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Volumn 288, Issue 12, 2013, Pages 8596-8609

Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL CHARACTERIZATION; CATALYTIC PROPERTIES; EXTRACELLULAR SIGNAL-REGULATED KINASE; MITOGEN ACTIVATED PROTEIN KINASE; PHYSIOLOGICAL FUNCTIONS; PROTEIN INTERACTION; PROTEIN-PROTEIN INTERACTIONS; STRUCTURAL MECHANISMS;

EID: 84875409408     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.452235     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 33747792064 scopus 로고    scopus 로고
    • MAPK signalling: ERK5 versus ERK1/2
    • DOI 10.1038/sj.embor.7400755, PII 7400755
    • Nishimoto, S., and Nishida, E. (2006) MAPK signalling: ERK5 versus ERK1/2. EMBO Rep. 7, 782-786 (Pubitemid 44275395)
    • (2006) EMBO Reports , vol.7 , Issue.8 , pp. 782-786
    • Nishimoto, S.1    Nishida, E.2
  • 2
    • 32144436881 scopus 로고    scopus 로고
    • Regulation of cellular functions by the ERK5 signalling pathway
    • DOI 10.1016/j.cellsig.2005.11.003, PII S0898656805003062
    • Wang, X., and Tournier, C. (2006) Regulation of cellular functions by the ERK5 signalling pathway. Cell Signal. 18, 753-760 (Pubitemid 43208930)
    • (2006) Cellular Signalling , vol.18 , Issue.6 , pp. 753-760
    • Wang, X.1    Tournier, C.2
  • 4
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou, G., Bao, Z. Q., and Dixon, J. E. (1995) Components of a new human protein kinase signal transduction pathway. J. Biol. Chem. 270, 12665-12669
    • (1995) J. Biol. Chem. , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3
  • 5
    • 0032531881 scopus 로고    scopus 로고
    • Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor
    • DOI 10.1038/27234
    • Kato, Y., Tapping, R. I., Huang, S., Watson, M. H., Ulevitch, R. J., and Lee, J. D. (1998) Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor. Nature 395, 713-716 (Pubitemid 28475970)
    • (1998) Nature , vol.395 , Issue.6703 , pp. 713-716
    • Kato, Y.1    Tapping, R.I.2    Huang, S.3    Watson, M.H.4    Ulevitch, R.J.5    Lee, J.-D.6
  • 6
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • DOI 10.1038/sj.onc.1210392, PII 1210392
    • Raman, M., Chen, W., and Cobb, M. H. (2007) Differential regulation and properties of MAPKs. Oncogene 26, 3100-3112 (Pubitemid 46763006)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 7
    • 0035863129 scopus 로고    scopus 로고
    • Differential regulation of mitogen-activated protein kinases ERK1/2 and ERK5 by neurotrophins, neuronal activity, and cAMP in neurons
    • Cavanaugh, J. E., Ham, J., Hetman, M., Poser, S., Yan, C., and Xia, Z. (2001) Differential regulation of mitogen-activated protein kinases ERK1/2 and ERK5 by neurotrophins, neuronal activity, and cAMP in neurons. J. Neurosci. 21, 434-443 (Pubitemid 32107434)
    • (2001) Journal of Neuroscience , vol.21 , Issue.2 , pp. 434-443
    • Cavanaugh, J.E.1    Ham, J.2    Hetman, M.3    Poser, S.4    Yan, C.5    Xia, Z.6
  • 10
    • 0037044718 scopus 로고    scopus 로고
    • ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression
    • DOI 10.1074/jbc.M207573200
    • Sohn, S. J., Sarvis, B. K., Cado, D., and Winoto, A. (2002) ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression. J. Biol. Chem. 277, 43344-43351 (Pubitemid 35285722)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43344-43351
    • Sohn, S.J.1    Sarvis, B.K.2    Cado, D.3    Winoto, A.4
  • 12
    • 0035896513 scopus 로고    scopus 로고
    • ERK5 and ERK2 cooperate to regulate NF-B and cell transformation
    • Pearson, G., English, J. M., White, M. A., and Cobb, M. H. (2001) ERK5 and ERK2 cooperate to regulate NF-B and cell transformation. J. Biol. Chem. 276, 7927-7931
    • (2001) J. Biol. Chem. , vol.276 , pp. 7927-7931
