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

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

Cite this

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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.",

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.",

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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.

M3 - Article

SN - 0300-5127

VL - 33

SP - 1341

EP - 1344

JO - Biochemical Society transactions

JF - Biochemical Society transactions

ER -