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Volumn 6, Issue 4, 2011, Pages

A model of a MAPK•substrate complex in an active conformation: A computational and experimental approach

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 1; TRANSCRIPTION FACTOR ETS 1; LIGAND; PEPTIDE;

EID: 79954524705     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018594     Document Type: Article
Times cited : (20)

References (36)
  • 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
  • 2
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman M, Chen W, Cobb MH, (2007) Differential regulation and properties of MAPKs. Oncogene 26: 3100-3112.
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 3
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ, (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90: 859-869.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 4
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G, (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15: 661-675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 6
    • 21644449056 scopus 로고    scopus 로고
    • Protein-protein interactions in the regulation of the extracellular signal-regulated kinase
    • Chuderland D, Seger R, (2005) Protein-protein interactions in the regulation of the extracellular signal-regulated kinase. Mol Biotechnol 29: 57-74.
    • (2005) Mol Biotechnol , vol.29 , pp. 57-74
    • Chuderland, D.1    Seger, R.2
  • 7
    • 0037155834 scopus 로고    scopus 로고
    • Specificity determinants in MAPK signaling to transcription factors
    • Barsyte-Lovejoy D, Galanis A, Sharrocks AD, (2002) Specificity determinants in MAPK signaling to transcription factors. J Biol Chem 277: 9896-9903.
    • (2002) J Biol Chem , vol.277 , pp. 9896-9903
    • Barsyte-Lovejoy, D.1    Galanis, A.2    Sharrocks, A.D.3
  • 8
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi RM, Nebreda AR, (2003) Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem J 372: 1-13.
    • (2003) Biochem J , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 9
    • 50349093357 scopus 로고    scopus 로고
    • Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs
    • Sheridan DL, Kong Y, Parker SA, Dalby KN, Turk BE, (2008) Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs. J Biol Chem 283: 19511-19520.
    • (2008) J Biol Chem , vol.283 , pp. 19511-19520
    • Sheridan, D.L.1    Kong, Y.2    Parker, S.A.3    Dalby, K.N.4    Turk, B.E.5
  • 11
    • 33751214237 scopus 로고    scopus 로고
    • Properties and regulation of a transiently assembled ERK2.Ets-1 signaling complex
    • Callaway KA, Rainey MA, Riggs AF, Abramczyk O, Dalby KN, (2006) Properties and regulation of a transiently assembled ERK2.Ets-1 signaling complex. Biochemistry 45: 13719-13733.
    • (2006) Biochemistry , vol.45 , pp. 13719-13733
    • Callaway, K.A.1    Rainey, M.A.2    Riggs, A.F.3    Abramczyk, O.4    Dalby, K.N.5
  • 12
    • 34547862095 scopus 로고    scopus 로고
    • Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding
    • Abramczyk O, Rainey MA, Barnes R, Martin L, Dalby KN, (2007) Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding. Biochemistry 46: 9174-9186.
    • (2007) Biochemistry , vol.46 , pp. 9174-9186
    • Abramczyk, O.1    Rainey, M.A.2    Barnes, R.3    Martin, L.4    Dalby, K.N.5
  • 13
    • 77951670691 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1
    • Callaway K, Waas WF, Rainey MA, Ren P, Dalby KN, (2010) Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1. Biochemistry 49: 3619-3630.
    • (2010) Biochemistry , vol.49 , pp. 3619-3630
    • Callaway, K.1    Waas, W.F.2    Rainey, M.A.3    Ren, P.4    Dalby, K.N.5
  • 14
    • 0036142763 scopus 로고    scopus 로고
    • An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors
    • Seidel JJ, Graves BJ, (2002) An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors. Genes Dev 16: 127-137.
    • (2002) Genes Dev , vol.16 , pp. 127-137
    • Seidel, J.J.1    Graves, B.J.2
  • 15
    • 0142031483 scopus 로고    scopus 로고
    • Two rate-limiting steps in the kinetic mechanism of the serine/threonine specific protein kinase ERK2: a case of fast phosphorylation followed by fast product release
    • Waas WF, Rainey MA, Szafranska AE, Dalby KN, (2003) Two rate-limiting steps in the kinetic mechanism of the serine/threonine specific protein kinase ERK2: a case of fast phosphorylation followed by fast product release. Biochemistry 42: 12273-12286.
    • (2003) Biochemistry , vol.42 , pp. 12273-12286
    • Waas, W.F.1    Rainey, M.A.2    Szafranska, A.E.3    Dalby, K.N.4
  • 16
    • 0037066745 scopus 로고    scopus 로고
    • Transient protein-protein interactions and a random-ordered kinetic mechanism for the phosphorylation of a transcription factor by extracellular-regulated protein kinase 2
    • Waas WF, Dalby KN, (2002) Transient protein-protein interactions and a random-ordered kinetic mechanism for the phosphorylation of a transcription factor by extracellular-regulated protein kinase 2. J Biol Chem 277: 12532-12540.