    • Pearson, G.1    English, J.M.2    White, M.A.3    Cobb, M.H.4
  • 13
    • 0034804675 scopus 로고    scopus 로고
    • Neurotrophins use the Erk5 pathway to mediate a retrograde survival response
    • DOI 10.1038/nn720
    • Watson, F. L., Heerssen, H. M., Bhattacharyya, A., Klesse, L., Lin, M. Z., and Segal, R. A. (2001) Neurotrophins use the Erk5 pathway to mediate a retrograde survival response. Nat. Neurosci. 4, 981-988 (Pubitemid 32924137)
    • (2001) Nature Neuroscience , vol.4 , Issue.10 , pp. 981-988
    • Watson, F.L.1    Heerssen, H.M.2    Bhattacharyya, A.3    Klesse, L.4    Lin, M.Z.5    Segal, R.A.6
  • 14
    • 13244291607 scopus 로고    scopus 로고
    • The unique C-terminal tail of the mitogen-activated protein kinase ERK5 regulates its activation and nuclear shuttling
    • DOI 10.1074/jbc.M412599200
    • Buschbeck, M., and Ullrich, A. (2005) The unique C-terminal tail of the mitogen-activated protein kinase ERK5 regulates its activation and nuclear shuttling. J. Biol. Chem. 280, 2659-2667 (Pubitemid 40189370)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2659-2667
    • Buschbeck, M.1    Ullrich, A.2
  • 15
    • 33644537037 scopus 로고    scopus 로고
    • Regulation of nuclear translocation of extracellular signal-regulated kinase 5 by active nuclear import and export mechanisms
    • Kondoh, K., Terasawa, K., Morimoto, H., and Nishida, E. (2006) Regulation of nuclear translocation of extracellular signal-regulated kinase 5 by active nuclear import and export mechanisms. Mol. Cell. Biol. 26, 1679-1690
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1679-1690
    • Kondoh, K.1    Terasawa, K.2    Morimoto, H.3    Nishida, E.4
  • 16
    • 0033278751 scopus 로고    scopus 로고
    • The evolution of the map kinase pathways: Coduplication of interacting proteins leads to new signaling cascades
    • Caffrey, D. R., O'Neill, L. A., and Shields, D. C. (1999) The evolution of the MAP kinase pathways: coduplication of interacting proteins leads to new signaling cascades. J. Mol. Evol. 49, 567-582 (Pubitemid 32268713)
    • (1999) Journal of Molecular Evolution , vol.49 , Issue.5 , pp. 567-582
    • Caffrey, D.R.1    O'Neill, L.A.J.2    Shields, D.C.3
  • 17
    • 80055048292 scopus 로고    scopus 로고
    • Evolutionary history of the vertebrate mitogen activated protein kinases family
    • Li, M., Liu, J., and Zhang, C. (2011) Evolutionary history of the vertebrate mitogen activated protein kinases family. PloS One 6, e26999
    • (2011) PloS One , vol.6
    • Li, M.1    Liu, J.2    Zhang, C.3
  • 18
    • 0030694387 scopus 로고    scopus 로고
    • BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C
    • Kato, Y., Kravchenko, V. V., Tapping, R. I., Han, J., Ulevitch, R. J., and Lee, J. D. (1997) BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. EMBO J. 16, 7054-7066 (Pubitemid 27520805)
    • (1997) EMBO Journal , vol.16 , Issue.23 , pp. 7054-7066
    • Kato, Y.1    Kravchenko, V.V.2    Tapping, R.I.3    Han, J.4    Ulevitch, R.J.5    Lee, J.-D.6
  • 20
    • 38049147787 scopus 로고    scopus 로고
    • MEF2: A central regulator of diverse developmental programs
    • Potthoff, M. J., and Olson, E. N. (2007) MEF2: a central regulator of diverse developmental programs. Development 134, 4131-4140
    • (2007) Development , vol.134 , pp. 4131-4140
    • Potthoff, M.J.1    Olson, E.N.2
  • 21
    • 0033788484 scopus 로고    scopus 로고
    • Aconserved docking motif in MAP kinases common to substrates, activators, and regulators
    • Tanoue, T., Adachi, M., Moriguchi, T., and Nishida, E. (2000)Aconserved 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
  • 22
    • 67649710849 scopus 로고    scopus 로고
    • Selectivity of docking sites in MAPK kinases
