| pubmed-article:10942602 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0079183 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:10942602 | lifeskim:mentions | umls-concept:C0205087 | lld:lifeskim |
| pubmed-article:10942602 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10942602 | pubmed:dateCreated | 2000-9-20 | lld:pubmed |
| pubmed-article:10942602 | pubmed:abstractText | 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). | lld:pubmed |
| pubmed-article:10942602 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10942602 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10942602 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10942602 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10942602 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:LeibovitchS... | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:LeibovitchM... | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:FernandezAA | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:MeijerLL | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:DucommunBB | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:KitzmannMM | lld:pubmed |
| pubmed-article:10942602 | pubmed:author | pubmed-author:TintignacL... | lld:pubmed |
| pubmed-article:10942602 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10942602 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10942602 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10942602 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:10942602 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10942602 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10942602 | pubmed:pagination | 300-7 | lld:pubmed |
| pubmed-article:10942602 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10942602 | pubmed:meshHeading | pubmed-meshheading:10942602... | lld:pubmed |
| pubmed-article:10942602 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10942602 | pubmed:articleTitle | Cyclin E-cdk2 phosphorylation promotes late G1-phase degradation of MyoD in muscle cells. | lld:pubmed |
| pubmed-article:10942602 | pubmed:affiliation | Laboratoire de Génétique Oncologique, Institut Gustave Roussy, Villejuif, 94805, France. | lld:pubmed |
| pubmed-article:10942602 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10942602 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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