Regulation of exocytosis by protein kinase C.
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-25 and Munc18 by PKC regulates distinct stages of exocytosis.
Morgan
A
A
The Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Liverpool, UK. amorgan@liv.ac.uk
Burgoyne
R D
RD
Barclay
J W
JW
Craig
T J
TJ
Prescott
G R
GR
Ciufo
L F
LF
Evans
G J O
GJ
Graham
M E
ME
D000818:Animals; D005089:Exocytosis / Q000502:physiology*; D051938:Munc18 Proteins / Q000378:metabolism; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D050825:Synaptosomal-Associated Protein 25 / Q000378:metabolism
D051938:Munc18 Proteins; D050825:Synaptosomal-Associated Protein 25; D011493:Protein Kinase C