    • (2002) J Biol Chem , vol.277 , pp. 12532-12540
    • Waas, W.F.1    Dalby, K.N.2
  • 18
    • 29144502234 scopus 로고    scopus 로고
    • The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network
    • Remenyi A, Good MC, Bhattacharyya RP, Lim WA, (2005) The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. Mol Cell 20: 951-962.
    • (2005) Mol Cell , vol.20 , pp. 951-962
    • Remenyi, A.1    Good, M.C.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 19
    • 67650543863 scopus 로고    scopus 로고
    • Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats
    • Hobeika M, Brockmann C, Gruessing F, Neuhaus D, Divita G, et al. (2009) Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats. J Biol Chem 284: 17575-17583.
    • (2009) J Biol Chem , vol.284 , pp. 17575-17583
    • Hobeika, M.1    Brockmann, C.2    Gruessing, F.3    Neuhaus, D.4    Divita, G.5
  • 22
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • Zhou T, Sun L, Humphreys J, Goldsmith EJ, (2006) Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 14: 1011-1019.
    • (2006) Structure , vol.14 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3    Goldsmith, E.J.4
  • 23
    • 1842665655 scopus 로고    scopus 로고
    • Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry
    • Lee T, Hoofnagle AN, Kabuyama Y, Stroud J, Min X, et al. (2004) Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry. Mol Cell 14: 43-55.
    • (2004) Mol Cell , vol.14 , pp. 43-55
    • Lee, T.1    Hoofnagle, A.N.2    Kabuyama, Y.3    Stroud, J.4    Min, X.5
  • 24
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge MD, Murray CW, Auton TR, Paolini GV, Mee RP, (1997) Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comput Aided Mol Des 11: 425-445.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 25
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R, (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 26
    • 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 AJ, 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.
    • (1999) Genes Dev , vol.13 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3    Muslin, A.J.4    Kornfeld, K.5
  • 27
    • 0034284131 scopus 로고    scopus 로고
    • Docking domains and substrate-specificity determination for MAP kinases
    • Sharrocks AD, Yang SH, Galanis A, (2000) Docking domains and substrate-specificity determination for MAP kinases. Trends Biochem Sci 25: 448-453.
    • (2000) Trends Biochem Sci , vol.25 , pp. 448-453
    • Sharrocks, A.D.1    Yang, S.H.2    Galanis, A.3
  • 28
    • 0035920179 scopus 로고    scopus 로고
    • Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues
    • Fantz DA, Jacobs D, Glossip D, Kornfeld K, (2001) Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues. J Biol Chem 276: 27256-27265.
    • (2001) J Biol Chem , vol.276 , pp. 27256-27265
    • Fantz, D.A.1    Jacobs, D.2    Glossip, D.3    Kornfeld, K.4
  • 29
    • 0035847076 scopus 로고    scopus 로고
    • Selective targeting of MAPKs to the ETS domain transcription factor SAP-1
    • Galanis A, Yang SH, Sharrocks AD, (2001) Selective targeting of MAPKs to the ETS domain transcription factor SAP-1. J Biol Chem 276: 965-973.
    • (2001) J Biol Chem , vol.276 , pp. 965-973
    • Galanis, A.1    Yang, S.H.2    Sharrocks, A.D.3
  • 30
    • 0036289349 scopus 로고    scopus 로고
    • Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b
    • Chang CI, Xu BE, Akella R, Cobb MH, Goldsmith EJ, (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.
    • (2002) Mol Cell , vol.9 , pp. 1241-1249
    • Chang, C.I.1    Xu, B.E.2    Akella, R.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 31
    • 3042689209 scopus 로고    scopus 로고
    • Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
    • Heo YS, Kim SK, Seo CI, Kim YK, Sung BJ, et al. (2004) Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125. EMBO J 23: 2185-2195.
    • (2004) EMBO J , vol.23 , pp. 2185-2195
    • Heo, Y.S.1    Kim, S.K.2    Seo, C.I.3    Kim, Y.K.4    Sung, B.J.5
  • 32
    • 33645765166 scopus 로고    scopus 로고
    • Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3
    • Liu S, Sun JP, Zhou B, Zhang ZY, (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
  • 33
    • 34248200476 scopus 로고    scopus 로고
    • Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer
    • ter Haar E, Prabhakar P, Liu X, Lepre C, (2007) Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer. J Biol Chem 282: 9733-9739.
    • (2007) J Biol Chem , vol.282 , pp. 9733-9739
    • ter Haar, E.1    Prabhakar, P.2    Liu, X.3    Lepre, C.4
  • 34
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ, (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293: 321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 35
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism
    • Huang Y, Liu Z, (2009) Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism. J Mol Biol 393: 1143-1159.
    • (2009) J Mol Biol , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.