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

Research output: Contribution to JournalArticleAcademicpeer-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 languageEnglish
Pages (from-to)487-500
Number of pages14
JournalNeuroscience
Volume143
Issue number2
DOIs
Publication statusPublished - 2006

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