| pubmed-article:21262764 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0080054 | lld:lifeskim |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0026255 | lld:lifeskim |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:21262764 | lifeskim:mentions | umls-concept:C0337094 | lld:lifeskim |
| pubmed-article:21262764 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:21262764 | pubmed:dateCreated | 2011-3-17 | lld:pubmed |
| pubmed-article:21262764 | pubmed:abstractText | The current paradigm states that exit from mitosis is triggered by the ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) acting in concert with an activator called CDC20. While this has been well established for a number of systems, the evidence of a critical role of CDC20 in somatic cells is not unequivocal. In this study, we reexamined whether mitotic exit can occur properly after CDC20 is depleted. Using single-cell analysis, we found that CDC20 depletion with small interfering RNAs (siRNAs) significantly impaired the degradation of APC/C substrates and delayed mitotic exit in various cancer cell lines. The recruitment of cyclin B1 to the core APC/C was defective after CDC20 downregulation. Nevertheless, CDC20-depleted cells were still able to complete mitosis, albeit requiring twice the normal time. Intriguingly, a high level of cyclin-dependent kinase 1 (CDK1)-inhibitory phosphorylation was induced during mitotic exit in CDC20-depleted cells. The expression of an siRNA-resistant CDC20 rescued both the mitotic exit delay and the CDK1-inhibitory phosphorylation. Moreover, the expression of a nonphosphorylatable CDK1 mutant or the downregulation of WEE1 and MYT1 abolished mitotic exit in CDC20-depleted cells. These findings indicate that, in the absence of sufficient APC/C activity, an alternative mechanism that utilized the classic inhibitory phosphorylation of CDK1 could mediate mitotic exit. | lld:pubmed |
| pubmed-article:21262764 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21262764 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21262764 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21262764 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21262764 | pubmed:issn | 1098-5549 | lld:pubmed |
| pubmed-article:21262764 | pubmed:author | pubmed-author:PoonRandy Y... | lld:pubmed |
| pubmed-article:21262764 | pubmed:author | pubmed-author:ChowJeremy... | lld:pubmed |
| pubmed-article:21262764 | pubmed:author | pubmed-author:MaHoi TangHT | lld:pubmed |
| pubmed-article:21262764 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21262764 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:21262764 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21262764 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21262764 | pubmed:pagination | 1478-91 | lld:pubmed |
| pubmed-article:21262764 | pubmed:dateRevised | 2011-10-3 | lld:pubmed |
| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
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| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
| pubmed-article:21262764 | pubmed:meshHeading | pubmed-meshheading:21262764... | lld:pubmed |
| pubmed-article:21262764 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21262764 | pubmed:articleTitle | Inhibitory phosphorylation of cyclin-dependent kinase 1 as a compensatory mechanism for mitosis exit. | lld:pubmed |
| pubmed-article:21262764 | pubmed:affiliation | Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong. | lld:pubmed |
| pubmed-article:21262764 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21262764 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:983 | entrezgene:pubmed | pubmed-article:21262764 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21262764 | lld:entrezgene |