    • Bardwell, A. J., Frankson, E., and Bardwell, L. (2009) Selectivity of docking sites in MAPK kinases. J. Biol. Chem. 284, 13165-13173
    • (2009) J. Biol. Chem. , vol.284 , pp. 13165-13173
    • Bardwell, A.J.1    Frankson, E.2    Bardwell, L.3
  • 24
    • 0036289349 scopus 로고    scopus 로고
    • Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b
    • DOI 10.1016/S1097-2765(02)00525-7
    • Chang, C. I., Xu, B. E., Akella, R., Cobb, M. H., and Goldsmith, E. J. (2002) Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b. Mol. Cell 9, 1241-1249 (Pubitemid 34722303)
    • (2002) Molecular Cell , vol.9 , Issue.6 , pp. 1241-1249
    • Chang, C.-I.1    Xu, B.-E.2    Akella, R.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 25
    • 29144502234 scopus 로고    scopus 로고
    • The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network
    • DOI 10.1016/j.molcel.2005.10.030, PII S1097276505017259
    • Reményi, A., Good, M. C., Bhattacharyya, R. P., and Lim, W. A. (2005) The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. Mol. Cell 20, 951-962 (Pubitemid 41814883)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 951-962
    • Remenyi, A.1    Good, M.C.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 26
    • 84875439909 scopus 로고    scopus 로고
    • Protein-peptide complex crystallization: A case study on the ERK2 mitogen-activated protein kinase
    • in press
    • Gógl, G., Töro, I., and Reményi, A. (2012) Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. Acta Crystallogr. D Biol. Crystallogr., in press
    • (2012) Acta Crystallogr. D Biol. Crystallogr.
    • Gógl, G.1    Töro, I.2    Reményi, A.3
  • 27
    • 0141484661 scopus 로고    scopus 로고
    • PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway
    • DOI 10.1074/jbc.C300313200
    • Nakamura, K., and Johnson, G. L. (2003) PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway. J. Biol. Chem. 278, 36989-36992 (Pubitemid 37175211)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 36989-36992
    • Nakamura, K.1    Johnson, G.L.2
  • 28
    • 34250215694 scopus 로고    scopus 로고
    • Noncanonical function of MEKK2 and MEK5 PB1 domains for coordinated extracellular signal-regulated kinase 5 and c-Jun N-terminal kinase signaling
    • DOI 10.1128/MCB.00125-07
    • Nakamura, K., and Johnson, G. L. (2007) Noncanonical function of MEKK2 and MEK5 PB1 domains for coordinated extracellular signalregulated kinase 5 and c-Jun N-terminal kinase signaling. Mol. Cell. Biol. 27, 4566-4577 (Pubitemid 46906577)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.12 , pp. 4566-4577
    • Nakamura, K.1    Johnson, G.L.2
  • 29
    • 33644745546 scopus 로고    scopus 로고
    • PB1 domain-dependent signaling complex is required for extracellular signal-regulated kinase 5 activation
    • DOI 10.1128/MCB.26.6.2065-2079.2006
    • Nakamura, K., Uhlik, M. T., Johnson, N. L., Hahn, K. M., and Johnson, G. L. (2006) PB1 domain-dependent signaling complex is required for extracellular signal-regulated kinase 5 activation. Mol. Cell. Biol. 26, 2065-2079 (Pubitemid 43346911)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.6 , pp. 2065-2079
    • Nakamura, K.1    Uhlik, M.T.2    Johnson, N.L.3    Hahn, K.M.4    Johnson, G.L.5
  • 30
    • 36749044194 scopus 로고    scopus 로고
    • Insight into the binding properties of MEKK3 PB1 to MEK5 PB1 from its solution structure
    • DOI 10.1021/bi701341n
    • Hu, Q., Shen, W., Huang, H., Liu, J., Zhang, J., Huang, X., Wu, J., and Shi, Y. (2007) Insight into the binding properties of MEKK3 PB1 to MEK5 PB1 from its solution structure. Biochemistry 46, 13478-13489 (Pubitemid 350214358)
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13478-13489
