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dc.contributor.authorLamson, Rachel E.
dc.contributor.authorTakahashi, Satoe
dc.contributor.authorWinters, Matthew J.
dc.contributor.authorPryciak, Peter M.
dc.date2022-08-11T08:09:00.000
dc.date.accessioned2022-08-23T16:14:58Z
dc.date.available2022-08-23T16:14:58Z
dc.date.issued2006-03-21
dc.date.submitted2008-10-15
dc.identifier.citationCurr Biol. 2006 Mar 21;16(6):618-23. <a href="http://dx.doi.org/10.1016/j.cub.2006.02.060 ">Link to article on publisher's site</a>
dc.identifier.issn0960-9822 (Print)
dc.identifier.doi10.1016/j.cub.2006.02.060
dc.identifier.pmid16546088
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33989
dc.description.abstractDistinct MAP kinase pathways in yeast share several signaling components , including the PAK Ste20 and the MAPKKK Ste11, yet signaling is specific. Mating pheromones trigger an initial step in which Ste20 activates Ste11 , and this requires plasma membrane recruitment of the MAP kinase cascade scaffold protein, Ste5 . Here, we demonstrate an additional role for Ste5 membrane localization. Once Ste11 is activated, signaling through the mating pathway remains minimal but is substantially amplified when Ste5 is recruited to the membrane either by the Gbetagamma dimer or by direct membrane targeting, even to internal membranes. Ste11 signaling is also amplified by Ste5 oligomerization and by a hyperactivating mutation in the Ste7 binding region of Ste5. We suggest a model in which membrane recruitment of Ste5 concentrates its binding partners and thereby amplifies signaling through the kinase cascade. We find similar behavior in the osmotically responsive HOG pathway. Remarkably, while both pheromone and hyperosmotic stimuli amplify signaling from constitutively active Ste11, the resulting signaling output remains pathway specific. These findings suggest a common mode of regulation in which pathway stimuli both initiate and amplify MAP kinase cascade signaling. The regulation of rate-limiting steps that lie after a branchpoint from shared components helps ensure signaling specificity.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16546088&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.cub.2006.02.060
dc.subjectAdaptor Proteins, Signal Transducing; Cell Membrane; Intracellular Membranes; MAP Kinase Signaling System; Models, Biological; Mutation; Plasmids; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleDual role for membrane localization in yeast MAP kinase cascade activation and its contribution to signaling fidelity
dc.typeJournal Article
dc.source.journaltitleCurrent biology : CB
dc.source.volume16
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/641
dc.identifier.contextkey651111
html.description.abstract<p>Distinct MAP kinase pathways in yeast share several signaling components , including the PAK Ste20 and the MAPKKK Ste11, yet signaling is specific. Mating pheromones trigger an initial step in which Ste20 activates Ste11 , and this requires plasma membrane recruitment of the MAP kinase cascade scaffold protein, Ste5 . Here, we demonstrate an additional role for Ste5 membrane localization. Once Ste11 is activated, signaling through the mating pathway remains minimal but is substantially amplified when Ste5 is recruited to the membrane either by the Gbetagamma dimer or by direct membrane targeting, even to internal membranes. Ste11 signaling is also amplified by Ste5 oligomerization and by a hyperactivating mutation in the Ste7 binding region of Ste5. We suggest a model in which membrane recruitment of Ste5 concentrates its binding partners and thereby amplifies signaling through the kinase cascade. We find similar behavior in the osmotically responsive HOG pathway. Remarkably, while both pheromone and hyperosmotic stimuli amplify signaling from constitutively active Ste11, the resulting signaling output remains pathway specific. These findings suggest a common mode of regulation in which pathway stimuli both initiate and amplify MAP kinase cascade signaling. The regulation of rate-limiting steps that lie after a branchpoint from shared components helps ensure signaling specificity.</p>
dc.identifier.submissionpathgsbs_sp/641
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages618-23


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