메뉴 건너뛰기




Volumn 363, Issue 4, 2007, Pages 942-947

Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe

Author keywords

MAP kinase; Methylglyoxal; Protein phosphatase; PTP1B; Schizosaccharomyces pombe; Signal transduction

Indexed keywords

METHYLGLYOXAL; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; SPC1 ENZYME; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 35148840655     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.09.071     Document Type: Article
Times cited : (6)

References (28)
  • 2
    • 0029954766 scopus 로고    scopus 로고
    • Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe
    • Degols G., Shiozaki K., and Russell P. Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe. Mol. Cell. Biol. 16 (1996) 2870-2877
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2870-2877
    • Degols, G.1    Shiozaki, K.2    Russell, P.3
  • 3
    • 0033821210 scopus 로고    scopus 로고
    • Cooperative regulation of DOG2, encoding 2-deoxyglucose-6-phosphate phosphatase, by Snf1 kinase and the high-osmolarity glycerol-mitogen-activated protein kinase cascade in stress responses of Saccharomyces cerevisiae
    • Tsujimoto Y., Izawa S., and Inoue Y. Cooperative regulation of DOG2, encoding 2-deoxyglucose-6-phosphate phosphatase, by Snf1 kinase and the high-osmolarity glycerol-mitogen-activated protein kinase cascade in stress responses of Saccharomyces cerevisiae. J. Bacteriol. 182 (2000) 5121-5126
    • (2000) J. Bacteriol. , vol.182 , pp. 5121-5126
    • Tsujimoto, Y.1    Izawa, S.2    Inoue, Y.3
  • 4
    • 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. The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion. Free Radic. Biol. Med. 29 (2000) 1043-1050
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 1043-1050
    • Singh, K.K.1
  • 5
    • 33646192122 scopus 로고    scopus 로고
    • A downshift in temperature activates the high osmolarity glycerol (HOG) pathway, which determines freeze tolerance in Saccharomyces cerevisiae
    • Panadero J., Pallotti C., Rodríguez-Vargas S., Randez-Gil F., and Prieto J.A. A downshift in temperature activates the high osmolarity glycerol (HOG) pathway, which determines freeze tolerance in Saccharomyces cerevisiae. J. Biol. Chem. 281 (2006) 4638-4645
    • (2006) J. Biol. Chem. , vol.281 , pp. 4638-4645
    • Panadero, J.1    Pallotti, C.2    Rodríguez-Vargas, S.3    Randez-Gil, F.4    Prieto, J.A.5
  • 6
    • 33745658629 scopus 로고    scopus 로고
    • Activation of the HOG pathway upon cold stress in Saccharomyces cerevisiae
    • Hayashi M., and Maeda T. Activation of the HOG pathway upon cold stress in Saccharomyces cerevisiae. J. Biochem. (Tokyo) 139 (2006) 797-803
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 797-803
    • Hayashi, M.1    Maeda, T.2
  • 7
    • 12844281130 scopus 로고    scopus 로고
    • Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crz1-mediated pathway in Saccharomyces cerevisiae
    • Maeta K., Izawa S., and Inoue Y. Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crz1-mediated pathway in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 253-260
    • (2005) J. Biol. Chem. , vol.280 , pp. 253-260
    • Maeta, K.1    Izawa, S.2    Inoue, Y.3
  • 8
    • 27744536479 scopus 로고    scopus 로고
    • The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe
    • Zuin A., Vivancos A.P., Sansó M., Takatsume Y., Ayté J., Inoue Y., and Hidalgo E. The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe. J. Biol. Chem. 280 (2005) 36708-36713
    • (2005) J. Biol. Chem. , vol.280 , pp. 36708-36713
    • Zuin, A.1    Vivancos, A.P.2    Sansó, M.3    Takatsume, Y.4    Ayté, J.5    Inoue, Y.6    Hidalgo, E.7
  • 9
    • 33646918686 scopus 로고    scopus 로고
    • Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe
    • Takatsume Y., Izawa S., and Inoue Y. Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 281 (2006) 9086-9092
    • (2006) J. Biol. Chem. , vol.281 , pp. 9086-9092
    • Takatsume, Y.1    Izawa, S.2    Inoue, Y.3
  • 10
    • 0029933943 scopus 로고    scopus 로고
    • Effect of methylglyoxal on human leukaemia 60 cell growth: modification of DNA G1 growth arrest and induction of apoptosis
    • Kang Y., Edwards L., and Thornalley P. Effect of methylglyoxal on human leukaemia 60 cell growth: modification of DNA G1 growth arrest and induction of apoptosis. Leuk. Res. 20 (1996) 397-405
    • (1996) Leuk. Res. , vol.20 , pp. 397-405
    • Kang, Y.1    Edwards, L.2    Thornalley, P.3
  • 11
    • 0028853680 scopus 로고
    • Methylglyoxal and regulation of its metabolism in microorganisms
    • Inoue Y., and Kimura A. Methylglyoxal and regulation of its metabolism in microorganisms. Adv. Microbiol. Phys. 37 (1995) 177-227
    • (1995) Adv. Microbiol. Phys. , vol.37 , pp. 177-227
    • Inoue, Y.1    Kimura, A.2
  • 12
    • 0029860016 scopus 로고    scopus 로고
    • Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae
    • Inoue Y., and Kimura A. Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 25958-25965
