation of distinct protein targets. In recent years, a variety of exocytotic proteins have been identified as PKC substrates, the best characterized of which are SNAP-25 (25 kDa synaptosome-associated protein) and Munc18. In the present study, we review recent evidence suggesting that site-specific phosphorylation of SNAP-2S and Munc18 by PKC regulates distinct stages of exocytosis.

Original languageEnglish
Pages (from-to)1341-1344
Number of pages4
JournalBiochemical Society Transactions
Volume33
Publication statusPublished - Dec 2005

Keywords

  • chromaffin cell
  • exocytosis
  • 25 kDa synaptosome-associated protein (SNAP-25)
  • Munc18
  • phorbol ester
  • protein kinase C (PKC)
  • ADRENAL CHROMAFFIN CELLS
  • SYNAPTOSOME-ASSOCIATED PROTEIN
  • RELEASABLE VESICLE POOL
  • BRAIN NERVE-TERMINALS
  • DEPENDENT PHOSPHORYLATION
  • DIFFERENTIAL PHOSPHORYLATION
  • NEUROTRANSMITTER RELEASE
  • PRESYNAPTIC PLASTICITY
  • POSSIBLE INVOLVEMENT
  • TRANSMITTER RELEASE

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