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Volumn 10, Issue 1, 2014, Pages

Data-driven modeling reconciles kinetics of ERK phosphorylation, localization, and activity states

Author keywords

growth factor receptors; mathematical model; mitogen activated protein kinases; negative feedback; nucleocytoplasmic shuttling

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PLATELET DERIVED GROWTH FACTOR; GROWTH FACTOR RECEPTOR;

EID: 84898662770     PISSN: None     EISSN: 17444292     Source Type: Journal    
DOI: 10.1002/msb.134708     Document Type: Article
Times cited : (50)

References (56)
  • 1
    • 84872796463 scopus 로고    scopus 로고
    • Frequency-modulated pulses of ERK activity transmit quantitative proliferation signals
    • Albeck JG, Mills GB, Brugge JS, (2013) Frequency-modulated pulses of ERK activity transmit quantitative proliferation signals. Mol Cell 49: 249-261
    • (2013) Mol Cell , vol.49 , pp. 249-261
    • Albeck, J.G.1    Mills, G.B.2    Brugge, J.S.3
  • 2
    • 0025120244 scopus 로고
    • Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
    • Anderson NG, Maller JL, Tonks NK, Sturgill TW, (1990) Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 343: 651-653
    • (1990) Nature , vol.343 , pp. 651-653
    • Anderson, N.G.1    Maller, J.L.2    Tonks, N.K.3    Sturgill, T.W.4
  • 3
    • 0037444809 scopus 로고    scopus 로고
    • Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity
    • DOI 10.1042/BJ20021806
    • Bardwell AJ, Abdollahi M, Bardwell L, (2003) Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity. Biochem J 370: 1077-1085 (Pubitemid 36399103)
    • (2003) Biochemical Journal , vol.370 , Issue.3 , pp. 1077-1085
    • Bardwell, A.J.1    Abdollahi, M.2    Bardwell, L.3
  • 4
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • DOI 10.1126/science.1068873
    • Bhalla US, Ram PT, Iyengar R, (2002) MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science 297: 1018-1023 (Pubitemid 34856036)
    • (2002) Science , vol.297 , Issue.5583 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 6
    • 85035221677 scopus 로고    scopus 로고
    • Statistical mechanical approaches to models with many poorly known parameters
    • Brown KS, Sethna JP, (2003) Statistical mechanical approaches to models with many poorly known parameters. Phys Rev E 68: 021904
    • (2003) Phys Rev e , vol.68 , pp. 021904
    • Brown, K.S.1    Sethna, J.P.2
  • 7
    • 13544252820 scopus 로고    scopus 로고
    • Live cell imaging of ERK and MEK: Simple binding equilibrium explains the regulated nucleocytoplasmic distribution of ERK
    • DOI 10.1074/jbc.M410031200
    • Burack WR, Shaw AS, (2005) Live cell imaging of ERK and MEK: simple binding equilibrium explains the regulated nucleocytoplasmic distribution of ERK. J Biol Chem 280: 3832-3837 (Pubitemid 40223853)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3832-3837
    • Burack, W.R.1    Shaw, A.S.2
  • 8
    • 78649746618 scopus 로고    scopus 로고
    • Stimulus-induced uncoupling of extracellular signal-regulated kinase phosphorylation from nuclear localization is dependent on docking domain interactions
    • Caunt CJ, McArdle CA, (2010) Stimulus-induced uncoupling of extracellular signal-regulated kinase phosphorylation from nuclear localization is dependent on docking domain interactions. J Cell Sci 123: 4310-4320
    • (2010) J Cell Sci , vol.123 , pp. 4310-4320
    • Caunt, C.J.1    McArdle, C.A.2
  • 10
    • 80052469143 scopus 로고    scopus 로고
    • Development and application of a phosphoproteomic method using electrostatic repulsion-hydrophilic interaction chromatography (ERLIC), IMAC and LC-MS/MS analysis to study Marek's disease virus infection
    • Chien K, Liu HC, Goshe MB, (2011) Development and application of a phosphoproteomic method using electrostatic repulsion-hydrophilic interaction chromatography (ERLIC), IMAC and LC-MS/MS analysis to study Marek's disease virus infection. J Proteome Res 10: 4041-4053
    • (2011) J Proteome Res , vol.10 , pp. 4041-4053
    • Chien, K.1    Liu, H.C.2    Goshe, M.B.3
  • 11
    • 77749322224 scopus 로고    scopus 로고
