메뉴 건너뛰기




Volumn 25, Issue 9, 2000, Pages 448-453

Docking domains and substrate-specificity determination for MAP kinases

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; ONCOPROTEIN; PROTEIN C JUN; PROTEIN V JUN; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0034284131     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01627-3     Document Type: Review
Times cited : (402)

References (35)
  • 1
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson M.J., Cobb M.H. Mitogen-activated protein kinase pathways. Curr. Opin. Cell Biol. 9:1997;180-186.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 180-186
    • Robinson, M.J.1    Cobb, M.H.2
  • 2
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • Whitmarsh A.J., Davis R.J. Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J. Mol. Med. 74:1996;589-607.
    • (1996) J. Mol. Med. , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 3
    • 0031977016 scopus 로고    scopus 로고
    • The riddle of MAP kinase signaling specificity
    • Madhani H.D., Fink G.R. The riddle of MAP kinase signaling specificity. Trends Genet. 14:1998;151-155.
    • (1998) Trends Genet. , vol.14 , pp. 151-155
    • Madhani, H.D.1    Fink, G.R.2
  • 4
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh A.J., Davis R.J. Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem. Sci. 23:1998;481-485.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 5
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi M.et al. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev. 7:1993;2135-2148.
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1
  • 6
    • 0028902996 scopus 로고
    • Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: Implications for repression of c-Jun function
    • Dai T.et al. Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells. implications for repression of c-Jun function Oncogene. 10:1995;849-855.
    • (1995) Oncogene , vol.10 , pp. 849-855
    • Dai, T.1
  • 7
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinases. J. Biol. Chem. 270:1995;16483-16486.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 8
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta S.et al. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science. 267:1995;389-393.
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1
  • 9
    • 0029034251 scopus 로고
    • ATF-2 contains a phosphorylation-dependent transcriptional activation domain
    • Livingstone C.et al. ATF-2 contains a phosphorylation-dependent transcriptional activation domain. EMBO J. 14:1995;1785-1797.
    • (1995) EMBO J. , vol.14 , pp. 1785-1797
    • Livingstone, C.1
  • 10
    • 0031882123 scopus 로고    scopus 로고
    • The Elk-1 ETS-domain transcription factor contains a MAP kinase targeting motif
    • Yang S.-H.et al. The Elk-1 ETS-domain transcription factor contains a MAP kinase targeting motif. Mol. Cell. Biol. 18:1998;710-720.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 710-720
    • Yang, S.-H.1
  • 11
    • 0033011595 scopus 로고    scopus 로고
    • Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors
    • Yang S.H.et al. Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors. Mol. Cell. Biol. 19:1999;4028-4038.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4028-4038
    • Yang, S.H.1
  • 12
    • 0029885419 scopus 로고    scopus 로고
    • Selective interaction of JNK protein kinase isoforms with transcription factors
    • Gupta S.et al. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J. 15:1996;2760-2770.
    • (1996) EMBO J. , vol.15 , pp. 2760-2770
    • Gupta, S.1
  • 13
    • 0032536816 scopus 로고    scopus 로고
    • Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1
    • Yang S.-H.et al. Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1. EMBO J. 17:1998;1740-1749.
    • (1998) EMBO J. , vol.17 , pp. 1740-1749
    • Yang, S.-H.1
  • 14
    • 0030606319 scopus 로고    scopus 로고
    • C-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions
    • Kallunki T.et al. c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. Cell. 87:1996;929-939.
    • (1996) Cell , vol.87 , pp. 929-939
    • Kallunki, T.1
  • 15
    • 0034595707 scopus 로고    scopus 로고
    • ERK2 MAP kinase binding, phosphorylation and regulation of PDE4D cAMP specific phosphodiesterases: The involvement of C-terminal docking sites and N-terminal UCR regions
    • MacKenzie S.J.et al. ERK2 MAP kinase binding, phosphorylation and regulation of PDE4D cAMP specific phosphodiesterases. the involvement of C-terminal docking sites and N-terminal UCR regions J. Biol. Chem. 275:2000;16609-16617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16609-16617
    • MacKenzie, S.J.1
  • 16
    • 0030826412 scopus 로고    scopus 로고
    • A cytoplasmic inhibitor of the JNK signal transduction pathway
    • Dickens M.et al. A cytoplasmic inhibitor of the JNK signal transduction pathway. Science. 277:1997;693-696.
    • (1997) Science , vol.277 , pp. 693-696
    • Dickens, M.1
  • 17
    • 0032534791 scopus 로고    scopus 로고
    • PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
    • Pulido R.et al. PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J. 17:1998;7337-7350.
    • (1998) EMBO J. , vol.17 , pp. 7337-7350
    • Pulido, R.1
  • 18
    • 0038845769 scopus 로고    scopus 로고
    • Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm
