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J Biol Chem. 2003 Apr 25;278(17):15297-303. Epub 2003 Feb 12.

Phosphorylation motifs regulating the stability and function of myocyte enhancer factor 2A.

Author information

1
Department of Biology, the Centre for Research in Mass Spectrometry, and the Department of Chemistry, York University, Toronto M3J 1P3, Canada.

Abstract

The phosphorylation status of the myocyte enhancer factor 2 (MEF2) transcriptional regulator is a critical determinant of its tissue-specific functions. However, due to the complexity of its phosphorylation pattern in vivo, a systematic inventory of MEF2A phosphorylation sites in mammalian cells has been difficult to obtain. We employed modern affinity purification techniques, combined with mass spectrometry, to identify several novel MEF2 phosphoacceptor sites. These include an evolutionarily conserved KSP motif, which we show is important in regulating the stability and function of MEF2A. Also, an indirect pathway in which a protein kinase casein kinase 2 phosphoacceptor site is phosphorylated by activation of p38 MAPK signaling was documented. Together, these findings identify several novel aspects of MEF2 regulation that may prove important in the control of gene expression in neuronal and muscle cells.

PMID:
12586839
DOI:
10.1074/jbc.M211312200
[Indexed for MEDLINE]
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