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Volumn 28, Issue 17, 2008, Pages 5172-5183

Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL; HOG1 PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; SSK1 PROTEIN; SSK2 PROTEIN; UNCLASSIFIED DRUG; YPD1 PROTEIN;

EID: 50249126692     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00589-08     Document Type: Article
Times cited : (55)

References (45)
  • 1
    • 34249007243 scopus 로고    scopus 로고
    • Requirement for the polarisome and formin function in Ssk2p-mediated actin recovery from osmotic stress in Saccharomyces cerevisiae
    • Bettinger, B. T., M. G. Clark, and D. C. Amberg. 2007. Requirement for the polarisome and formin function in Ssk2p-mediated actin recovery from osmotic stress in Saccharomyces cerevisiae. Genetics 175:1637- 1648.
    • (2007) Genetics , vol.175 , pp. 1637-1648
    • Bettinger, B.T.1    Clark, M.G.2    Amberg, D.C.3
  • 2
    • 0034025395 scopus 로고    scopus 로고
    • Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1
    • Bilsland-Marchesan, E., J. Ariño, H. Saito, P. Sunnerhagen, and F. Posas. 2000. Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1. Mol. Cell. Biol. 20:3887-3895.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 3887-3895
    • Bilsland-Marchesan, E.1    Ariño, J.2    Saito, H.3    Sunnerhagen, P.4    Posas, F.5
  • 5
    • 5444253797 scopus 로고    scopus 로고
    • Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1
    • Escote, X., M. Zapater, J. Clotet, and F. Posas. 2004. Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1. Nat. Cell Biol. 6:997-1002.
    • (2004) Nat. Cell Biol , vol.6 , pp. 997-1002
    • Escote, X.1    Zapater, M.2    Clotet, J.3    Posas, F.4
  • 6
    • 0028227829 scopus 로고
    • Cloning vectors for the synthesis of epitope-tagged, truncated and chimeric proteins in Saccharomyces cerevisiae
    • Foreman, P. K., and R. W. Davis. 1994. Cloning vectors for the synthesis of epitope-tagged, truncated and chimeric proteins in Saccharomyces cerevisiae. Gene 144:63-68.
    • (1994) Gene , vol.144 , pp. 63-68
    • Foreman, P.K.1    Davis, R.W.2
  • 7
    • 34248205790 scopus 로고    scopus 로고
    • Bacterial response regulators: Versatile regulatory strategies from common domains
    • Gao, R., T. R. Mack, and A. M. Stock. 2007. Bacterial response regulators: versatile regulatory strategies from common domains. Trends Biochem. Sci. 32:225-234.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 225-234
    • Gao, R.1    Mack, T.R.2    Stock, A.M.3
  • 9
    • 0034624879 scopus 로고    scopus 로고
    • The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
    • Halkides, C. J., M. M. McEvoy, E. Casper, P. Matsumura, K. Volz, and F. W. Dahlquist. 2000. The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry 39:5280-5286.
    • (2000) Biochemistry , vol.39 , pp. 5280-5286
    • Halkides, C.J.1    McEvoy, M.M.2    Casper, E.3    Matsumura, P.4    Volz, K.5    Dahlquist, F.W.6
  • 11
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann, S. 2002. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66:300-372.
    • (2002) Microbiol. Mol. Biol. Rev , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 12
    • 0030760722 scopus 로고    scopus 로고
    • Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1
    • Jacoby, T., H. Flanagan, A. Faykin, A. G. Seto, C. Mattison, and I. Ota. 1997. Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1. J. Biol. Chem. 272:17749-17755.
    • (1997) J. Biol. Chem , vol.272 , pp. 17749-17755
    • Jacoby, T.1    Flanagan, H.2    Faykin, A.3    Seto, A.G.4    Mattison, C.5    Ota, I.6
  • 13
    • 0034461243 scopus 로고    scopus 로고
    • Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain
    • Janiak-Spens, F., D. P. Sparling, and A. H. West. 2000. Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. J. Bacteriol. 182:6673-6678.
    • (2000) J. Bacteriol , vol.182 , pp. 6673-6678
    • Janiak-Spens, F.1    Sparling, D.P.2    West, A.H.3
  • 14
    • 0032948810 scopus 로고    scopus 로고
    • Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins
    • Janiak-Spens, F., J. M. Sparling, M. Gurfinkel, and A. H. West. 1999. Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins. J. Bacteriol. 181:411-417.
    • (1999) J. Bacteriol , vol.181 , pp. 411-417
    • Janiak-Spens, F.1    Sparling, J.M.2    Gurfinkel, M.3    West, A.H.4
  • 15
    • 0029028962 scopus 로고
    • Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor
    • Maeda, T., M. Takekawa, and H. Saito. 1995. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 269:554-558.
    • (1995) Science , vol.269 , pp. 554-558
    • Maeda, T.1    Takekawa, M.2    Saito, H.3
  • 16
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • Maeda, T., S. M. Wurgler-Murphy, and H. Saito. 1994. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369:242-245.