    • Timing-dependent actions of NGF required for cell differentiation
    • Chung J, Kubota H, Ozaki Y, Uda S, Kuroda S, (2010) Timing-dependent actions of NGF required for cell differentiation. PLoS ONE 5: e9011
    • (2010) PLoS ONE , vol.5
    • Chung, J.1    Kubota, H.2    Ozaki, Y.3    Uda, S.4    Kuroda, S.5
  • 12
    • 84055223930 scopus 로고    scopus 로고
    • Data-driven modelling of receptor tyrosine kinase signalling networks quantifies receptor-specific potencies of PI3K- and Ras-dependent ERK activation
    • Cirit M, Haugh JM, (2012) Data-driven modelling of receptor tyrosine kinase signalling networks quantifies receptor-specific potencies of PI3K- and Ras-dependent ERK activation. Biochem J 441: 77-85
    • (2012) Biochem J , vol.441 , pp. 77-85
    • Cirit, M.1    Haugh, J.M.2
  • 13
    • 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, Haugh JM, (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
  • 14
    • 71149092283 scopus 로고    scopus 로고
    • Dynamics and variability of ERK2 response to EGF in individual living cells
    • Cohen-Saidon C, Cohen AA, Sigal A, Liron Y, Alon U, (2009) Dynamics and variability of ERK2 response to EGF in individual living cells. Mol Cell 36: 885-893
    • (2009) Mol Cell , vol.36 , pp. 885-893
    • Cohen-Saidon, C.1    Cohen, A.A.2    Sigal, A.3    Liron, Y.4    Alon, U.5
  • 16
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • DOI 10.1038/sj.onc.1210421, PII 1210421
    • Dhillon AS, Hagan S, Rath O, Kolch W, (2007) MAP kinase signalling pathways in cancer. Oncogene 26: 3279-3290 (Pubitemid 46763021)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 20
    • 0029786994 scopus 로고    scopus 로고
    • 2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal
    • DOI 10.1074/jbc.271.33.20024
    • Fukuda M, Gotoh I, Gotoh Y, Nishida E, (1996) Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J Biol Chem 271: 20024-20028 (Pubitemid 26281751)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.33 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3    Nishidaf, E.4
  • 21
    • 0028297817 scopus 로고
    • MEK-1 phosphorylation by MEK kinase, Raf, and mitogen-activated protein kinase: Analysis of phosphopeptides and regulation of activity
    • Gardner AM, Vaillancourt RR, Lange-Carter CA, Johnson GL, (1994) MEK-1 phosphorylation by MEK kinase, Raf, and mitogen-activated protein kinase: analysis of phosphopeptides and regulation of activity. Mol Biol Cell 5: 193-201 (Pubitemid 24108465)
    • (1994) Molecular Biology of the Cell , vol.5 , Issue.2 , pp. 193-201
    • Gardner, A.M.1    Vaillancourt, R.R.2    Lange-Carter, C.A.3    Johnson, G.L.4
  • 23
    • 84867174770 scopus 로고    scopus 로고
    • Combined computational and experimental analysis reveals mitogen-activated protein kinase-mediated feedback phosphorylation as a mechanism for signaling specificity
    • Hao N, Yildirim N, Nagiec MJ, Parnell SC, Errede B, Dohlman HG, Elston TC, (2012) Combined computational and experimental analysis reveals mitogen-activated protein kinase-mediated feedback phosphorylation as a mechanism for signaling specificity. Mol Biol Cell 23: 3899-3910
    • (2012) Mol Biol Cell , vol.23 , pp. 3899-3910
    • Hao, N.1    Yildirim, N.2    Nagiec, M.J.3    Parnell, S.C.4    Errede, B.5    Dohlman, H.G.6    Elston, T.C.7
  • 25
    • 84860468362 scopus 로고    scopus 로고
    • Live-cell fluorescence microscopy with molecular biosensors: What are we really measuring?
    • Haugh JM, (2012) Live-cell fluorescence microscopy with molecular biosensors: what are we really measuring? Biophys J 102: 2003-2011
    • (2012) Biophys J , vol.102 , pp. 2003-2011
    • Haugh, J.M.1
  • 26
    • 80053577384 scopus 로고    scopus 로고
    • Spatiotemporally regulated protein kinase A activity is a critical regulator of growth factor-stimulated extracellular signal-regulated kinase signaling in PC12 cells
    • Herbst KJ, Allen MD, Zhang J, (2011) Spatiotemporally regulated protein kinase A activity is a critical regulator of growth factor-stimulated extracellular signal-regulated kinase signaling in PC12 cells. Mol Cell Biol 31: 4063-4075
