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Volumn 1, Issue 2, 2002, Pages 163-173

Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress

Author keywords

[No Author keywords available]

Indexed keywords

SUS SCROFA;

EID: 0036548318     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.1.2.163-173.2002     Document Type: Article
Times cited : (182)

References (46)
  • 1
    • 0028302033 scopus 로고
    • GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway
    • Albertyn, J., S. Hohmann, J. M. Thevelein, and B. A. Prior. 1994. GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway. Mol. Cell. Biol. 14:4135-4144.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4135-4144
    • Albertyn, J.1    Hohmann, S.2    Thevelein, J.M.3    Prior, B.A.4
  • 2
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel, B., I. Wunning, and A. Varshavsky. 1990. The recognition component of the N-end rule pathway. EMBO J. 9:3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 3
    • 0033552609 scopus 로고    scopus 로고
    • A novel regulatory mechanism of MAP kinase activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase
    • Blanco-Aparicio, C., J. Torres, and R. Pulido. 1999. A novel regulatory mechanism of MAP kinase activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. J. Cell Biol. 147:1129-1136.
    • (1999) J. Cell Biol. , vol.147 , pp. 1129-1136
    • Blanco-Aparicio, C.1    Torres, J.2    Pulido, R.3
  • 4
    • 0028145758 scopus 로고
    • The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual specificity phosphatase action
    • Bott, C. M., S. G. Thorneycroft, and C. J. Marshall. 1994. The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual specificity phosphatase action. FEBS Lett. 352:201-205.
    • (1994) FEBS Lett. , vol.352 , pp. 201-205
    • Bott, C.M.1    Thorneycroft, S.G.2    Marshall, C.J.3
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 0029561101 scopus 로고
    • A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway
    • Davenport, K. R., M. Sohaskey, Y. Kamada, D. E. Levin, and M. C. Gustin. 1995. A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway. J. Biol. Chem. 270:30157-30161.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30157-30161
    • Davenport, K.R.1    Sohaskey, M.2    Kamada, Y.3    Levin, D.E.4    Gustin, M.C.5
  • 7
    • 0028157519 scopus 로고
    • MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae
    • Doi, K., A. Gartner, G. Ammerer, B. Errede, H. Shinkawa, K. Sugimoto, and K. Matsumoto. 1994. MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. EMBO J. 13:61-70.
    • (1994) EMBO J. , vol.13 , pp. 61-70
    • Doi, K.1    Gartner, A.2    Ammerer, G.3    Errede, B.4    Shinkawa, H.5    Sugimoto, K.6    Matsumoto, K.7
  • 8
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain, M., R. J. Dohmen, F. Levy, and A. Varshavsky. 1996. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15:4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 9
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 10
    • 0031736099 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways in the yeast Saccharomyces cerevisiae
    • Gustin, M. C., J. Albertyn, M. Alexander, and K. Davenport. 1998. Mitogen-activated protein kinase pathways in the yeast Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 62:1264-1300.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1264-1300
    • Gustin, M.C.1    Albertyn, J.2    Alexander, M.3    Davenport, K.4
  • 11
    • 0029965551 scopus 로고    scopus 로고
    • The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: Isolation of a FUS3 mutant that is insensitive to the repression mechanism
    • Hall, J. P., v. Cherkasova, E. Elion, M. C. Gustin, and E. Winter. 1996. The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: isolation of a FUS3 mutant that is insensitive to the repression mechanism. Mol. Cell. Biol. 16:6715-6723.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6715-6723
    • Hall, J.P.1    Cherkasova, V.2    Elion, E.3    Gustin, M.C.4    Winter, E.5
  • 12
    • 0031472233 scopus 로고    scopus 로고
    • A protein-aceous gene regulatory thermometer in Salmonella
    • Hurme, R., K. D. Berndt, S. J. Normark, and M. Rhen. 1997. A protein-aceous gene regulatory thermometer in Salmonella. Cell 90:55-64.
    • (1997) Cell , vol.90 , pp. 55-64
    • Hurme, R.1    Berndt, K.D.2    Normark, S.J.3    Rhen, M.4
  • 13
    • 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
  • 14
    • 11944273348 scopus 로고
    • The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response
    • Kamada, Y., U. S. Jung, J. Piotrowski, and D. E. Levin. 1995. The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes Dev. 9:1559-1571.
    • (1995) Genes Dev. , vol.9 , pp. 1559-1571