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 18
    • 34147210229 scopus 로고    scopus 로고
    • Activation of MTK1/MEKK4 by GADD45 through induced N-C dissociation and dimerization-mediated trans autophosphorylation of the MTK1 kinase domain
    • Miyake, Z., M. Takekawa, Q. Ge, and H. Saito. 2007. Activation of MTK1/MEKK4 by GADD45 through induced N-C dissociation and dimerization-mediated trans autophosphorylation of the MTK1 kinase domain. Mol. Cell. Biol. 27:2765-2776.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2765-2776
    • Miyake, Z.1    Takekawa, M.2    Ge, Q.3    Saito, H.4
  • 19
    • 0031982205 scopus 로고    scopus 로고
    • His-Asp phosphotransfer signal transduction
    • Mizuno, T. 1998. His-Asp phosphotransfer signal transduction. J. Biochem. 123:555-563.
    • (1998) J. Biochem , vol.123 , pp. 555-563
    • Mizuno, T.1
  • 20
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg, D., R. Müller, and M. Funk. 1994. Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res. 22:5767-5768.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Müller, R.2    Funk, M.3
  • 21
    • 0032530170 scopus 로고    scopus 로고
    • The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae
    • O'Rourke, S. M., and I. Herskowitz. 1998. The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae. Genes Dev. 12:2874-2886.
    • (1998) Genes Dev , vol.12 , pp. 2874-2886
    • O'Rourke, S.M.1    Herskowitz, I.2
  • 22
    • 0027507956 scopus 로고
    • A yeast protein similar to bacterial two-component regulators
    • Ota, I. M., and A. Varshavsky. 1993. A yeast protein similar to bacterial two-component regulators. Science 262:566-569.
    • (1993) Science , vol.262 , pp. 566-569
    • Ota, I.M.1    Varshavsky, A.2
  • 23
    • 14844346486 scopus 로고    scopus 로고
    • A common docking site for response regulators on the yeast phosphorelay protein YPD1
    • Porter, S. W., and A. H. West. 2005. A common docking site for response regulators on the yeast phosphorelay protein YPD1. Biochem. Biophys. Res. Commun. 1748:138-145.
    • (2005) Biochem. Biophys. Res. Commun , vol.1748 , pp. 138-145
    • Porter, S.W.1    West, A.H.2
  • 24
    • 0038375049 scopus 로고    scopus 로고
    • Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p
    • Porter, S. W., Q. Xu, and A. H. West. 2003. Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p. Eukaryot. Cell 2:27-33.
    • (2003) Eukaryot. Cell , vol.2 , pp. 27-33
    • Porter, S.W.1    Xu, Q.2    West, A.H.3
  • 25
    • 0032473427 scopus 로고    scopus 로고
    • Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator
    • Posas, F., and H. Saito. 1998. Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator. EMBO J. 17:1385-1394.
    • (1998) EMBO J , vol.17 , pp. 1385-1394
    • Posas, F.1    Saito, H.2
  • 26
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor
    • Posas, F., S. M. Wurgler-Murphy, T. Maeda, E. A. Witten, T. C. Thai, and H. Saito. 1996. Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor. Cell 86:865-875.
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 27
    • 0038153182 scopus 로고    scopus 로고
    • Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure
    • Reiser, V., D. C. Raitt, and H. Saito. 2003. Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. J. Cell Biol. 161:1035-1040.
    • (2003) J. Cell Biol , vol.161 , pp. 1035-1040
    • Reiser, V.1    Raitt, D.C.2    Saito, H.3
  • 28
    • 0033887436 scopus 로고    scopus 로고
    • A tale of two components: A novel kinase and a regulatory switch
    • Robinson, V. L., D. R. Buckler, and A. M. Stock. 2000. A tale of two components: a novel kinase and a regulatory switch. Nat. Struct. Biol. 7:626-633.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 626-633
    • Robinson, V.L.1    Buckler, D.R.2    Stock, A.M.3
  • 30
    • 0042691653 scopus 로고    scopus 로고
    • Phosphorelay-regulated degradation of the yeast Ssk1p response regulator by the ubiquitin-proteasome system
    • Sato, N., H. Kawahara, A. Toh-e, and T. Maeda. 2003. Phosphorelay-regulated degradation of the yeast Ssk1p response regulator by the ubiquitin-proteasome system. Mol. Cell. Biol. 23:6662-6671.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 6662-6671
    • Sato, N.1    Kawahara, H.2    Toh-e, A.3    Maeda, T.4
  • 31
    • 0033527581 scopus 로고    scopus 로고
    • Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1 from Saccharomyces cerevisiae
    • Song, H. K., J. Y. Lee, M. G. Lee, J. Moon, K. Min, J. K. Yang, and S. W. Suh. 1999. Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1 from Saccharomyces cerevisiae. J. Mol. Biol. 293:753-761.
