메뉴 건너뛰기




Volumn 36, Issue C, 1996, Pages 49-65

Structural Analysis of the MAP Kinase ERK2 and Studies of MAP Kinase Regulatory Pathways

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 6; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE;

EID: 0030358762     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60576-1     Document Type: Article
Times cited : (24)

References (53)
  • 1
    • 0026773119 scopus 로고
    • Identification of an activator of the microtubule-associated protein 2 kinases ERK1 and ERK2 in PC12 cells stimulated with nerve growth factor or bradykinin
    • Ahn N.G., Robbins D.J., Haycock J.W., Seger R., Cobb M.H., and Krebs E.G. Identification of an activator of the microtubule-associated protein 2 kinases ERK1 and ERK2 in PC12 cells stimulated with nerve growth factor or bradykinin. J. Neurochem. 59 (1992) 147-156
    • (1992) J. Neurochem. , vol.59 , pp. 147-156
    • Ahn, N.G.1    Robbins, D.J.2    Haycock, J.W.3    Seger, R.4    Cobb, M.H.5    Krebs, E.G.6
  • 2
    • 0025832605 scopus 로고
    • Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase
    • Ahn N.G., Seger R., Bratlien R.L., Diltz C.D., Tonks N.K., and Krebs E.G. Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase. J. Biol. Chem. 266 (1991) 4220-4227
    • (1991) J. Biol. Chem. , vol.266 , pp. 4220-4227
    • Ahn, N.G.1    Seger, R.2    Bratlien, R.L.3    Diltz, C.D.4    Tonks, N.K.5    Krebs, E.G.6
  • 4
    • 0027306121 scopus 로고
    • The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts
    • Alessi D.R., Smythe C., and Keyse S.M. The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts. Oncogene 8 (1993) 2015-2020
    • (1993) Oncogene , vol.8 , pp. 2015-2020
    • Alessi, D.R.1    Smythe, C.2    Keyse, S.M.3
  • 5
    • 0025120244 scopus 로고
    • Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
    • Anderson N.G., Mailer J.L., Tonks N.K., and Sturgill T.W. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 343 (1990) 651-653
    • (1990) Nature , vol.343 , pp. 651-653
    • Anderson, N.G.1    Mailer, J.L.2    Tonks, N.K.3    Sturgill, T.W.4
  • 6
    • 0027233448 scopus 로고
    • Signal transduction via the MAP kinases: Proceed at your own RSK
    • Blenis J. Signal transduction via the MAP kinases: Proceed at your own RSK. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 5889-5892
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5889-5892
    • Blenis, J.1
  • 7
    • 0026165752 scopus 로고
    • Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies
    • Boulton T.G., and Cobb M.H. Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies. Cell Regul. 2 (1991) 357-371
    • (1991) Cell Regul. , vol.2 , pp. 357-371
    • Boulton, T.G.1    Cobb, M.H.2
  • 10
    • 0028216851 scopus 로고
    • A role for autophosphorylation revealed by activated alleles of FUS3, the yeast MAP kinase homolog
    • Brill J.A., Elion E.A., and Fink G.R. A role for autophosphorylation revealed by activated alleles of FUS3, the yeast MAP kinase homolog. Mol. Cell. Biol. 5 (1994) 297-312
    • (1994) Mol. Cell. Biol. , vol.5 , pp. 297-312
    • Brill, J.A.1    Elion, E.A.2    Fink, G.R.3
  • 11
    • 0028328631 scopus 로고
    • A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways
    • Brunner D., Oellers N., Szabad J., Biggs W.H., Zipursky S.L., and Hafen E. A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways. Cell 76 (1994) 875-888
    • (1994) Cell , vol.76 , pp. 875-888
    • Brunner, D.1    Oellers, N.2    Szabad, J.3    Biggs, W.H.4    Zipursky, S.L.5    Hafen, E.6
  • 13
    • 0028492040 scopus 로고
    • The mitogen-activated protein kinases, ERK1 and ERK2. Sent
    • Cobb M.H., Hepler J.E., Cheng M., and Robbins D. The mitogen-activated protein kinases, ERK1 and ERK2. Sent. Cancer Biol. 5 (1994) 261-268
    • (1994) Cancer Biol. , vol.5 , pp. 261-268
    • Cobb, M.H.1    Hepler, J.E.2    Cheng, M.3    Robbins, D.4
  • 14
    • 0028073283 scopus 로고
    • MAPKS: New JNK expands the group
    • Davis R. MAPKS: New JNK expands the group. TIBS 19 (1994) 470-473
    • (1994) TIBS , vol.19 , pp. 470-473
    • Davis, R.1
  • 15
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis R.J. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268 (1993) 14553-14556
    • (1993) J. Biol. Chem. , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 16
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro
    • Dent P., Haser W., Haystead T.A.J., Vincent L.A., Roberts T.M., and Sturgill T.W. Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. Science 257 (1992) 1404-1407
