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Volumn 288, Issue 32, 2013, Pages 23322-23330

Precisely ordered phosphorylation reactions in the p38 mitogen-activated protein (MAP) kinase cascade

Author keywords

[No Author keywords available]

Indexed keywords

HILL COEFFICIENT; IN-VITRO; LC-MS/MS; MAPK CASCADES; MITOGEN ACTIVATED PROTEIN KINASE; ORDER OF REACTION; P38 MAPK; PHOSPHORYLATION REACTIONS;

EID: 84881404692     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462101     Document Type: Article
Times cited : (27)

References (56)
  • 1
    • 34547179997 scopus 로고    scopus 로고
    • MAP kinase pathways: The first twenty years
    • Avruch, J. (2007) MAP kinase pathways: the first twenty years. Biochim. Biophys. Acta 1773, 1150-1160
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1150-1160
    • Avruch, J.1
  • 4
    • 79952112019 scopus 로고    scopus 로고
    • The MAP kinase signaling cascades: A system of hundreds of components regulates a diverse array of physiological functions
    • Keshet, Y., and Seger, R. (2010) The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions. Methods Mol. Biol. 661, 3-38
    • (2010) Methods Mol. Biol. , vol.661 , pp. 3-38
    • Keshet, Y.1    Seger, R.2
  • 5
    • 84872392161 scopus 로고    scopus 로고
    • MAP kinase signalling cascades and transcriptional regulation
    • Yang, S. H., Sharrocks, A. D., and Whitmarsh, A. J. (2013) MAP kinase signalling cascades and transcriptional regulation. Gene 513, 1-13
    • (2013) Gene , vol.513 , pp. 1-13
    • Yang, S.H.1    Sharrocks, A.D.2    Whitmarsh, A.J.3
  • 6
    • 0027932676 scopus 로고
    • Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: Determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis
    • Mansour, S. J., Resing, K. A., Candi, J. M., Hermann, A. S., Gloor, J. W., Herskind, K. R., Wartmann, M., Davis, R. J., and Ahn, N. G. (1994) Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis. J. Biochem. 116, 304-314
    • (1994) J. Biochem. , vol.116 , pp. 304-314
    • Mansour, S.J.1    Resing, K.A.2    Candi, J.M.3    Hermann, A.S.4    Gloor, J.W.5    Herskind, K.R.6    Wartmann, M.7    Davis, R.J.8    Ahn, N.G.9
  • 7
    • 0025832605 scopus 로고
    • Multiple components in an epidermal growth factor-stimulated protein kinase cascade: In vitro activation of a myelin basic protein/ microtubule-associated protein 2 kinase
    • Ahn, N. G., Seger, R., Bratlien, R. L., Diltz, C. D., Tonks, N. K., and Krebs, E. G. (1991) Multiple components in an epidermal growth factor-stimulated protein kinase cascade: in vitro activation of a myelin basic protein/ microtubule-associated protein 2 kinase. J. Biol. Chem. 266, 4220-4227
    • (1991) J. Biol. Chem. , vol.266 , pp. 4220-4227
    • Ahn, N.G.1    Seger, R.2    Bratlien, R.L.3    Diltz, C.D.4    Tonks, N.K.5    Krebs, E.G.6
  • 8
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez, F. A., Raden, D. L., and Davis, R. J. (1991) Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J. Biol. Chem. 266, 22159-22163
    • (1991) J. Biol. Chem. , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 9
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell, J. E., Jr., and Machleder, E. M. (1998) The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280, 895-898
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 10
    • 0242515913 scopus 로고    scopus 로고
    • The JNK cascade as a biochemical switch in mammalian cells: Ultrasensitive and all-or-none responses
