Journal
CELLULAR SIGNALLING
Volume 16, Issue 5, Pages 551-563Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2003.09.006
Keywords
CaM kinase II; myogenin; phosphorylation; muscle activity
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Funding
- NIDDK NIH HHS [R37 DK034171] Funding Source: Medline
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During development of the neuromuscular junction (NMJ), extrajunctional expression of genes, whose products are destined for the synapse, is suppressed by muscle activity. One of the best-studied examples of activity-dependent gene regulation in muscle are those encoding nicotinic acetylcholine receptor (nAChR) subunits. We recently showed that nAChR gene expression is inhibited by calcium/ calmodulin-dependent protein kinase II (CaMKII) and CaMKII inhibitors block activity-dependent suppression of these genes. Here we report results investigating the mechanism by which CaMKII suppresses nAChR gene expression. We show that the muscle helix-loop-helix transcription factor, myogenin, is necessary for activity-dependent control of nAChR gene expression in cultured rat myotubes and is a substrate for CaMKII both in vitro and in vivo. CaMKII phosphorylation of myogenin is induced by muscle activity and this phosphorylation influences DNA binding and transactivation. Thus we have identified a signaling mechanism by which muscle activity controls nAChR gene expression in developing muscle. (C) 2003 Elsevier Inc. All rights reserved.
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