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

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

School of Biology

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	1341-1344
Number of pages	4
Journal	Biochemical Society Transactions
Volume	33
Publication status	Published - 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

Cite this

@article{2b5d53a51c324234ab9573845ac61dbf,

title = "Regulation of exocytosis by protein kinase C",

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.",

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",

author = "A Morgan and Burgoyne, {R D} and Barclay, {J W} and Craig, {T J} and Prescott, {G R} and Ciufo, {L F} and Evans, {G J O} and Graham, {M E}",

year = "2005",

month = dec,

language = "English",

volume = "33",

pages = "1341--1344",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Regulation of exocytosis by protein kinase C

AU - Morgan, A

AU - Burgoyne, R D

AU - Barclay, J W

AU - Craig, T J

AU - Prescott, G R

AU - Ciufo, L F

AU - Evans, G J O

AU - Graham, M E

PY - 2005/12

Y1 - 2005/12

N2 - 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.

AB - 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.

KW - chromaffin cell

KW - exocytosis

KW - 25 kDa synaptosome-associated protein (SNAP-25)

KW - Munc18

KW - phorbol ester

KW - protein kinase C (PKC)

KW - ADRENAL CHROMAFFIN CELLS

KW - SYNAPTOSOME-ASSOCIATED PROTEIN

KW - RELEASABLE VESICLE POOL

KW - BRAIN NERVE-TERMINALS

KW - DEPENDENT PHOSPHORYLATION

KW - DIFFERENTIAL PHOSPHORYLATION

KW - NEUROTRANSMITTER RELEASE

KW - PRESYNAPTIC PLASTICITY

KW - POSSIBLE INVOLVEMENT

KW - TRANSMITTER RELEASE

M3 - Article

SN - 0300-5127

VL - 33

SP - 1341

EP - 1344

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -

Regulation of exocytosis by protein kinase C

Abstract

Keywords

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