Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells

U. Nili; H. de Wit; A. Gulyas-Kovacs; R.F.G. Toonen; J.B. Sorensen; M. Verhage; U. Ashery

doi:10.1016/j.neuroscience.2006.08.014

Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells

U. Nili, H. de Wit, A. Gulyas-Kovacs, R.F.G. Toonen, J.B. Sorensen, M. Verhage, U. Ashery

Functional Genomics

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Activation of protein kinase C (PKC) after robust stimulation is necessary for vesicle pool replenishment in secretory cells. Here we studied the contribution of a prominent downstream PKC target, Munc18-1, to this process in bovine chromaffin cells. In these cells, both activation of endogenous PKC and overexpressing of Munc18-1 promote vesicle pool replenishment after an extensive stimulation. In order to study the physiological relevance of PKC-dependent Munc18-1 phosphorylation, we generated two Munc18-1 phospho-mutants; one that mimics a constitutively PKC-phosphorylated Munc18-1 (i.e. a phosphomimetic mutant; Munc18-1

Original language	English
Pages (from-to)	487-500
Number of pages	14
Journal	Neuroscience
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/j.neuroscience.2006.08.014
Publication status	Published - 2006

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10.1016/j.neuroscience.2006.08.014

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title = "Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells",

abstract = "Activation of protein kinase C (PKC) after robust stimulation is necessary for vesicle pool replenishment in secretory cells. Here we studied the contribution of a prominent downstream PKC target, Munc18-1, to this process in bovine chromaffin cells. In these cells, both activation of endogenous PKC and overexpressing of Munc18-1 promote vesicle pool replenishment after an extensive stimulation. In order to study the physiological relevance of PKC-dependent Munc18-1 phosphorylation, we generated two Munc18-1 phospho-mutants; one that mimics a constitutively PKC-phosphorylated Munc18-1 (i.e. a phosphomimetic mutant; Munc18-1",

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T1 - Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells

AU - Nili, U.

AU - de Wit, H.

AU - Gulyas-Kovacs, A.

AU - Toonen, R.F.G.

AU - Sorensen, J.B.

AU - Verhage, M.

AU - Ashery, U.

PY - 2006

Y1 - 2006

N2 - Activation of protein kinase C (PKC) after robust stimulation is necessary for vesicle pool replenishment in secretory cells. Here we studied the contribution of a prominent downstream PKC target, Munc18-1, to this process in bovine chromaffin cells. In these cells, both activation of endogenous PKC and overexpressing of Munc18-1 promote vesicle pool replenishment after an extensive stimulation. In order to study the physiological relevance of PKC-dependent Munc18-1 phosphorylation, we generated two Munc18-1 phospho-mutants; one that mimics a constitutively PKC-phosphorylated Munc18-1 (i.e. a phosphomimetic mutant; Munc18-1

AB - Activation of protein kinase C (PKC) after robust stimulation is necessary for vesicle pool replenishment in secretory cells. Here we studied the contribution of a prominent downstream PKC target, Munc18-1, to this process in bovine chromaffin cells. In these cells, both activation of endogenous PKC and overexpressing of Munc18-1 promote vesicle pool replenishment after an extensive stimulation. In order to study the physiological relevance of PKC-dependent Munc18-1 phosphorylation, we generated two Munc18-1 phospho-mutants; one that mimics a constitutively PKC-phosphorylated Munc18-1 (i.e. a phosphomimetic mutant; Munc18-1

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DO - 10.1016/j.neuroscience.2006.08.014

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VL - 143

SP - 487

EP - 500

JO - Neuroscience

JF - Neuroscience

IS - 2

ER -

Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells

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