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dc.contributor.authorStrickfaden, Shelly Catherine
dc.contributor.authorWinters, Matthew J.
dc.contributor.authorBen-Ari, Giora
dc.contributor.authorLamson, Rachel E.
dc.contributor.authorTyers, Michael D.
dc.contributor.authorPryciak, Peter M.
dc.date2022-08-11T08:08:49.000
dc.date.accessioned2022-08-23T16:09:16Z
dc.date.available2022-08-23T16:09:16Z
dc.date.issued2007-02-10
dc.date.submitted2009-01-13
dc.identifier.citationCell. 2007 Feb 9;128(3):519-31. <a href="http://dx.doi.org/10.1016/j.cell.2006.12.032">Link to article on publisher's site</a>
dc.identifier.issn0092-8674 (Print)
dc.identifier.doi10.1016/j.cell.2006.12.032
dc.identifier.pmid17289571
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32651
dc.description.abstractYeast cells arrest in the G1 phase of the cell cycle upon exposure to mating pheromones. As cells commit to a new cycle, G1 CDK activity (Cln/CDK) inhibits signaling through the mating MAPK cascade. Here we show that the target of this inhibition is Ste5, the MAPK cascade scaffold protein. Cln/CDK disrupts Ste5 membrane localization by phosphorylating a cluster of sites that flank a small, basic, membrane-binding motif in Ste5. Effective inhibition of Ste5 signaling requires multiple phosphorylation sites and a substantial accumulation of negative charge, which suggests that Ste5 acts as a sensor for high G1 CDK activity. Thus, Ste5 is an integration point for both external and internal signals. When Ste5 cannot be phosphorylated, pheromone triggers an aberrant arrest of cells outside G1 either in the presence or absence of the CDK-inhibitor protein Far1. These findings define a mechanism and physiological benefit of restricting antiproliferative signaling to G1.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17289571&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.cell.2006.12.032
dc.subjectAdaptor Proteins, Signal Transducing; Cell Cycle Proteins; Cell Differentiation; Cell Membrane; Cyclin-Dependent Kinases; Cyclins; Electrostatics; *G1 Phase; *MAP Kinase Signaling System; Mitogen-Activated Protein Kinases; Phosphorylation; Protein Structure, Tertiary; Repressor Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA mechanism for cell-cycle regulation of MAP kinase signaling in a yeast differentiation pathway
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume128
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1210
dc.identifier.contextkey693120
html.description.abstract<p>Yeast cells arrest in the G1 phase of the cell cycle upon exposure to mating pheromones. As cells commit to a new cycle, G1 CDK activity (Cln/CDK) inhibits signaling through the mating MAPK cascade. Here we show that the target of this inhibition is Ste5, the MAPK cascade scaffold protein. Cln/CDK disrupts Ste5 membrane localization by phosphorylating a cluster of sites that flank a small, basic, membrane-binding motif in Ste5. Effective inhibition of Ste5 signaling requires multiple phosphorylation sites and a substantial accumulation of negative charge, which suggests that Ste5 acts as a sensor for high G1 CDK activity. Thus, Ste5 is an integration point for both external and internal signals. When Ste5 cannot be phosphorylated, pheromone triggers an aberrant arrest of cells outside G1 either in the presence or absence of the CDK-inhibitor protein Far1. These findings define a mechanism and physiological benefit of restricting antiproliferative signaling to G1.</p>
dc.identifier.submissionpathgsbs_sp/1210
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages519-31


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