    • Bagowski, C. P., Besser, J., Frey, C. R., and Ferrell, J. E., Jr. (2003) The JNK cascade as a biochemical switch in mammalian cells: ultrasensitive and all-or-none responses. Curr. Biol. 13, 315-320
    • (2003) Curr. Biol. , vol.13 , pp. 315-320
    • Bagowski, C.P.1    Besser, J.2    Frey, C.R.3    Ferrell Jr., J.E.4
  • 11
    • 8644266706 scopus 로고    scopus 로고
    • Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways
    • Whitehurst, A., Cobb, M. H., and White, M. A. (2004) Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways. Mol. Cell. Biol. 24, 10145-10150
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10145-10150
    • Whitehurst, A.1    Cobb, M.H.2    White, M.A.3
  • 12
    • 18944374155 scopus 로고    scopus 로고
    • Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells
    • Mackeigan, J. P., Murphy, L. O., Dimitri, C. A., and Blenis, J. (2005) Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells. Mol. Cell. Biol. 25, 4676-4682
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4676-4682
    • Mackeigan, J.P.1    Murphy, L.O.2    Dimitri, C.A.3    Blenis, J.4
  • 14
    • 78449248996 scopus 로고    scopus 로고
    • Systematic quantification of negative feedback mechanisms in the extracellular signal-regulated kinase (ERK) signaling network
    • Cirit, M., Wang, C. C., and Haugh, J. M. (2010) Systematic quantification of negative feedback mechanisms in the extracellular signal-regulated kinase (ERK) signaling network. J. Biol. Chem. 285, 36736-36744
    • (2010) J. Biol. Chem. , vol.285 , pp. 36736-36744
    • Cirit, M.1    Wang, C.C.2    Haugh, J.M.3
  • 16
    • 77952093377 scopus 로고    scopus 로고
    • The scaffold protein Ste5 directly controls a switch-like mating decision in yeast
    • Malleshaiah, M. K., Shahrezaei, V., Swain, P. S., and Michnick, S. W. (2010) The scaffold protein Ste5 directly controls a switch-like mating decision in yeast. Nature 465, 101-105
    • (2010) Nature , vol.465 , pp. 101-105
    • Malleshaiah, M.K.1    Shahrezaei, V.2    Swain, P.S.3    Michnick, S.W.4
  • 17
    • 78650929625 scopus 로고    scopus 로고
    • Tunable signal processing in synthetic MAP kinase cascades
    • O'Shaughnessy, E. C., Palani, S., Collins, J. J., and Sarkar, C. A. (2011) Tunable signal processing in synthetic MAP kinase cascades. Cell 144, 119-131
    • (2011) Cell , vol.144 , pp. 119-131
    • O'Shaughnessy, E.C.1    Palani, S.2    Collins, J.J.3    Sarkar, C.A.4
  • 19
    • 0030746219 scopus 로고    scopus 로고
    • Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase
    • Ferrell, J. E., Jr., and Bhatt, R. R. (1997) Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase. J. Biol. Chem. 272, 19008-19016
    • (1997) J. Biol. Chem. , vol.272 , pp. 19008-19016
    • Ferrell Jr., J.E.1    Bhatt, R.R.2
  • 20
    • 33846820252 scopus 로고    scopus 로고
    • Versatile regulation of multisite protein phosphorylation by the order of phosphate processing and protein-protein interactions
    • Salazar, C., and Höfer, T. (2007) Versatile regulation of multisite protein phosphorylation by the order of phosphate processing and protein-protein interactions. FEBS J 274, 1046-1061
    • (2007) FEBS J , vol.274 , pp. 1046-1061
    • Salazar, C.1    Höfer, T.2
  • 21
    • 55549104054 scopus 로고    scopus 로고
    • Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38in different phosphorylation states
