| pubmed-article:17373649 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17373649 | lifeskim:mentions | umls-concept:C0385333 | lld:lifeskim |
| pubmed-article:17373649 | lifeskim:mentions | umls-concept:C1155874 | lld:lifeskim |
| pubmed-article:17373649 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:17373649 | lifeskim:mentions | umls-concept:C1655265 | lld:lifeskim |
| pubmed-article:17373649 | lifeskim:mentions | umls-concept:C0052418 | lld:lifeskim |
| pubmed-article:17373649 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17373649 | pubmed:dateCreated | 2007-6-4 | lld:pubmed |
| pubmed-article:17373649 | pubmed:abstractText | Timely induction of cyclin B1 controls mitotic entry, whereas its proteolysis is essential for mitotic exit. By contrast, cyclin B1 transcription is repressed during G(2) arrest induced by DNA damage. The p38 mitogen-activated protein kinase is involved in the G(2) checkpoint; yet, its impact on cyclin B1 protein levels remains unclear. Here we show that untimely proteolysis of cyclin B1 following p38 activation contributes to G(2) checkpoint. Exposing early G(2) cells to arsenite impeded cyclin B1 protein accumulation, Cdk1 activation, and G(2)-to-M progression. Conversely, cyclin B1 was non-degradable in late G(2) and mitotic cells after arsenite. Cyclin B1 proteolysis was enhanced by arsenite in early G(2) and asynchronous cells. This rapid destruction of cyclin B1 was mediated via the ubiquitin-proteasome pathway probably in a Cdc20 and Cdh1 independent mechanism. Under arsenite, inhibition of p38 activation or depletion of p38alpha suppressed cyclin B1 ubiquitination and proteolysis, while forced expression of MKK6-p38 accelerated these events. Inactivation of p38 in arsenite-treated early G(2) cells allowed G(2)-to-M progression, blocked apoptosis, increased cell viability, and decreased micronucleus formation. Thus, p38 signaling pathway triggering cyclin B1 proteolysis after arsenite may play an important role in connecting G(2) arrest with apoptosis or genome instability. | lld:pubmed |
| pubmed-article:17373649 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17373649 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17373649 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17373649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17373649 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17373649 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17373649 | pubmed:issn | 0021-9541 | lld:pubmed |
| pubmed-article:17373649 | pubmed:author | pubmed-author:YangJia-LingJ... | lld:pubmed |
| pubmed-article:17373649 | pubmed:author | pubmed-author:LiJu-PiJP | lld:pubmed |
| pubmed-article:17373649 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17373649 | pubmed:volume | 212 | lld:pubmed |
| pubmed-article:17373649 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17373649 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17373649 | pubmed:pagination | 481-8 | lld:pubmed |
| pubmed-article:17373649 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:17373649 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17373649 | pubmed:articleTitle | Cyclin B1 proteolysis via p38 MAPK signaling participates in G2 checkpoint elicited by arsenite. | lld:pubmed |
| pubmed-article:17373649 | pubmed:affiliation | Molecular Carcinogenesis Laboratory, Institute of Biotechnology and Department of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan. | lld:pubmed |
| pubmed-article:17373649 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17373649 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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