    • Zuniga A.et al. Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. J. Biol. Chem. 274:1999;21900-21907.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21900-21907
    • Zuniga, A.1
  • 19
    • 0030272039 scopus 로고    scopus 로고
    • A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAP KINASEs
    • Bardwell L., Thorner J. A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAP KINASEs. Trends Biochem. Sci. 21:1996;373-374.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 373-374
    • Bardwell, L.1    Thorner, J.2
  • 20
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T.et al. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat. Cell. Biol. 2:2000;110-116.
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 110-116
    • Tanoue, T.1
  • 21
    • 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-E.et al. 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. 274:1999;34029-34035.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34029-34035
    • Xu, B-E.1
  • 22
    • 0033545604 scopus 로고    scopus 로고
    • A MAP kinase docking site is required for phosphorylation and activation of p90(rsk)/MAPKAP kinase-1
    • Gavin A.C., Nebreda A.R. A MAP kinase docking site is required for phosphorylation and activation of p90(rsk)/MAPKAP kinase-1. Curr. Biol. 9:1999;281-284.
    • (1999) Curr. Biol. , vol.9 , pp. 281-284
    • Gavin, A.C.1    Nebreda, A.R.2
  • 23
    • 0033613857 scopus 로고    scopus 로고
    • Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo
    • Smith J.A.et al. Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo. J. Biol. Chem. 274:1999;2893-2898.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2893-2898
    • Smith, J.A.1
  • 24
    • 0032509335 scopus 로고    scopus 로고
    • Analysis of the interaction between c-Jun and c-Jun N-terminal kinase in vivo
    • May G.H.et al. Analysis of the interaction between c-Jun and c-Jun N-terminal kinase in vivo. J. Biol. Chem. 273:1998;33429-33435.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33429-33435
    • May, G.H.1
  • 25
    • 0031904310 scopus 로고    scopus 로고
    • Gain-of-function mutations in the Caenorhabditis elegans lin-1 ETS gene identify a C-terminal regulatory domain phosphorylated by ERK MAP kinase
    • Jacobs D.et al. Gain-of-function mutations in the Caenorhabditis elegans lin-1 ETS gene identify a C-terminal regulatory domain phosphorylated by ERK MAP kinase. Genetics. 149:1998;1809-1822.
    • (1998) Genetics , vol.149 , pp. 1809-1822
    • Jacobs, D.1
  • 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.et al. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev. 13:1999;163-175.
    • (1999) Genes Dev. , vol.13 , pp. 163-175
    • Jacobs, D.1
  • 27
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh A.J.et al. A mammalian scaffold complex that selectively mediates MAP kinase activation. Science. 281:1998;1671-1674.
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1
  • 28
    • 0032531753 scopus 로고    scopus 로고
    • Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1
    • Yang C.C.et al. Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1. Nucleic Acids Res. 26:1998;4771-4777.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4771-4777
    • Yang, C.C.1
  • 29
    • 0032518334 scopus 로고    scopus 로고
    • An oncogenic mutation uncouples the v-Jun oncoprotein from positive regulation by the SAPK/JNK pathway in vivo
    • May G.H.et al. An oncogenic mutation uncouples the v-Jun oncoprotein from positive regulation by the SAPK/JNK pathway in vivo. Curr. Biol. 8:1998;117-120.
    • (1998) Curr. Biol. , vol.8 , pp. 117-120
    • May, G.H.1
  • 30
    • 0032700045 scopus 로고    scopus 로고
    • A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase
    • Zhan X.L., Guan K.L. A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase. Genes Dev. 13:1999;2811-2827.
    • (1999) Genes Dev. , vol.13 , pp. 2811-2827
    • Zhan, X.L.1    Guan, K.L.2
  • 31
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki T.et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev. 8:1994;2996-3007.
    • (1994) Genes Dev. , vol.8 , pp. 2996-3007
    • Kallunki, T.1
  • 32
    • 0033539882 scopus 로고    scopus 로고
    • Identification of two distinct regions of p38 MAP kinase required for substrate binding and phosphorylation
    • Gum R.J., Young P.R. Identification of two distinct regions of p38 MAP kinase required for substrate binding and phosphorylation. Biochem. Biophys. Res. Commun. 266:1999;284-289.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 284-289
    • Gum, R.J.1    Young, P.R.2
  • 33
    • 0032557632 scopus 로고    scopus 로고
    • Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
    • Camps M.et al. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science. 280:1998;1262-1265.
    • (1998) Science , vol.280 , pp. 1262-1265
    • Camps, M.1
  • 34
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R.et al. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science. 253:1991;414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1
  • 35
    • 0033529034 scopus 로고    scopus 로고
    • Protein modification: Docking sites for kinases
    • Holland P.M., Cooper J.A. Protein modification. docking sites for kinases Curr. Biol. 9:1999;329-331.
    • (1999) Curr. Biol. , vol.9 , pp. 329-331
    • Holland, P.M.1    Cooper, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.