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Volumn 108, Issue 31, 2011, Pages 12675-12680

Processive phosphorylation of ERK MAP kinase in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE;

EID: 79961243052     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1104030108     Document Type: Article
Times cited : (158)

References (34)
  • 1
    • 24944553549 scopus 로고    scopus 로고
    • MAP kinase pathways
    • Qi M, Elion EA (2005) MAP kinase pathways. JCell Sci 118:3569-3572.
    • (2005) JCell Sci , vol.118 , pp. 3569-3572
    • Qi, M.1    Elion, E.A.2
  • 2
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M (2001) Mammalian MAP kinase signalling cascades. Nature 410:37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 3
    • 0035413618 scopus 로고    scopus 로고
    • MAP kinases
    • Chen Z, et al. (2001) MAP kinases. ChemRev 101:2449-2476.
    • (2001) ChemRev , vol.101 , pp. 2449-2476
    • Chen, Z.1
  • 4
    • 0027410497 scopus 로고
    • The MAP kinase cascade is essential for diverse signal transduction pathways
    • Nishida E, Gotoh Y (1993) The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem Sci 18:128-131.
    • (1993) Trends Biochem Sci , vol.18 , pp. 128-131
    • Nishida, E.1    Gotoh, Y.2
  • 5
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Songyang Z, et al. (1996) A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol Cell Biol 16:6486-6493.
    • (1996) Mol Cell Biol , vol.16 , pp. 6486-6493
    • Songyang, Z.1
  • 6
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell JE, Jr, Machleder EM (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
  • 7
    • 0345359924 scopus 로고    scopus 로고
    • A positive-feedback-based bistable 'memory module'that governs a cell fate decision
    • Xiong W, Ferrell JE, Jr (2003) A positive-feedback-based bistable 'memory module'that governs a cell fate decision. Nature 426:460-465.
    • (2003) Nature , vol.426 , pp. 460-465
    • Xiong, W.1    Ferrell Jr., J.E.2
  • 8
    • 33847355217 scopus 로고    scopus 로고
    • Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate
    • Santos SD, Verveer PJ, Bastiaens PI (2007) Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate. Nat Cell Biol 9:324-330.
    • (2007) Nat Cell Biol , vol.9 , pp. 324-330
    • Santos, S.D.1    Verveer, P.J.2    Bastiaens, P.I.3
  • 9
    • 33845607123 scopus 로고    scopus 로고
    • Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling
    • Daniels MA, et al. (2006) Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling. Nature 444:724-729.
    • (2006) Nature , vol.444 , pp. 724-729
    • Daniels, M.A.1
  • 10
    • 64649094816 scopus 로고    scopus 로고
    • KSR1 modulates the sensitivity of mitogen-activated protein kinase pathway activation in T cells without altering fundamental system outputs
    • Lin J, Harding A, Giurisato E, Shaw AS (2009) KSR1 modulates the sensitivity of mitogen-activated protein kinase pathway activation in T cells without altering fundamental system outputs. Mol Cell Biol 29:2082-2091.
    • (2009) Mol Cell Biol , vol.29 , pp. 2082-2091
    • Lin, J.1    Harding, A.2    Giurisato, E.3    Shaw, A.S.4
  • 11
    • 0030746219 scopus 로고    scopus 로고
    • Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase
    • Ferrell JE, Jr, Bhatt RR (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
  • 12
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang CY, Ferrell JE, Jr (1996) Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc Natl Acad Sci USA 93:10078-10083.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 13
    • 0842288229 scopus 로고    scopus 로고
    • Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades
    • Markevich NI, Hoek JB, Kholodenko BN (2004) Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades. J Cell Biol 164:353-359.
    • (2004) J Cell Biol , vol.164 , pp. 353-359
    • Markevich, N.I.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 15
    • 0030972112 scopus 로고    scopus 로고
    • The activating dual phosphorylation of MAPK by MEK is nonprocessive
    • Burack WR, Sturgill TW (1997) The activating dual phosphorylation of MAPK by MEK is nonprocessive. Biochemistry (Mosc) 36:5929-5933.
    • (1997) Biochemistry (Mosc) , vol.36 , pp. 5929-5933
    • Burack, W.R.1    Sturgill, T.W.2
  • 16
    • 26944476331 scopus 로고    scopus 로고
    • Regulated cell-to-cell variation in a cell-fate decision system
    • Colman-Lerner A, et al. (2005) Regulated cell-to-cell variation in a cell-fate decision system. Nature 437:699-706.
    • (2005) Nature , vol.437 , pp. 699-706
    • Colman-Lerner, A.1
  • 17
    • 0034777940 scopus 로고    scopus 로고
    • Graded mode of transcriptional induction in yeast pheromone signalling revealed by single-cell analysis
    • Poritz MA, Malmstrom S, Kim MK, Rossmeissl PJ, Kamb A (2001) Graded mode of transcriptional induction in yeast pheromone signalling revealed by single-cell analysis. Yeast 18:1331-1338.