    • (2011) Mol Cell Biol , vol.31 , pp. 4063-4075
    • Herbst, K.J.1    Allen, M.D.2    Zhang, J.3
  • 27
    • 84863877454 scopus 로고    scopus 로고
    • A kinetic model of ERK cyclic pathway on substrate control
    • Hirashima T, (2012) A kinetic model of ERK cyclic pathway on substrate control. Math Biosci 239: 207-212
    • (2012) Math Biosci , vol.239 , pp. 207-212
    • Hirashima, T.1
  • 28
    • 0037403309 scopus 로고    scopus 로고
    • Examining the mechanism of Erk nuclear translocation using green fluorescent protein
    • DOI 10.1016/S0014-4827(03)00037-5
    • Horgan AM, Stork PJ, (2003) Examining the mechanism of Erk nuclear translocation using green fluorescent protein. Exp Cell Res 285: 208-220 (Pubitemid 36428954)
    • (2003) Experimental Cell Research , vol.285 , Issue.2 , pp. 208-220
    • Horgan, A.M.1    Stork, P.J.S.2
  • 34
    • 79952113734 scopus 로고    scopus 로고
    • Localization and trafficking of fluorescently tagged Erk1 and Erk2
    • Marchi M, Parra R, Costa M, Ratto GM, (2010) Localization and trafficking of fluorescently tagged Erk1 and Erk2. Method Mol Biol 661: 287-301
    • (2010) Method Mol Biol , vol.661 , pp. 287-301
    • Marchi, M.1    Parra, R.2    Costa, M.3    Ratto, G.M.4
  • 35
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-related kinase activation
    • Marshall CJ, (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-related kinase activation. Cell 80: 179-185
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 36
    • 34248575149 scopus 로고    scopus 로고
    • Integrating signals from RTKs to ERK/MAPK
    • DOI 10.1038/sj.onc.1210394, PII 1210394
    • McKay MM, Morrison DK, (2007) Integrating signals from RTKs to ERK/MAPK. Oncogene 26: 3113-3121 (Pubitemid 46763008)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3113-3121
    • McKay, M.M.1    Morrison, D.K.2
  • 37
    • 0141733263 scopus 로고    scopus 로고
    • Kinetic analysis of platelet-derived growth factor receptor/ phosphoinositide 3-kinase/Akt signaling in fibroblasts
    • DOI 10.1074/jbc.M304968200
    • Park CS, Schneider IC, Haugh JM, (2003) Kinetic analysis of platelet-derived growth factor receptor/phosphoinositide 3-kinase/Akt signaling in fibroblasts. J Biol Chem 278: 37064-37072 (Pubitemid 37175220)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37064-37072
    • Park, C.S.1    Schneider, I.C.2    Haugh, J.M.3
  • 38
    • 79960907910 scopus 로고    scopus 로고
    • The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation
    • Plotnikov A, Zehorai E, Procaccia S, Seger R, (2011) The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation. BBA Mol Cell Res 1813: 1619-1633
    • (2011) BBA Mol Cell Res , vol.1813 , pp. 1619-1633
    • Plotnikov, A.1    Zehorai, E.2    Procaccia, S.3    Seger, R.4
  • 39
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • DOI 10.1038/sj.onc.1210422, PII 1210422
    • Roberts PJ, Der CJ, (2007) Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene 26: 3291-3310 (Pubitemid 46763022)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3291-3310
    • Roberts, P.J.1    Der, C.J.2
  • 40
    • 84870539840 scopus 로고    scopus 로고
    • Crosstalk and competition in signaling networks
    • Rowland MA, Fontana W, Deeds EJ, (2012) Crosstalk and competition in signaling networks. Biophys J 103: 2389-2398
    • (2012) Biophys J , vol.103 , pp. 2389-2398
    • Rowland, M.A.1    Fontana, W.2    Deeds, E.J.3
  • 41
    • 17344362384 scopus 로고    scopus 로고
    • Prediction and validation of the distinct dynamics of transient and sustained ERK activation
    • DOI 10.1038/ncb1233
    • Sasagawa S, Ozaki Y, Fujita K, Kuroda S, (2005) Prediction and validation of the distinct dynamics of transient and sustained ERK activation. Nat Cell Biol 7: 365-373 (Pubitemid 40533125)
    • (2005) Nature Cell Biology , vol.7 , Issue.4 , pp. 365-373
    • Sasagawa, S.1    Ozaki, Y.-I.2    Fujita, K.3    Kuroda, S.4
  • 42
    • 33947361161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells
    • DOI 10.1021/ac062171d
    • Sato M, Kawai Y, Umezawa Y, (2007) Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells. Anal Chem 79: 2570-2575 (Pubitemid 46449042)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2570-2575
