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• W2091301979 abstract "Proliferating myoblasts already express MyoD before the induction of differentiation. Overexpression of MyoD in normal and transformed cell lines was shown to block cells from entering S phase, suggesting that the MyoD growth suppressive effect must be tightly controlled in growing myoblasts. Here we show that during G1 phase, but not in G2, MyoD abundance is down-regulated by the ubiquitin-proteasome pathway through phosphorylation of serine 200. Roscovitine, a specific inhibitor of cyclin-Cdk2 complexes, prevents both phosphorylation and degradation of MyoD in G1. Inhibition of the ubiquitin-dependent proteasome pathway by MG132 results in stabilization of MyoD-wt, with little effect on a MyoD mutant where serine 200 is replaced by an alanine. Our results show that MyoD Ser200 is the substrate for phosphorylation by cyclin E-Cdk2 stimulating its degradation by the ubiquitin-proteasome system which controls MyoD levels in G1. Phosphorylation/degradation of MyoD at the end of G1 thus represents the regulatory checkpoint in growing myoblasts allowing progression into S phase in a manner similar to the recently examplified cdk2-phosphorylation/degradation of p27(Kip1)." @default.
• W2091301979 created "2016-06-24" @default.
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• W2091301979 date "2000-08-01" @default.
• W2091301979 modified "2023-10-18" @default.
• W2091301979 title "Cyclin E–Cdk2 Phosphorylation Promotes Late G1-Phase Degradation of MyoD in Muscle Cells" @default.
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• W2091301979 doi "https://doi.org/10.1006/excr.2000.4973" @default.
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