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dc.contributor.authorArsenault, Heather E.
dc.contributor.authorRoy, Jagoree
dc.contributor.authorMapa, Claudine E.
dc.contributor.authorCyert, Martha S.
dc.contributor.authorBenanti, Jennifer A
dc.date2022-08-11T08:09:19.000
dc.date.accessioned2022-08-23T16:26:17Z
dc.date.available2022-08-23T16:26:17Z
dc.date.issued2015-10-15
dc.date.submitted2015-11-30
dc.identifier.citationMol Biol Cell. 2015 Oct 15;26(20):3570-7. doi: 10.1091/mbc.E15-07-0469. Epub 2015 Aug 12. <a href="http://dx.doi.org/10.1091/mbc.E15-07-0469">Link to article on publisher's site</a>
dc.identifier.issn1059-1524 (Linking)
dc.identifier.doi10.1091/mbc.E15-07-0469
dc.identifier.pmid26269584
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36533
dc.description.abstractCyclin-dependent kinase (Cdk1) orchestrates progression through the cell cycle by coordinating the activities of cell-cycle regulators. Although phosphatases that oppose Cdk1 are likely to be necessary to establish dynamic phosphorylation, specific phosphatases that target most Cdk1 substrates have not been identified. In budding yeast, the transcription factor Hcm1 activates expression of genes that regulate chromosome segregation and is critical for maintaining genome stability. Previously we found that Hcm1 activity and degradation are stimulated by Cdk1 phosphorylation of distinct clusters of sites. Here we show that, upon exposure to environmental stress, the phosphatase calcineurin inhibits Hcm1 by specifically removing activating phosphorylations and that this regulation is important for cells to delay proliferation when they encounter stress. Our work identifies a mechanism by which proliferative signals from Cdk1 are removed in response to stress and suggests that Hcm1 functions as a rheostat that integrates stimulatory and inhibitory signals to control cell proliferation.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=26269584&dopt=Abstract">Link to Article in PubMed</a>
dc.rights<p>© 2015 Arsenault, Roy, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</p>
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.subjectMolecular Biology
dc.titleHcm1 integrates signals from Cdk1 and calcineurin to control cell proliferation
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume26
dc.source.issue20
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1027&amp;context=mccb_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/mccb_pubs/27
dc.identifier.contextkey7884827
refterms.dateFOA2022-08-23T16:26:18Z
html.description.abstract<p>Cyclin-dependent kinase (Cdk1) orchestrates progression through the cell cycle by coordinating the activities of cell-cycle regulators. Although phosphatases that oppose Cdk1 are likely to be necessary to establish dynamic phosphorylation, specific phosphatases that target most Cdk1 substrates have not been identified. In budding yeast, the transcription factor Hcm1 activates expression of genes that regulate chromosome segregation and is critical for maintaining genome stability. Previously we found that Hcm1 activity and degradation are stimulated by Cdk1 phosphorylation of distinct clusters of sites. Here we show that, upon exposure to environmental stress, the phosphatase calcineurin inhibits Hcm1 by specifically removing activating phosphorylations and that this regulation is important for cells to delay proliferation when they encounter stress. Our work identifies a mechanism by which proliferative signals from Cdk1 are removed in response to stress and suggests that Hcm1 functions as a rheostat that integrates stimulatory and inhibitory signals to control cell proliferation.</p>
dc.identifier.submissionpathmccb_pubs/27
dc.contributor.departmentDepartment of Molecular, Cell and Cancer Biology
dc.source.pages3570-7


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<p>© 2015 Arsenault, Roy, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</p>
Except where otherwise noted, this item's license is described as <p>© 2015 Arsenault, Roy, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</p>