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Article: Inhibitory phosphorylation of cyclin-dependent kinase 1 as a compensatory mechanism for mitosis exit

TitleInhibitory phosphorylation of cyclin-dependent kinase 1 as a compensatory mechanism for mitosis exit
Authors
Issue Date2011
Citation
Molecular and Cellular Biology, 2011, v. 31, n. 7, p. 1478-1491 How to Cite?
AbstractThe 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. © 2011, American Society for Microbiology.
Persistent Identifierhttp://hdl.handle.net/10722/307109
ISSN
2023 Impact Factor: 3.2
2023 SCImago Journal Rankings: 1.452
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChow, Jeremy P.H.-
dc.contributor.authorPoon, Randy Y.C.-
dc.contributor.authorMa, Hoi Tang-
dc.date.accessioned2021-11-03T06:21:57Z-
dc.date.available2021-11-03T06:21:57Z-
dc.date.issued2011-
dc.identifier.citationMolecular and Cellular Biology, 2011, v. 31, n. 7, p. 1478-1491-
dc.identifier.issn0270-7306-
dc.identifier.urihttp://hdl.handle.net/10722/307109-
dc.description.abstractThe 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. © 2011, American Society for Microbiology.-
dc.languageeng-
dc.relation.ispartofMolecular and Cellular Biology-
dc.titleInhibitory phosphorylation of cyclin-dependent kinase 1 as a compensatory mechanism for mitosis exit-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1128/MCB.00891-10-
dc.identifier.pmid21262764-
dc.identifier.pmcidPMC3135293-
dc.identifier.scopuseid_2-s2.0-79953793743-
dc.identifier.volume31-
dc.identifier.issue7-
dc.identifier.spage1478-
dc.identifier.epage1491-
dc.identifier.eissn1098-5549-
dc.identifier.isiWOS:000288437100013-

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