    • Hu, Q.1    Shen, W.2    Huang, H.3    Liu, J.4    Zhang, J.5    Huang, X.6    Wu, J.7    Shi, Y.8
  • 31
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta crystallogr
    • Kabsch, W. (2010) XDS. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 37
    • 4344695112 scopus 로고    scopus 로고
    • ERK5 is targeted to myocyte enhancer factor 2A (MEF2A) through a MAPK docking motif
    • DOI 10.1042/BJ20031940
    • Barsyte-Lovejoy, D., Galanis, A., Clancy, A., and Sharrocks, A. D. (2004) ERK5 is targeted to myocyte enhancer factor 2A (MEF2A) through a MAPK docking motif. Biochem. J. 381, 693-699 (Pubitemid 39120478)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 693-699
    • Barsyte-Lovejoy, D.1    Galanis, A.2    Clancy, A.3    Sharrocks, A.D.4
  • 39
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M. H., and Goldsmith, E. J. (1994) Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367, 704-711
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 40
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • DOI 10.1016/j.str.2006.04.006, PII S096921260600222X
    • Zhou, T., Sun, L., Humphreys, J., and Goldsmith, E. J. (2006) Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 14, 1011-1019 (Pubitemid 43831663)
    • (2006) Structure , vol.14 , Issue.6 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3    Goldsmith, E.J.4
  • 41
    • 33645765166 scopus 로고    scopus 로고
    • Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3
    • Liu, S., Sun, J. P., Zhou, B., and Zhang, Z. Y. (2006) Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3. Proc. Natl. Acad. Sci. U.S.A. 103, 5326-5331
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5326-5331
    • Liu, S.1    Sun, J.P.2    Zhou, B.3    Zhang, Z.Y.4
  • 42
    • 78149425640 scopus 로고    scopus 로고
    • Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase
    • Ma, W., Shang, Y., Wei, Z., Wen, W., Wang, W., and Zhang, M. (2010) Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase. Structure 18, 1502-1511
    • (2010) Structure , vol.18 , pp. 1502-1511
    • Ma, W.1    Shang, Y.2    Wei, Z.3    Wen, W.4    Wang, W.5    Zhang, M.6
  • 43
    • 0033555229 scopus 로고    scopus 로고
    • Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
    • Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., and Kornfeld, K. (1999) Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev. 13, 163-175 (Pubitemid 29061947)
    • (1999) Genes and Development , vol.13 , Issue.2 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3    Muslin, A.J.4    Kornfeld, K.5
  • 44
    • 32444442870 scopus 로고    scopus 로고
    • The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway
    • DOI 10.1126/science.1120941
    • Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., and Lim, W. A. (2006) The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. Science 311, 822-826 (Pubitemid 43228840)
    • (2006) Science , vol.311 , Issue.5762 , pp. 822-826
    • Bhattacharyya, R.P.1    Remenyi, A.2    Good, M.C.3    Bashor, C.J.4    Falick, A.M.5    Lim, W.A.6
  • 45
    • 41149130109 scopus 로고    scopus 로고
    • Two adjacent docking sites in the yeast Hog1 Mitogen-Activated Protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase
    • DOI 10.1128/MCB.01817-07
    • Murakami, Y., Tatebayashi, K., and Saito, H. (2008) Two adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase. Mol. Cell. Biol. 28, 2481-2494 (Pubitemid 351429991)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.7 , pp. 2481-2494
    • Murakami, Y.1    Tatebayashi, K.2    Saito, H.3
  • 46
    • 67749129536 scopus 로고    scopus 로고
    • Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif
    • Aberg, E., Torgersen, K. M., Johansen, B., Keyse, S. M., Perander, M., and Seternes, O. M. (2009) Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif. J. Biol. Chem. 284, 19392-19401
    • (2009) J. Biol. Chem. , vol.284 , pp. 19392-19401
    • Aberg, E.1    Torgersen, K.M.2    Johansen, B.3    Keyse, S.M.4    Perander, M.5    Seternes, O.M.6
  • 48
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta, S., Campbell, D., Dérijard, 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    Dérijard, B.3    Davis, R.J.4
  • 49
    • 0034284131 scopus 로고    scopus 로고
    • Docking domains and substrate-specificity determination for MAP kinases
    • DOI 10.1016/S0968-0004(00)01627-3, PII S0968000400016273
    • Sharrocks, A. D., Yang, S. H., and Galanis, A. (2000) Docking domains and substrate-specificity determination forMAPkinases. Trends Biochem. Sci. 25, 448-453 (Pubitemid 30662413)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.9 , pp. 448-453
    • Sharrocks, A.D.1    Yang, S.-H.2    Galanis, A.3
  • 50
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • DOI 10.1038/nature02178
    • Zarrinpar, A., Park, S. H., and Lim, W. A. (2003) Optimization of specificity in a cellular protein interaction network by negative selection. Nature 426, 676-680 (Pubitemid 38009377)
    • (2003) Nature , vol.426 , Issue.6967 , pp. 676-680
    • Zarrinpar, A.1    Park, S.-H.2    Lim, W.A.3
  • 52
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • DOI 10.1016/j.molcel.2006.08.002, PII S1097276506005375
    • Moscat, J., Diaz-Meco, M. T., Albert, A., and Campuzano, S. (2006) Cell signaling and function organized by PB1 domain interactions. Mol. Cell 23, 631-640 (Pubitemid 44292560)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 53
    • 68549087161 scopus 로고    scopus 로고
    • Scaffolds: Interaction platforms for cellular signalling circuits
    • Zeke, A., Lukács, M., Lim, W. A., and Reményi, A. (2009) Scaffolds: interaction platforms for cellular signalling circuits. Trends Cell Biol. 19, 364-374
    • (2009) Trends Cell Biol. , vol.19 , pp. 364-374
    • Zeke, A.1    Lukács, M.2    Lim, W.A.3    Reményi, A.4
  • 54
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • DOI 10.1146/annurev.biochem.75.103004.142710
    • Bhattacharyya, R. P., Reményi, A., Yeh, B. J., and Lim, W. A. (2006) Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Ann Rev. Biochem. 75, 655- 680 (Pubitemid 44118047)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 55
    • 47049121578 scopus 로고    scopus 로고
    • The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus
    • Guo, C., and Whitmarsh, A. J. (2008) The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus. J. Biol. Chem. 283, 15903-15911
    • (2008) J. Biol. Chem. , vol.283 , pp. 15903-15911
    • Guo, C.1    Whitmarsh, A.J.2
  • 56
    • 79959938207 scopus 로고    scopus 로고
    • Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase
    • Won, A. P., Garbarino, J. E., and Lim, W. A. (2011) Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase. Proc. Natl. Acad. Sci. U.S.A. 108, 9809 -9814
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9809-9814
    • Won, A.P.1    Garbarino, J.E.2    Lim, W.A.3
  • 58
    • 34547228831 scopus 로고    scopus 로고
    • Atypical mitogen-activated protein kinases: Structure, regulation and functions
    • DOI 10.1016/j.bbamcr.2006.11.001, PII S0167488906003703
    • Coulombe, P., and Meloche, S. (2007) Atypical mitogen-activated protein kinases: structure, regulation and functions. Biochim. Biophys. Acta 1773, 1376-1387 (Pubitemid 47125971)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.8 , pp. 1376-1387
    • Coulombe, P.1    Meloche, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.