    • Kamada, Y.1    Jung, U.S.2    Piotrowski, J.3    Levin, D.E.4
  • 16
    • 0031900740 scopus 로고    scopus 로고
    • Signal transduction through MAP kinase cascades
    • Lewis, T. S., P. S. Shapiro, and N. G. Ahn. 1998. Signal transduction through MAP kinase cascades. Adv. Cancer Res. 74:49-139.
    • (1998) Adv. Cancer Res. , vol.74 , pp. 49-139
    • Lewis, T.S.1    Shapiro, P.S.2    Ahn, N.G.3
  • 17
    • 0018426004 scopus 로고
    • Thermosensory transduction in Escherichia coli: Inhibition of the thermoresponse by L-serine
    • Maeda, K., and Y. Imae. 1979. Thermosensory transduction in Escherichia coli: inhibition of the thermoresponse by L-serine. Proc. Natl. Acad. Sci. USA 76:91-95.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 91-95
    • Maeda, K.1    Imae, Y.2
  • 18
    • 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
  • 19
    • 0027202272 scopus 로고
    • Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae
    • Maeda, T., A. Y. Tsai, and H. Saito. 1993. Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:5408-5417.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5408-5417
    • Maeda, T.1    Tsai, A.Y.2    Saito, H.3
  • 20
    • 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
  • 21
    • 0032519787 scopus 로고    scopus 로고
    • Puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila
    • Martin-Blanco, E., A. Gampel, J. Ring, K. Virdee, N. Kirov, A. M. Tolkovsky, and A. Martinez-Arias. 1998. puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila. Genes Dev. 12:557-570.
    • (1998) Genes Dev. , vol.12 , pp. 557-570
    • Martin-Blanco, E.1    Gampel, A.2    Ring, J.3    Virdee, K.4    Kirov, N.5    Tolkovsky, A.M.6    Martinez-Arias, A.7
  • 22
    • 0034658668 scopus 로고    scopus 로고
    • Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast
    • Mattison, C. P., and I. M. Ota. 2000. Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast. Genes Dev. 14:1229-1235.
    • (2000) Genes Dev. , vol.14 , pp. 1229-1235
    • Mattison, C.P.1    Ota, I.M.2
  • 23
    • 0032718779 scopus 로고    scopus 로고
    • Differential regulation of the cell wall integrity mitogen-activated protein kinase pathway in budding yeast by the protein tyrosine phosphatases Ptp2 and Ptp3
    • Mattison, C. P., S. S. Spencer, K. A. Kresge, J. Lee, and I. M. Ota. 1999. Differential regulation of the cell wall integrity mitogen-activated protein kinase pathway in budding yeast by the protein tyrosine phosphatases Ptp2 and Ptp3. Mol. Cell. Biol. 19:7651-7660.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7651-7660
    • Mattison, C.P.1    Spencer, S.S.2    Kresge, K.A.3    Lee, J.4    Ota, I.M.5
  • 24
    • 0021237174 scopus 로고
    • Conditional inversion of the thermoresponse in Escherichia coli
    • Mizuno, T., and Y. Imae. 1984. Conditional inversion of the thermoresponse in Escherichia coli. J. Bacteriol. 159:360-367.
    • (1984) J. Bacteriol. , vol.159 , pp. 360-367
    • Mizuno, T.1    Imae, Y.2
  • 25
    • 0023034916 scopus 로고
    • Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions
    • Myers, A. M., A. Tzagoloff, D. M. Kinney, and C. J. Lusty. 1986. Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene 45:299-310.
    • (1986) Gene , vol.45 , pp. 299-310
    • Myers, A.M.1    Tzagoloff, A.2    Kinney, D.M.3    Lusty, C.J.4
  • 26
    • 0026060881 scopus 로고
    • Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli
    • Nara, T., L. Lee, and Y. Imae. 1991. Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli. J. Bacteriol. 173:1120-1124.
    • (1991) J. Bacteriol. , vol.173 , pp. 1120-1124
    • Nara, T.1    Lee, L.2    Imae, Y.3
  • 27
    • 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
  • 28
    • 0032939637 scopus 로고    scopus 로고
    • The extracellular domain of the Saccharomyces cerevisiae Sln1p membrane osmolarity sensor is necessary for kinase activity
    • Ostrander, D. B., and J. A. Gorman. 1999. The extracellular domain of the Saccharomyces cerevisiae Sln1p membrane osmolarity sensor is necessary for kinase activity. J. Bacteriol. 181:2527-2534.
    • (1999) J. Bacteriol. , vol.181 , pp. 2527-2534
    • Ostrander, D.B.1    Gorman, J.A.2
  • 29
    • 0026535446 scopus 로고
    • A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant
    • Ota, I. M., and A. Varshavsky. 1992. A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant. Proc. Natl. Acad. Sci. USA 89:2355-2359.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2355-2359
    • Ota, I.M.1    Varshavsky, A.2
  • 30
    • 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
  • 31
    • 0030815562 scopus 로고    scopus 로고
    • Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: Scaffold role of Pbs2p MAPKK
    • Posas, F., and H. Saito. 1997. Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK. Science 276:1702-1705.
