[HTML][HTML] Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis
JW Barclay, TJ Craig, RJ Fisher, LF Ciufo… - Journal of Biological …, 2003 - ASBMB
Protein phosphorylation by protein kinase C (PKC) has been implicated in the control of
neurotransmitter release and various forms of synaptic plasticity. The PKC substrates
responsible for phosphorylation-dependent changes in regulated exocytosisin vivo have not
been identified. Munc18a is essential for neurotransmitter release by exocytosis and can be
phosphorylated by PKCin vitro on Ser-306 and Ser-313. We demonstrate that it is
phosphorylated on Ser-313 in response to phorbol ester treatment in adrenal chromaffin …
neurotransmitter release and various forms of synaptic plasticity. The PKC substrates
responsible for phosphorylation-dependent changes in regulated exocytosisin vivo have not
been identified. Munc18a is essential for neurotransmitter release by exocytosis and can be
phosphorylated by PKCin vitro on Ser-306 and Ser-313. We demonstrate that it is
phosphorylated on Ser-313 in response to phorbol ester treatment in adrenal chromaffin …