    • (1999) J. Mol. Biol , vol.293 , pp. 753-761
    • Song, H.K.1    Lee, J.Y.2    Lee, M.G.3    Moon, J.4    Min, K.5    Yang, J.K.6    Suh, S.W.7
  • 34
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 35
    • 0032514967 scopus 로고    scopus 로고
    • A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK
    • Takekawa, M., and H. Saito. 1998. A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK. Cell 95:521-530.
    • (1998) Cell , vol.95 , pp. 521-530
    • Takekawa, M.1    Saito, H.2
  • 36
    • 0042313963 scopus 로고    scopus 로고
    • A docking site determining specificity of Pbs2 MAPKK for Ssk2/Ssk22 MAPKKKs in the yeast HOG pathway
    • Tatebayashi, K., M. Takekawa, and H. Saito. 2003. A docking site determining specificity of Pbs2 MAPKK for Ssk2/Ssk22 MAPKKKs in the yeast HOG pathway. EMBO J. 22:3624-3634.
    • (2003) EMBO J , vol.22 , pp. 3624-3634
    • Tatebayashi, K.1    Takekawa, M.2    Saito, H.3
  • 37
    • 34547780646 scopus 로고    scopus 로고
    • Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway
    • Tatebayashi, K., K. Tanaka, H.-Y. Yang, K. Yamamoto, Y. Matsushita, T. Tomida, M. Imai, and H. Saito. 2007. Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway. EMBO J. 26:3521-3533.
    • (2007) EMBO J , vol.26 , pp. 3521-3533
    • Tatebayashi, K.1    Tanaka, K.2    Yang, H.-Y.3    Yamamoto, K.4    Matsushita, Y.5    Tomida, T.6    Imai, M.7    Saito, H.8
  • 38
    • 33746313417 scopus 로고    scopus 로고
    • Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway
    • Tatebayashi, K., K. Yamamoto, K. Tanaka, T. Tomida, T. Maruoka, E. Kasukawa, and H. Saito. 2006. Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway. EMBO J. 25:3033-3044.
    • (2006) EMBO J , vol.25 , pp. 3033-3044
    • Tatebayashi, K.1    Yamamoto, K.2    Tanaka, K.3    Tomida, T.4    Maruoka, T.5    Kasukawa, E.6    Saito, H.7
  • 39
    • 0035826689 scopus 로고    scopus 로고
    • Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast
    • Teige, M., E. Scheikl, V. Reiser, H. Ruis, and G. Ammerer. 2001. Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast. Proc. Natl. Acad. Sci. USA 98:5625-5630.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5625-5630
    • Teige, M.1    Scheikl, E.2    Reiser, V.3    Ruis, H.4    Ammerer, G.5
  • 40
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-angstrom resolution
    • Volz, K., and P. Matsumura. 1991. Crystal structure of Escherichia coli CheY refined at 1.7-angstrom resolution. J. Biol. Chem. 266:15511-15519.
    • (1991) J. Biol. Chem , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 41
    • 0031027466 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases
    • Wurgler-Murphy, S. M., T. Maeda, E. A. Witten, and H. Saito. 1997. Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases. Mol. Cell. Biol. 17:1289-1297.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 1289-1297
    • Wurgler-Murphy, S.M.1    Maeda, T.2    Witten, E.A.3    Saito, H.4
  • 42
    • 0344436666 scopus 로고    scopus 로고
    • The yeast YPD1/SLN1 complex: Insights into molecular recognition in two-component signaling systems
    • Xu, Q., S. W. Porter, and A. H. West. 2003. The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure 11:1569-1581.
    • (2003) Structure , vol.11 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3
  • 43
    • 0033536688 scopus 로고    scopus 로고
    • Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1
    • Xu, Q., and A. H. West. 1999. Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1. J. Mol. Biol. 292:1039-1050.
    • (1999) J. Mol. Biol , vol.292 , pp. 1039-1050
    • Xu, Q.1    West, A.H.2
  • 44
    • 0037769208 scopus 로고    scopus 로고
    • Actin recovery and bud emergence in osmotically stressed cells requires the conserved actin interacting mitogen-activated protein kinase kinase kinase Ssk2p/MTK1 and the scaffold protein Spa2p
    • Yuzyuk, T., and D. C. Amberg. 2003. Actin recovery and bud emergence in osmotically stressed cells requires the conserved actin interacting mitogen-activated protein kinase kinase kinase Ssk2p/MTK1 and the scaffold protein Spa2p. Mol. Biol. Cell 14:3013-3026.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3013-3026
    • Yuzyuk, T.1    Amberg, D.C.2
  • 45
    • 0036679163 scopus 로고    scopus 로고
    • The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress
    • Yuzyuk, T., M. Foehr, and D. C. Amberg. 2002. The MEK kinase Ssk2p promotes actin cytoskeleton recovery after osmotic stress. Mol. Biol. Cell 13:2869-2880.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2869-2880
    • Yuzyuk, T.1    Foehr, M.2    Amberg, D.C.3


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