    • Zhang, Y. Y., Mei, Z. Q., Wu, J. W., and Wang, Z. X. (2008) Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38in different phosphorylation states. J. Biol. Chem. 283, 26591-26601
    • (2008) J. Biol. Chem. , vol.283 , pp. 26591-26601
    • Zhang, Y.Y.1    Mei, Z.Q.2    Wu, J.W.3    Wang, Z.X.4
  • 22
    • 53749086219 scopus 로고    scopus 로고
    • Analysis of dual phosphorylation of Hog1 MAP kinase in Saccharomyces cerevisiae using quantitative mass spectrometry
    • Choi, M. Y., Kang, G. Y., Hur, J. Y., Jung, J. W., Kim, K. P., and Park, S. H. (2008) Analysis of dual phosphorylation of Hog1 MAP kinase in Saccharomyces cerevisiae using quantitative mass spectrometry. Mol. Cells 26, 200-205
    • (2008) Mol. Cells , vol.26 , pp. 200-205
    • Choi, M.Y.1    Kang, G.Y.2    Hur, J.Y.3    Jung, J.W.4    Kim, K.P.5    Park, S.H.6
  • 23
    • 0038353123 scopus 로고    scopus 로고
    • Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vital for Hog1 biological activity
    • Bell, M., and Engelberg, D. (2003) Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vital for Hog1 biological activity. J. Biol. Chem. 278, 14603-14606
    • (2003) J. Biol. Chem. , vol.278 , pp. 14603-14606
    • Bell, M.1    Engelberg, D.2
  • 25
    • 33751392926 scopus 로고    scopus 로고
    • Structures of p38active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation
    • Diskin, R., Lebendiker, M., Engelberg, D., and Livnah, O. (2007) Structures of p38active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation. J. Mol. Biol. 365, 66-76
    • (2007) J. Mol. Biol. , vol.365 , pp. 66-76
    • Diskin, R.1    Lebendiker, M.2    Engelberg, D.3    Livnah, O.4
  • 26
    • 0028329630 scopus 로고
    • Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues
    • Zheng, C. F., and Guan, K. L. (1994) Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J. 13, 1123-1131
    • (1994) EMBO J. , vol.13 , pp. 1123-1131
    • Zheng, C.F.1    Guan, K.L.2
  • 28
    • 4644232397 scopus 로고    scopus 로고
    • Crystal structure of the TAO2 kinase domain: Activation and specificity of a Ste20p MAP3K
    • Zhou, T., Raman, M., Gao, Y., Earnest, S., Chen, Z., Machius, M., Cobb, M. H., and Goldsmith, E. J. (2004) Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K. Structure 12, 1891-1900
    • (2004) Structure , vol.12 , pp. 1891-1900
    • Zhou, T.1    Raman, M.2    Gao, Y.3    Earnest, S.4    Chen, Z.5    Machius, M.6    Cobb, M.H.7    Goldsmith, E.J.8
  • 29
    • 9144253936 scopus 로고    scopus 로고
    • The ASK1-MAP kinase cascades in mammalian stress response
    • Matsukawa, J., Matsuzawa, A., Takeda, K., and Ichijo, H. (2004) The ASK1-MAP kinase cascades in mammalian stress response. J. Biochem. 136, 261-265
    • (2004) J. Biochem. , vol.136 , pp. 261-265
    • Matsukawa, J.1    Matsuzawa, A.2    Takeda, K.3    Ichijo, H.4
  • 30
    • 0032582644 scopus 로고    scopus 로고
    • Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades
    • Hutchison, M., Berman, K. S., and Cobb, M. H. (1998) Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades. J. Biol. Chem. 273, 28625-28632
    • (1998) J. Biol. Chem. , vol.273 , pp. 28625-28632
    • Hutchison, M.1    Berman, K.S.2    Cobb, M.H.3
  • 31
    • 0035937158 scopus 로고    scopus 로고
    • The kinetic mechanism of the dual phosphorylation of the ATF2 transcription factor by p38 mitogen-activated protein (MAP) kinase: Implications for signal/response profiles of MAP kinase pathways
