[HTML][HTML] β phorbol ester-and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs
JS Rhee, A Betz, S Pyott, K Reim, F Varoqueaux… - Cell, 2002 - cell.com
JS Rhee, A Betz, S Pyott, K Reim, F Varoqueaux, I Augustin, D Hesse, TC Südhof…
Cell, 2002•cell.comMunc13-1 is a presynaptic protein with an essential role in synaptic vesicle priming. It
contains a diacylglycerol (DAG)/β phorbol ester binding C 1 domain and is a potential target
of the DAG second messenger pathway that may act in parallel with PKCs. Using genetically
modified mice that express a DAG/β phorbol ester binding-deficient Munc13-1 H567K
variant instead of the wild-type protein, we determined the relative contribution of PKCs and
Munc13-1 to DAG/β phorbol ester-dependent regulation of neurotransmitter release. We …
contains a diacylglycerol (DAG)/β phorbol ester binding C 1 domain and is a potential target
of the DAG second messenger pathway that may act in parallel with PKCs. Using genetically
modified mice that express a DAG/β phorbol ester binding-deficient Munc13-1 H567K
variant instead of the wild-type protein, we determined the relative contribution of PKCs and
Munc13-1 to DAG/β phorbol ester-dependent regulation of neurotransmitter release. We …
Abstract
Munc13-1 is a presynaptic protein with an essential role in synaptic vesicle priming. It contains a diacylglycerol (DAG)/β phorbol ester binding C1 domain and is a potential target of the DAG second messenger pathway that may act in parallel with PKCs. Using genetically modified mice that express a DAG/β phorbol ester binding-deficient Munc13-1H567K variant instead of the wild-type protein, we determined the relative contribution of PKCs and Munc13-1 to DAG/β phorbol ester-dependent regulation of neurotransmitter release. We show that Munc13s are the main presynaptic DAG/β phorbol ester receptors in hippocampal neurons. Modulation of Munc13-1 activity by second messengers via the DAG/β phorbol ester binding C1 domain is essential for use-dependent alterations of synaptic efficacy and survival.
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