    • (2001) Yeast , vol.18 , pp. 1331-1338
    • Poritz, M.A.1    Malmstrom, S.2    Kim, M.K.3    Rossmeissl, P.J.4    Kamb, A.5
  • 18
    • 49649109812 scopus 로고    scopus 로고
    • Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade
    • Takahashi S, Pryciak PM (2008) Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade. Curr Biol 18:1184-1191.
    • (2008) Curr Biol , vol.18 , pp. 1184-1191
    • Takahashi, S.1    Pryciak, P.M.2
  • 19
    • 18944374155 scopus 로고    scopus 로고
    • Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells
    • Mackeigan JP, Murphy LO, Dimitri CA, 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
  • 20
    • 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 MH, White MA (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
  • 21
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • Levchenko A, Bruck J, Sternberg PW (2000) Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc Natl Acad Sci USA 97:5818-5823.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 22
    • 0034009390 scopus 로고    scopus 로고
    • Signal transduction: Hanging on a scaffold
    • Burack WR, Shaw AS (2000) Signal transduction: hanging on a scaffold. Curr Opin Cell Biol 12:211-216.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 211-216
    • Burack, W.R.1    Shaw, A.S.2
  • 23
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch W (2005) Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat Rev Mol Cell Biol 6:827-837.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 827-837
    • Kolch, W.1
  • 24
    • 34548379387 scopus 로고    scopus 로고
    • Processive phosphorylation: Mechanism and biological importance
    • Patwardhan P, MillerWT (2007) Processive phosphorylation: mechanism and biological importance. Cellular Signalling 19:2218-2226.
    • (2007) Cellular Signalling , vol.19 , pp. 2218-2226
    • Patwardhan, P.1    Miller, W.T.2
  • 25
    • 58149083028 scopus 로고    scopus 로고
    • Scaffold proteins and immune-cell signalling
    • Shaw AS, Filbert EL (2009) Scaffold proteins and immune-cell signalling. Nat Rev Immunol 9:47-56.
    • (2009) Nat Rev Immunol , vol.9 , pp. 47-56
    • Shaw, A.S.1    Filbert, E.L.2
  • 26
    • 34047174559 scopus 로고    scopus 로고
    • A module of negative feedback regulators defines growth factor signaling
    • Amit I, et al. (2007) A module of negative feedback regulators defines growth factor signaling. Nat Genet 39:503-512.
    • (2007) Nat Genet , vol.39 , pp. 503-512
    • Amit, I.1
  • 28
    • 73849116154 scopus 로고    scopus 로고
    • Theoretical and experimental analysis links isoform-specific ERK signalling to cell fate decisions
    • Schilling M, et al. (2009) Theoretical and experimental analysis links isoform-specific ERK signalling to cell fate decisions. Mol Syst Biol 5:334-1-18.
    • (2009) Mol Syst Biol , vol.5 , pp. 334-1118
    • Schilling, M.1
  • 29
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis RJ (2001) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr Opin Struct Biol 11:114-119.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 30
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton AP (2006) How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 119:2863-2869.
    • (2006) J Cell Sci , vol.119 , pp. 2863-2869
    • Minton, A.P.1
  • 31
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • Shtilerman MD, Ding TT, Lansbury PT, Jr (2002) Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry (Mosc) 41:3855-3860.
    • (2002) Biochemistry (Mosc) , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury Jr., P.T.3
  • 32
    • 77249093066 scopus 로고    scopus 로고
    • Spatio-temporal correlations can drastically change the response of a MAPK pathway
    • Takahashi K, Tanase-Nicola S, ten Wolde PR (2010) Spatio-temporal correlations can drastically change the response of a MAPK pathway. Proc Natl Acad Sci USA 107:2473-2478.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2473-2478
    • Takahashi, K.1    Tanase-Nicola, S.2    Ten Wolde, P.R.3
  • 33
    • 0038732770 scopus 로고    scopus 로고
    • EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation
    • Reynolds AR, Tischer C, Verveer PJ, Rocks O, Bastiaens PI (2003) EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation. Nat Cell Biol 5:447-453.
    • (2003) Nat Cell Biol , vol.5 , pp. 447-453
    • Reynolds, A.R.1    Tischer, C.2    Verveer, P.J.3    Rocks, O.4    Bastiaens, P.I.5
  • 34
    • 33646852421 scopus 로고    scopus 로고
    • Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes
    • Fujioka A, et al. (2006) Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes. J Biol Chem 281:8917-8926.
    • (2006) J Biol Chem , vol.281 , pp. 8917-8926
    • Fujioka, A.1


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