    • Waas, W. F., Lo, H. H., and Dalby, K. N. (2001) The kinetic mechanism of the dual phosphorylation of the ATF2 transcription factor by p38 mitogen-activated protein (MAP) kinase: implications for signal/response profiles of MAP kinase pathways. J. Biol. Chem. 276, 5676-5684
    • (2001) J. Biol. Chem. , vol.276 , pp. 5676-5684
    • Waas, W.F.1    Lo, H.H.2    Dalby, K.N.3
  • 32
    • 79952111889 scopus 로고    scopus 로고
    • Structural studies of MAP Kinase cascade components
    • Goldsmith, E. J., Min, X., He, H., and Zhou, T. (2010) Structural studies of MAP Kinase cascade components. Methods Mol. Biol. 661, 223-237
    • (2010) Methods Mol. Biol. , vol.661 , pp. 223-237
    • Goldsmith, E.J.1    Min, X.2    He, H.3    Zhou, T.4
  • 37
    • 78649775811 scopus 로고    scopus 로고
    • The third conformation of p38MAP kinase observed in phosphorylated p38and in solution
    • Akella, R., Min, X., Wu, Q., Gardner, K. H., and Goldsmith, E. J. (2010) The third conformation of p38MAP kinase observed in phosphorylated p38and in solution. Structure 18, 1571-1578
    • (2010) Structure , vol.18 , pp. 1571-1578
    • Akella, R.1    Min, X.2    Wu, Q.3    Gardner, K.H.4    Goldsmith, E.J.5
  • 39
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 40
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237, 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 41
    • 69949100557 scopus 로고    scopus 로고
    • Application of the Van Slyke-Cullen irreversible mechanism in the analysis of enzymatic progress curves
    • Kuzmic, P. (2009) Application of the Van Slyke-Cullen irreversible mechanism in the analysis of enzymatic progress curves. Anal. Biochem. 394, 287-289
    • (2009) Anal. Biochem. , vol.394 , pp. 287-289
    • Kuzmic, P.1
  • 42
    • 0007589020 scopus 로고
    • The mode of action of urease and of enzymes in general
    • Van Slyke, D. D., and Cullen, G. E. (1914) The mode of action of urease and of enzymes in general. J. Biol. Chem. 19, 141-180
    • (1914) J. Biol. Chem. , vol.19 , pp. 141-180
    • Van Slyke, D.D.1    Cullen, G.E.2
  • 43
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogenactivated protein kinase cascade
    • Huang, C. Y., and Ferrell, J. E., Jr. (1996) Ultrasensitivity in the mitogenactivated protein kinase cascade. Proc. Natl. Acad. Sci. U.S.A. 93, 10078-10083
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 44
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta, S., Campbell, D., Derijard, B., and Davis, R. J. (1995) Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 267, 389-393
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Derijard, B.3    Davis, R.J.4
  • 45
    • 69249232043 scopus 로고    scopus 로고
    • The nuclear appearance of ERK1/2 and p38 determines the sequential induction of ATF2-Thr71 and ATF2-Thr69 phosphorylation by serum in JNKdeficient cells
    • Baan, B., van der Zon, G. C., Maassen, J. A., and Ouwens, D. M. (2009) The nuclear appearance of ERK1/2 and p38 determines the sequential induction of ATF2-Thr71 and ATF2-Thr69 phosphorylation by serum in JNKdeficient cells. Mol. Cell. Endocrinol. 311, 94-100
    • (2009) Mol. Cell. Endocrinol. , vol.311 , pp. 94-100
    • Baan, B.1    Van Der Zon, G.C.2    Maassen, J.A.3    Ouwens, D.M.4
  • 46
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., Zheng, J. H., Ten Eyck, L. F., Ashford, V. A., Xuong, N. H., Taylor, S. S., and Sowadski, J. M. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 47
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq, A., and Zhou, M. M. (2004) Structure and regulation of MAPK phosphatases. Cell. Signal. 16, 769-779
