title: Pho85 kinase, a cyclin-dependent kinase, regulates nuclear accumulation of the Rim101 transcription factor in the stress response of Saccharomyces cerevisiae.
abstract: The budding yeast Saccharomyces cerevisiae alters its gene expression profile in response to changing environmental conditions. The Pho85 kinase, one of the yeast cyclin-dependent kinases (CDK), is known to play an important role in the cellular response to alterations in parameters such as nutrient levels and salinity. Several genes whose expression is regulated, either directly or indirectly, by the Rim101 transcription factor become constitutively activated when Pho85 function is absent. Because Rim101 is responsible for adaptation to alkaline conditions, this observation suggests an interaction between Pho85 and Rim101 in the response to alkaline stress. We have found that Pho85 affects neither RIM101 transcription, the proteolytic processing that is required for Rim101 activation, nor Rim101 stability. Rather, Pho85 regulates the nuclear accumulation of active Rim101, possibly via phosphorylation. Additionally, we report that Pho85 and the transcription factor Pho4 are necessary for adaptation to alkaline conditions and that PTK2 activation by Pho4 is involved in this process. These findings illustrate novel roles for the regulators of the PHO system when yeast cells cope with various environmental stresses potentially threatening their survival.
authors.affiliation: Department of Microbiology and Immunology, Keio University School of Medicine, Tokyo, Japan. mas@sc.itc.keio.ac.jp
authors.forename: Masafumi
authors.initials: M
authors.lastname: Nishizawa
authors.forename: Mirai
authors.initials: M
authors.lastname: Tanigawa
authors.forename: Michio
authors.initials: M
authors.lastname: Hayashi
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Maeda
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Yazaki
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Saeki
authors.forename: Akio
authors.initials: A
authors.lastname: Toh-e
mesh_terms: D018844:Cyclin-Dependent Kinases / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D013312:Stress, Physiological / Q000235:genetics*
chemical_list: C489601:RIM101 protein, S cerevisiae; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; C522753:PTK2 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases; D018844:Cyclin-Dependent Kinases; C058605:PHO85 protein, S cerevisiae
references.citation: Mol Cell Biol. 1997 Mar;17(3):1212-23
references.pmid: 9032248
references.citation: Genes Dev. 1998 Sep 1;12(17):2673-83
references.pmid: 9732266
references.citation: Eukaryot Cell. 2008 Jun;7(6):949-57
references.pmid: 18408055
references.citation: Annu Rev Genet. 2001;35:647-72
references.pmid: 11700296
references.citation: Nat Cell Biol. 2004 Oct;6(10):997-1002
references.pmid: 15448699
references.citation: Genetics. 1997 Jan;145(1):63-73
references.pmid: 9017390
references.citation: J Biol Chem. 2002 Aug 23;277(34):31079-88
references.pmid: 12058033
references.citation: J Biol Chem. 1999 Nov 26;274(48):33859-62
references.pmid: 10567344
references.citation: J Biol Chem. 2001 Jan 19;276(3):1850-6
references.pmid: 11050096
references.citation: Yeast. 2004 Aug;21(11):903-18
references.pmid: 15334555
references.citation: Mol Cell Biol. 2002 Jul;22(14):5076-88
references.pmid: 12077337
references.citation: Genes Genet Syst. 1997 Dec;72(6):323-34
references.pmid: 9544531
references.citation: PLoS Biol. 2008 Dec 23;6(12):2817-30
references.pmid: 19108609
references.citation: Mol Cell Biol. 2000 Oct;20(20):7654-61
references.pmid: 11003661
references.citation: Mol Cell Biol. 2005 Nov;25(21):9478-90
references.pmid: 16227598
references.citation: Microbiol Rev. 1995 Jun;59(2):304-22
references.pmid: 7603412
references.citation: J Biol Chem. 2004 May 7;279(19):19698-704
references.pmid: 14993228
references.citation: Mol Cell Biol. 2003 Jan;23(1):229-37
references.pmid: 12482976
references.citation: Annu Rev Microbiol. 2004;58:425-51
references.pmid: 15487944
references.citation: Yeast. 2001 Feb;18(3):239-49
references.pmid: 11180457
references.citation: Mol Cell. 2007 Jun 8;26(5):663-74
references.pmid: 17560372
references.citation: Mol Cell. 2006 Feb 3;21(3):319-30
references.pmid: 16455487
references.citation: EMBO J. 2005 Dec 21;24(24):4271-8
references.pmid: 16308562
references.citation: Nature. 1998 Dec 3;396(6710):482-6
references.pmid: 9853758
references.citation: Eukaryot Cell. 2004 Jun;3(3):741-51
references.pmid: 15189995
references.citation: J Biol Chem. 1989 May 5;264(13):7437-46
references.pmid: 2523395
references.citation: Nature. 2002 Jul 25;418(6896):387-91
references.pmid: 12140549
references.citation: Nucleic Acids Res. 1993 Aug 11;21(16):3789-97
references.pmid: 8367297
references.citation: Trends Biochem Sci. 2002 Feb;27(2):87-93
references.pmid: 11852246
references.citation: J Biol Chem. 2007 Nov 30;282(48):34735-47
references.pmid: 17911112
references.citation: Mol Microbiol. 2002 Dec;46(5):1319-33
references.pmid: 12453218
references.citation: Yeast. 1998 Jan 30;14(2):115-32
references.pmid: 9483801
references.citation: Mol Biol Cell. 2000 Mar;11(3):915-27
references.pmid: 10712509
references.citation: Cell. 2002 Oct 18;111(2):155-8
references.pmid: 12408859
references.citation: Mol Cell Biol. 2001 Mar;21(5):1688-99
references.pmid: 11238906
references.citation: Mol Cell Biol. 2003 Jan;23(2):677-86
references.pmid: 12509465
references.citation: Cell. 2004 Dec 29;119(7):969-79
references.pmid: 15620355
references.citation: Nat Struct Mol Biol. 2006 Oct;13(10):908-14
references.pmid: 16964260