    • (1992) Science , vol.257 , pp. 1404-1407
    • Dent, P.1    Haser, W.2    Haystead, T.A.J.3    Vincent, L.A.4    Roberts, T.M.5    Sturgill, T.W.6
  • 18
    • 0028297817 scopus 로고
    • MEK-1 phosphorylation by MEK kinase, Raf, and mitogen-activated protein kinase. Analysis of phosphopeptides and regulation of activity. Mol. Biol
    • Gardner A.M., Vaillancourt R.R., Lange-Carter C.A., and Johnson G.L. MEK-1 phosphorylation by MEK kinase, Raf, and mitogen-activated protein kinase. Analysis of phosphopeptides and regulation of activity. Mol. Biol. Cell 5 (1994) 193-201
    • (1994) Cell , vol.5 , pp. 193-201
    • Gardner, A.M.1    Vaillancourt, R.R.2    Lange-Carter, C.A.3    Johnson, G.L.4
  • 20
    • 0025875819 scopus 로고
    • Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinases
    • Gómez N., and Cohen P. Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinases. Nature 353 (1991) 170-173
    • (1991) Nature , vol.353 , pp. 170-173
    • Gómez, N.1    Cohen, P.2
  • 21
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J., Lee J.-D., Bibbs L., and Ulevitch R.J. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265 (1994) 808-811
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.-D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 22
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks S.K., Quinn A.M., and Hunter T. The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains. Science 241 (1988) 42-52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 23
    • 0028359636 scopus 로고
    • Insulin activates a novel adipocyte mitogen-activated protein kinase kinase kinase that shows rapid phasic kinetics and is distinct from c-Raf
    • Haystead C.M.M., Gregory P., Shirazi A., Fadden P., Mosse C., Dent P., and Haystead T.A.J. Insulin activates a novel adipocyte mitogen-activated protein kinase kinase kinase that shows rapid phasic kinetics and is distinct from c-Raf. J. Biol. Chem. 269 (1994) 12804-12808
    • (1994) J. Biol. Chem. , vol.269 , pp. 12804-12808
    • Haystead, C.M.M.1    Gregory, P.2    Shirazi, A.3    Fadden, P.4    Mosse, C.5    Dent, P.6    Haystead, T.A.J.7
  • 24
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • Herskowitz I. MAP kinase pathways in yeast: For mating and more. Cell 80 (1995) 187-197
    • (1995) Cell , vol.80 , pp. 187-197
    • Herskowitz, I.1
  • 26
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling. Cell 80 (1995) 225-236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 28
  • 29
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R., Zheng J., Ten Eyck L.F., Xuong N.-H., Taylor S.S., and Sowadski J.M. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253 (1991) 414-429
    • (1991) Science , vol.253 , pp. 414-429
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Xuong, N.-H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 30
    • 0026637326 scopus 로고
    • Pheromone response in yeast
    • Kurjan J. Pheromone response in yeast. Annu. Rev. Biochem. 61 (1992) 1097-1129
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1097-1129
    • Kurjan, J.1
  • 32
    • 0026764517 scopus 로고
    • Growth factor-induced activation of a kinase activity which causes regulatory phosphorylation of p42/ microtubule-associated protein kinase
    • L'Allemain G.L., Her J.-H., Wu J., Sturgill T.W., and Weber M.J. Growth factor-induced activation of a kinase activity which causes regulatory phosphorylation of p42/ microtubule-associated protein kinase. Mol. Cell. Biol. 12 (1992) 2222-2229
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2222-2229
    • L'Allemain, G.L.1    Her, J.-H.2    Wu, J.3    Sturgill, T.W.4    Weber, M.J.5
  • 33
    • 0027215820 scopus 로고
    • A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf
    • Lange-Carter C.A., Pleiman C.M., Gardner A.M., Blumer K.J., and Johnson G.L. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science 260 (1993) 315-319
    • (1993) Science , vol.260 , pp. 315-319
    • Lange-Carter, C.A.1    Pleiman, C.M.2    Gardner, A.M.3    Blumer, K.J.4    Johnson, G.L.5
  • 35
    • 0342746820 scopus 로고
    • A multitude of MAP kinase activation pathways
    • Levin D.E., and Errede B. A multitude of MAP kinase activation pathways. J. NIH Res. 5 (1993) 49-52
    • (1993) J. NIH Res. , vol.5 , pp. 49-52
    • Levin, D.E.1    Errede, B.2
  • 37
    • 0025885772 scopus 로고
    • Signal transduction during pheromone response in yeast
    • Marsh L., Neiman A.M., and Herskowitz I. Signal transduction during pheromone response in yeast. Annu. Rev. Cell Biol. 7 (1991) 699-728