    • Sato, M.1    Kawai, Y.2    Umezawa, Y.3
  • 45
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • DOI 10.1038/nbt0402-370
    • Schoeberl B, Eichler-Jonsson C, Gilles ED, Muller G, (2002) Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nat Biotechnol 20: 370-375 (Pubitemid 34286330)
    • (2002) Nature Biotechnology , vol.20 , Issue.4 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 47
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M, (2007) Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 8: 195-208
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 49
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T, Adachi M, Moriguchi T, Nishida E, (2000) A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat Cell Biol 2: 110-116
    • (2000) Nat Cell Biol , vol.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 50
    • 60749087137 scopus 로고    scopus 로고
    • PI3K-dependent crosstalk interactions converge with Ras as quantifiable inputs integrated by Erk
    • 246
    • Wang C-C, Cirit M, Haugh JM, (2009) PI3K-dependent crosstalk interactions converge with Ras as quantifiable inputs integrated by Erk. Mol Syst Biol 5: 246
    • (2009) Mol Syst Biol , vol.5
    • Wang, C.-C.1    Cirit, M.2    Haugh, J.M.3
  • 51
    • 77951091683 scopus 로고    scopus 로고
    • Basic fibroblast growth factor regulates persistent Erk oscillations in premalignant but not malignant JB6 cells
    • Weber TJ, Shankaran H, Wiley HS, Opresko LK, Chrisler WB, Quesenberry RD, (2010) Basic fibroblast growth factor regulates persistent Erk oscillations in premalignant but not malignant JB6 cells. J Invest Dermatol 130: 1444-1456
    • (2010) J Invest Dermatol , vol.130 , pp. 1444-1456
    • Weber, T.J.1    Shankaran, H.2    Wiley, H.S.3    Opresko, L.K.4    Chrisler, W.B.5    Quesenberry, R.D.6
  • 52
    • 73949146865 scopus 로고    scopus 로고
    • Directional persistence of cell migration coincides with stability of asymmetric intracellular signaling
    • Weiger MC, Ahmed S, Welf ES, Haugh JM, (2010) Directional persistence of cell migration coincides with stability of asymmetric intracellular signaling. Biophys J 98: 67-75
    • (2010) Biophys J , vol.98 , pp. 67-75
    • Weiger, M.C.1    Ahmed, S.2    Welf, E.S.3    Haugh, J.M.4
  • 53
    • 84860295783 scopus 로고    scopus 로고
    • Migrating fibroblasts reorient directionality by a metastable, PI3K-dependent mechanism
    • Welf ES, Ahmed S, Johnson HE, Melvin AT, Haugh JM, (2012) Migrating fibroblasts reorient directionality by a metastable, PI3K-dependent mechanism. J Cell Biol 197: 105-114
    • (2012) J Cell Biol , vol.197 , pp. 105-114
    • Welf, E.S.1    Ahmed, S.2    Johnson, H.E.3    Melvin, A.T.4    Haugh, J.M.5
  • 54
    • 0033607522 scopus 로고    scopus 로고
    • The N-terminal ERK-binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo
    • Xu B, Wilsbacher JL, Collisson T, Cobb MH, (1999) The N-terminal ERK-binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo. J Biol Chem 274: 34029-34035 (Pubitemid 129511735)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.48 , pp. 34029-34035
    • Xu, B.-E.1    Wilsbacher, J.L.2    Collisson, T.3    Cobb, M.H.4
  • 55
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions
    • DOI 10.1159/000094762, PII N130170763401
    • Yoon S, Seger R, (2006) The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24: 21-44 (Pubitemid 43108774)
    • (2006) Growth Factors , vol.24 , Issue.1 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 56
    • 71849119627 scopus 로고    scopus 로고
    • The subcellular localization of Mek and Erk: A novel nuclear translocation signal (NTS) paves a way to the nucleus
    • Zehorai E, Yao Z, Plotnikov A, Seger R, (2010) The subcellular localization of Mek and Erk: a novel nuclear translocation signal (NTS) paves a way to the nucleus. Mol Cell Endocrinol 314: 213-220
    • (2010) Mol Cell Endocrinol , vol.314 , pp. 213-220
    • Zehorai, E.1    Yao, Z.2    Plotnikov, A.3    Seger, R.4


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