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A more recent version of this article appeared on June 1, 2002
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Submitted on August 16, 2001
Revised on December 31, 2001
Accepted on February 1, 2002
1 Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China
2 Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China (present address: Division of Medical Oncology, Box 1128, Mount Sinai Medical Center, One Gustave L. Levy Place, New York, NY 10029)
3 School and Department of Medicine, University of California, San Diego, La Jolla, CA 92095, USA
4 Department of Oncology, University of Western Ontario, London, Ontario, Canada N6A 4L6
5 Molecular Oncology Group, Department of Medicine, McGill University Health Center, Montreal, Quebec, Canada H3A 1A1
* Corresponding author. E-mail address: bczgwu{at}ust.hk.
In this report, we identify myogenin as an important transcriptional target under the control of three intracellular signaling pathways, namely the p38 MAP kinase (MAPK), calcium-calmodulin-dependent protein kinase (CaMK), and calcineurin-mediated pathways, during skeletal muscle differentiation. Three cis-elements (i.e., the E box, MEF2 and MEF3 sites) in the proximal myogenin promoter in response to these three pathways are defined. MyoD, MEF2s and Six proteins, the trans-activators bound to these cis-elements, are shown to be activated by these signaling pathways. Our data support a model in which all three signaling pathways act in parallel but non-redundantly to control myogenin expression. Inhibition of any one pathway will result in abolished or reduced myogenin expression and subsequent phenotypic differentiation. In addition, we demonstrate that CaMK and calcineurin fail to activate MEF2s in Rhabdomyosarcoma-derived RD cells. In the case of CaMK, we show its activation in response to differentiation signals and its effect on the cytoplasmic translocation of histone deacetylases 5 (HDAC5) are not compromised in RD cells, suggesting HDAC5 cytoplasmic translocation is necessary but not sufficient and additional signal is required in conjunction with CaMK to activate MEF2 proteins.
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