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 699-728
    • Marsh, L.1    Neiman, A.M.2    Herskowitz, I.3
  • 38
    • 0027513768 scopus 로고
    • Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase and MAP kinase
    • Matsuda S., Gotoh Y., and Nishida E. Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase and MAP kinase. J. Biol. Chem. 268 (1993) 3277-3281
    • (1993) J. Biol. Chem. , vol.268 , pp. 3277-3281
    • Matsuda, S.1    Gotoh, Y.2    Nishida, E.3
  • 40
    • 0027462979 scopus 로고
    • Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro
    • Posada J., Yew N., Ahn N.G., Vande Woude G.F., and Cooper J.A. Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro. Mol. Cell. Biol. 13 (1993) 2546-2553
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2546-2553
    • Posada, J.1    Yew, N.2    Ahn, N.G.3    Vande Woude, G.F.4    Cooper, J.A.5
  • 42
    • 0028216315 scopus 로고
    • MAP kinases ERK1 and ERK2: Pleiotropic enzymes in a ubiquitous signaling network
    • Robbins D.J., Zhen E., Cheng M., Xu S., Ebert D., and Cobb M.H. MAP kinases ERK1 and ERK2: Pleiotropic enzymes in a ubiquitous signaling network. Adv. Cancer Res. 63 (1994) 93-116
    • (1994) Adv. Cancer Res. , vol.63 , pp. 93-116
    • Robbins, D.J.1    Zhen, E.2    Cheng, M.3    Xu, S.4    Ebert, D.5    Cobb, M.H.6
  • 43
  • 44
    • 0028219853 scopus 로고
    • Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation
    • Rossomando A.J., Dent P., Sturgill T.W., and Marshak D.R. Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation. Mol. Cell. Biol. 14 (1994) 1594-1602
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1594-1602
    • Rossomando, A.J.1    Dent, P.2    Sturgill, T.W.3    Marshak, D.R.4
  • 45
    • 0026690922 scopus 로고
    • Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells
    • Seger R., Ahn N.G., Posada J., Munar E.S., Jensen A.M., Cooper J.A., Cobb M.H.-., and Krebs E.G. Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J. Biol. Chem. 267 (1992) 14373-14381
    • (1992) J. Biol. Chem. , vol.267 , pp. 14373-14381
    • Seger, R.1    Ahn, N.G.2    Posada, J.3    Munar, E.S.4    Jensen, A.M.5    Cooper, J.A.6    Cobb, M.H.-.7    Krebs, E.G.8
  • 46
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation
    • Sontag E., Federov S., Robbins D., Cobb M., and Mumby M. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation. Cell 75 (1993) 887-897
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Federov, S.2    Robbins, D.3    Cobb, M.4    Mumby, M.5
  • 47
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • Sun H., Charles C.H., Lau L.F., and Tonks N.K. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75 (1993) 487-493
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 49
    • 0028670788 scopus 로고
    • Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
    • Yan M., Dal T., Deak J.C., Kyriakis J.M., Zon L.I., Woodgett J.R., and Templeton D.J. Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature 372 (1994) 798-800
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dal, T.2    Deak, J.C.3    Kyriakis, J.M.4    Zon, L.I.5    Woodgett, J.R.6    Templeton, D.J.7
  • 50
    • 0028308224 scopus 로고
    • Identification of 2 serine residues of MEK-1 that are differentially phosphorylated during activation by raf and MEK kinase
    • Yan M., and Templeton D.J. Identification of 2 serine residues of MEK-1 that are differentially phosphorylated during activation by raf and MEK kinase. J. Biol. Chem. 269 (1994) 19067-19073
    • (1994) J. Biol. Chem. , vol.269 , pp. 19067-19073
    • Yan, M.1    Templeton, D.J.2
  • 51
    • 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. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367 (1994) 704-710
    • (1994) Nature , vol.367 , pp. 704-710
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 52
    • 0029644242 scopus 로고
    • Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
    • Zhang J., Zhang F., Ebert D., Cobb M.H., and Goldsmith E.J. Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. Nature Structure 3 (1995) 299-307
    • (1995) Nature Structure , vol.3 , pp. 299-307
    • Zhang, J.1    Zhang, F.2    Ebert, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 53
    • 0027323844 scopus 로고
    • Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase
    • Zheng C.-F., and Guan K.-L. Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase. J. Biol. Chem. 268 (1993) 16116-16119
    • (1993) J. Biol. Chem. , vol.268 , pp. 16116-16119
    • Zheng, C.-F.1    Guan, K.-L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.