    • (1997) Science , vol.276 , pp. 1702-1705
    • Posas, F.1    Saito, H.2
  • 32
    • 0031658234 scopus 로고    scopus 로고
    • Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway
    • Posas, F., E. A. Witten, and H. Saito. 1998. Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway. Mol. Cell. Biol. 18:5788-5796.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5788-5796
    • Posas, F.1    Witten, E.A.2    Saito, H.3
  • 33
    • 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
  • 34
    • 0034282495 scopus 로고    scopus 로고
    • Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway
    • Raitt, D. C., F. Posas, and H. Saito. 2000. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. EMBO J. 19:4623-4631.
    • (2000) EMBO J. , vol.19 , pp. 4623-4631
    • Raitt, D.C.1    Posas, F.2    Saito, H.3
  • 35
    • 0034282235 scopus 로고    scopus 로고
    • Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42
    • Reiser, V., S. M. Salah, and G. Ammerer. 2000. Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42. Nat. Cell Biol. 2:620-627.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 620-627
    • Reiser, V.1    Salah, S.M.2    Ammerer, G.3
  • 36
    • 0033193930 scopus 로고    scopus 로고
    • Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase
    • Saxena, M., S. Williams, K. Tasken, and T. Mustelin. 1999. Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase. Nat. Cell Biol. 1:305-311.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 305-311
    • Saxena, M.1    Williams, S.2    Tasken, K.3    Mustelin, T.4
  • 37
    • 0029563651 scopus 로고
    • Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast
    • Shiozaki, K., and P. Russell. 1995. Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature 378:739-743.
    • (1995) Nature , vol.378 , pp. 739-743
    • Shiozaki, K.1    Russell, P.2
  • 38
    • 0034669693 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion
    • Singh, K. K. 2000. The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion. Free Radic. Biol. Med. 29:1043-1050.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 1043-1050
    • Singh, K.K.1
  • 39
    • 0033928677 scopus 로고    scopus 로고
    • Response of Saccharomyces cerevisiae to severe osmotic stress: Evidence for a novel activation mechanism of the HOG MAP kinase pathway
    • Van Wuytswinkel, O., V. Reiser, M. Siderius, M. C. Kelders, G. Ammerer, H. Ruis, and W. H. Mager. 2000. Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway. Mol. Microbiol. 37:382-397.
    • (2000) Mol. Microbiol. , vol.37 , pp. 382-397
    • Van Wuytswinkel, O.1    Reiser, V.2    Siderius, M.3    Kelders, M.C.4    Ammerer, G.5    Ruis, H.6    Mager, W.H.7
  • 40
    • 0034750802 scopus 로고    scopus 로고
    • Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1
    • Warmka, J., J. Hanneman, J. Lee, D. Amin, and I. Ota. 2001. Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1. Mol. Cell. Biol. 21:51-60.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 51-60
    • Warmka, J.1    Hanneman, J.2    Lee, J.3    Amin, D.4    Ota, I.5
  • 41
    • 0030957532 scopus 로고    scopus 로고
    • Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway
    • Watanabe, Y., G. Takaesu, M. Hagiwara, K. Irie, and K. Matsumoto. 1997. Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Mol. Cell. Biol. 17:2615-2623.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2615-2623
    • Watanabe, Y.1    Takaesu, G.2    Hagiwara, M.3    Irie, K.4    Matsumoto, K.5
  • 42
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann, C., S. Gibson, M. B. Jarpe, and G. L. Johnson. 1999. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79:143-180.
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 43
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • Wu, C. 1995. Heat shock transcription factors: structure and regulation. Annu. Rev. Cell Dev. Biol. 11:441-469.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 441-469
    • Wu, C.1
  • 44
    • 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
  • 45
    • 0030820725 scopus 로고    scopus 로고
    • Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae
    • Zhan, X. L., R. J. Deschenes, and K. L. Guan. 1997. Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae. Genes Dev. 11:1690-1702.
    • (1997) Genes Dev. , vol.11 , pp. 1690-1702
    • Zhan, X.L.1    Deschenes, R.J.2    Guan, K.L.3
  • 46
    • 0032700045 scopus 로고    scopus 로고
    • A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 toward the Fus3 MAP kinase
    • Zhan, X. L., and K. L. Guan. 1999. A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 toward the Fus3 MAP kinase. Genes Dev. 13:2811-2827.
    • (1999) Genes Dev. , vol.13 , pp. 2811-2827
    • Zhan, X.L.1    Guan, K.L.2


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