    • (2004) Cell. Signal. , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 48
    • 0035943595 scopus 로고    scopus 로고
    • The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3
    • Zhao, Y., and Zhang, Z. Y. (2001) The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3. J. Biol. Chem. 276, 32382-32391
    • (2001) J. Biol. Chem. , vol.276 , pp. 32382-32391
    • Zhao, Y.1    Zhang, Z.Y.2
  • 49
    • 0037200054 scopus 로고    scopus 로고
    • The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases
    • Zhou, B., Wang, Z. X., Zhao, Y., Brautigan, D. L., and Zhang, Z. Y. (2002) The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases. J. Biol. Chem. 277, 31818-31825
    • (2002) J. Biol. Chem. , vol.277 , pp. 31818-31825
    • Zhou, B.1    Wang, Z.X.2    Zhao, Y.3    Brautigan, D.L.4    Zhang, Z.Y.5
  • 50
    • 17544363814 scopus 로고    scopus 로고
    • Characterization of a protein kinase that phosphorylates serine 189 of the mitogen-activated protein kinase homolog ERK3
    • Cheng, M., Zhen, E., Robinson, M. J., Ebert, D., Goldsmith, E., and Cobb, M. H. (1996) Characterization of a protein kinase that phosphorylates serine 189 of the mitogen-activated protein kinase homolog ERK3. J. Biol. Chem. 271, 12057-12062
    • (1996) J. Biol. Chem. , vol.271 , pp. 12057-12062
    • Cheng, M.1    Zhen, E.2    Robinson, M.J.3    Ebert, D.4    Goldsmith, E.5    Cobb, M.H.6
  • 51
    • 33947304756 scopus 로고    scopus 로고
    • Substrate competition as a source of ultrasensitivity in the inactivation of Wee1
    • Kim, S. Y., and Ferrell, J. E., Jr. (2007) Substrate competition as a source of ultrasensitivity in the inactivation of Wee1. Cell 128, 1133-1145
    • (2007) Cell , vol.128 , pp. 1133-1145
    • Kim, S.Y.1    Ferrell Jr., J.E.2
  • 52
    • 33344455174 scopus 로고    scopus 로고
    • Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction
    • Furdui, C. M., Lew, E. D., Schlessinger, J., and Anderson, K. S. (2006) Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol. Cell 21, 711-717
    • (2006) Mol. Cell , vol.21 , pp. 711-717
    • Furdui, C.M.1    Lew, E.D.2    Schlessinger, J.3    Anderson, K.S.4
  • 53
    • 84867904006 scopus 로고    scopus 로고
    • ATF2-At the crossroad of nuclear and cytosolic functions
    • Lau, E., and Ronai, Z. A. (2012) ATF2-at the crossroad of nuclear and cytosolic functions. J. Cell Sci. 125, 2815-2824
    • (2012) J. Cell Sci. , vol.125 , pp. 2815-2824
    • Lau, E.1    Ronai, Z.A.2
  • 54
    • 67749117934 scopus 로고    scopus 로고
    • Signal integration by JNK and p38 MAPK pathways in cancer development
    • Wagner, E. F., and Nebreda, A. R. (2009) Signal integration by JNK and p38 MAPK pathways in cancer development. Nat. Rev. Cancer 9, 537-549
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 537-549
    • Wagner, E.F.1    Nebreda, A.R.2
  • 55
    • 0038574979 scopus 로고    scopus 로고
    • Ion suppression in mass spectrometry
    • Annesley, T. M. (2003) Ion suppression in mass spectrometry. Clin. Chem. 49, 1041-1044
    • (2003) Clin. Chem. , vol.49 , pp. 1041-1044
    • Annesley, T.M.1
  • 56
    • 71549142265 scopus 로고    scopus 로고
    • DynaFit-a software package for enzymology
    • Kuzmic, P. (2009) DynaFit-a software package for enzymology. Methods Enzymol. 467, 247-280
    • (2009) Methods Enzymol. , vol.467 , pp. 247-280
    • Kuzmic, P.1


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