    • (1996) J. Biol. Chem. , vol.271 , pp. 25958-25965
    • Inoue, Y.1    Kimura, A.2
  • 13
    • 2442666359 scopus 로고    scopus 로고
    • Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe
    • Takatsume Y., Izawa S., and Inoue Y. Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe. Arch. Microbiol. 181 (2004) 371-377
    • (2004) Arch. Microbiol. , vol.181 , pp. 371-377
    • Takatsume, Y.1    Izawa, S.2    Inoue, Y.3
  • 14
    • 4544374631 scopus 로고    scopus 로고
    • Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis
    • Maeta K., Izawa S., Okazaki S., Kuge S., and Inoue Y. Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis. Mol. Cell. Biol. 24 (2004) 8753-8764
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8753-8764
    • Maeta, K.1    Izawa, S.2    Okazaki, S.3    Kuge, S.4    Inoue, Y.5
  • 15
    • 0035816581 scopus 로고    scopus 로고
    • Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation
    • Bell M., Capone R., Pashtan I., Levitzki A., and Engelberg D. Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation. J. Biol. Chem. 276 (2001) 25351-25358
    • (2001) J. Biol. Chem. , vol.276 , pp. 25351-25358
    • Bell, M.1    Capone, R.2    Pashtan, I.3    Levitzki, A.4    Engelberg, D.5
  • 16
    • 0029089795 scopus 로고
    • Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast
    • Millar J., Buck V., and Wilkinson M. Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast. Genes Dev. 9 (1995) 2117-2130
    • (1995) Genes Dev. , vol.9 , pp. 2117-2130
    • Millar, J.1    Buck, V.2    Wilkinson, M.3
  • 17
    • 0030806899 scopus 로고    scopus 로고
    • Stress-activated protein kinase pathway in cell cycle control of fission yeast
    • Shiozaki K., and Russell P. Stress-activated protein kinase pathway in cell cycle control of fission yeast. Methods Enzymol. 283 (1997) 506-520
    • (1997) Methods Enzymol. , vol.283 , pp. 506-520
    • Shiozaki, K.1    Russell, P.2
  • 19
    • 0020463759 scopus 로고
    • Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate
    • Swarup G., Cohen S., and Garbers D. Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate. Biochem. Biophys. Res. Commun. 107 (1982) 1104-1109
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1104-1109
    • Swarup, G.1    Cohen, S.2    Garbers, D.3
  • 20
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J., and Tanner K. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.1    Tanner, K.2
  • 21
    • 0030887994 scopus 로고    scopus 로고
    • Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1
    • Lohse D., Denu J., Santoro N., and Dixon J. Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry 36 (1997) 4568-4575
    • (1997) Biochemistry , vol.36 , pp. 4568-4575
    • Lohse, D.1    Denu, J.2    Santoro, N.3    Dixon, J.4
  • 22
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., and Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 (2005) 183-189
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 23
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, Andersen J., Myers M., Meng T., Hinks J., Tonks N., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen1    Andersen, J.2    Myers, M.3    Meng, T.4    Hinks, J.5    Tonks, N.6    Barford, D.7
  • 24
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R., Congreve M., Tisi D., Carr R., and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423 (2003) 773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 25
    • 0027256148 scopus 로고
    • Glyoxalase II: molecular characteristics, kinetics and mechanism
    • Vander Jagt D. Glyoxalase II: molecular characteristics, kinetics and mechanism. Biochem. Soc. Trans. 21 (1993) 522-527
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 522-527
    • Vander Jagt, D.1
  • 26
    • 0032939905 scopus 로고    scopus 로고
    • Metformin reduces systemic methylglyoxal levels in type 2 diabetes
    • Beisswenger P., Howell S., Touchette A., Lal S., and Szwergold B. Metformin reduces systemic methylglyoxal levels in type 2 diabetes. Diabetes 48 (1999) 198-202
    • (1999) Diabetes , vol.48 , pp. 198-202
    • Beisswenger, P.1    Howell, S.2    Touchette, A.3    Lal, S.4    Szwergold, B.5
  • 27
    • 0028292698 scopus 로고
    • Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications
    • McLellan, Thornalley P., Benn J., and Sonksen P. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. (Lond.) 87 (1994) 21-29
    • (1994) Clin. Sci. (Lond.) , vol.87 , pp. 21-29
    • McLellan1    Thornalley, P.2    Benn, J.3    Sonksen, P.4
  • 28
    • 0037341276 scopus 로고    scopus 로고
    • Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression
    • Carlson, Koterski S., Sciotti R., Poccard G., and Rondinone C. Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression. Diabetes 52 (2003) 634-641
    • (2003) Diabetes , vol.52 , pp. 634-641
    • Carlson1    Koterski, S.2    Sciotti, R.3    Poccard, G.4    Rondinone, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.