메뉴 건너뛰기




Volumn 5, Issue 19, 2006, Pages 2210-2215

Regulation of MAP kinases by the VHR dual-specific phosphatase: Implications for cell growth and differentiation

Author keywords

ERK; JNK; MAPK; MKP; p38; VHR

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATASE; STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE 1; UNCLASSIFIED DRUG; VACCINIA H1 RELATED DUAL SPECIFIC PHOSPHATASE ENZYME;

EID: 33749635844     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.5.19.3267     Document Type: Review
Times cited : (32)

References (119)
  • 1
    • 0035197914 scopus 로고    scopus 로고
    • Isolation and characterization of pmk-(1-3): Three p38 homologs in Caenorhabditis elegans
    • Berman K, McKay J, Avery L, Cobb M. Isolation and characterization of pmk-(1-3): Three p38 homologs in Caenorhabditis elegans. Mol Cell Biol Res Comm 2001; 4:337-44.
    • (2001) Mol Cell Biol Res Comm , vol.4 , pp. 337-344
    • Berman, K.1    McKay, J.2    Avery, L.3    Cobb, M.4
  • 2
    • 0026638823 scopus 로고
    • Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase
    • Biggs IIIrd Wh, Zipursky SL. Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase. Proc Natl Acad Sci USA 1992; 89:6295-9.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6295-6299
    • Biggs III, Wh.1    Zipursky, S.L.2
  • 4
    • 0024442034 scopus 로고
    • A putative protein kinase overcomes pheromone-induced arrest of cell cycling in S. cerevisiae
    • Courchesne WE, Kunisawa R, Thorner J. A putative protein kinase overcomes pheromone-induced arrest of cell cycling in S. cerevisiae. Cell 1989; 58:1107-19.
    • (1989) Cell , vol.58 , pp. 1107-1119
    • Courchesne, W.E.1    Kunisawa, R.2    Thorner, J.3
  • 5
    • 0031962080 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase
    • Han SJ, Choi KY, Brey PT, Lee WJ. Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase. J Biol Chem 1998; 273:369-74.
    • (1998) J Biol Chem , vol.273 , pp. 369-374
    • Han, S.J.1    Choi, K.Y.2    Brey, P.T.3    Lee, W.J.4
  • 6
    • 0028107517 scopus 로고
    • A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of vulval cell fates in Caenorhabditis elegans
    • Lackner MR, Kornfeld K, Miller LM, Horvitz HR, Kim SK. A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of vulval cell fates in Caenorhabditis elegans. Genes Dev 1994; 8:160-73.
    • (1994) Genes Dev , vol.8 , pp. 160-173
    • Lackner, M.R.1    Kornfeld, K.2    Miller, L.M.3    Horvitz, H.R.4    Kim, S.K.5
  • 7
    • 0033168580 scopus 로고    scopus 로고
    • A Caenorhabditis elegans JNK signal transduction pathway regulates coordinated movement via type-D GABAergic motor neurons
    • Kawasaki M, Hisamoto N, Iino Y, Yamamoto M, Ninomiya-Tsuji J, Matsumoto K. A Caenorhabditis elegans JNK signal transduction pathway regulates coordinated movement via type-D GABAergic motor neurons. EMBO J 1999; 18:3604-15.
    • (1999) EMBO J , vol.18 , pp. 3604-3615
    • Kawasaki, M.1    Hisamoto, N.2    Iino, Y.3    Yamamoto, M.4    Ninomiya-Tsuji, J.5    Matsumoto, K.6
  • 8
    • 0029824847 scopus 로고    scopus 로고
    • A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila
    • Sluss HK, Han Z, Barrett T, Davis RJ, Ip YT. A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila. Genes Dev 1996; 10:2745-58.
    • (1996) Genes Dev , vol.10 , pp. 2745-2758
    • Sluss, H.K.1    Han, Z.2    Barrett, T.3    Davis, R.J.4    Ip, Y.T.5
  • 9
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis JM, Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev 2001; 81:807-69.
    • (2001) Physiol Rev , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 10
    • 0030911475 scopus 로고    scopus 로고
    • Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C
    • Lin Q, Schwarz J, Bucana CN, Olson E. Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C. Science 1997; 276:1404-7.
    • (1997) Science , vol.276 , pp. 1404-1407
    • Lin, Q.1    Schwarz, J.2    Bucana, C.N.3    Olson, E.4
  • 11
    • 0037047109 scopus 로고    scopus 로고
    • Erk5 null mice display multiple extraembryonic vascular and embryonic cardiovascular defects
    • Regan CP, Li W, Boucher DM, Spatz S, Su MS, Kuida K. Erk5 null mice display multiple extraembryonic vascular and embryonic cardiovascular defects. Proc Natl Acad Sci USA 2002; 99:9248-53.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9248-9253
    • Regan, C.P.1    Li, W.2    Boucher, D.M.3    Spatz, S.4    Su, M.S.5    Kuida, K.6
  • 12
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J, Lee J, Bibbs L, Ulevitch R. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 1994; 265:808-11.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.2    Bibbs, L.3    Ulevitch, R.4
  • 13
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J, Gupta S, Dickens M, Han J. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem 1995; 270:7420-6.
    • (1995) J Biol Chem , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Dickens, M.3    Han, J.4
  • 15
    • 0033118607 scopus 로고    scopus 로고
    • The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development
    • Kuan CY, Yang DD, Roy DRS, Davis RJ, Rakic P, Flavell RA. The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 1999; 22:667-76.
    • (1999) Neuron , vol.22 , pp. 667-676
    • Kuan, C.Y.1    Yang, D.D.2    Roy, D.R.S.3    Davis, R.J.4    Rakic, P.5    Flavell, R.A.6
  • 16
    • 0842329801 scopus 로고    scopus 로고
    • 2/M transit independent of p53, leading to endoreduplication, decreased proliferation, and apoptosis in breast cancer cells
    • 2/M transit independent of p53, leading to endoreduplication, decreased proliferation, and apoptosis in breast cancer cells. Oncogene 2004; 23:596-604.
    • (2004) Oncogene , vol.23 , pp. 596-604
    • Mingo-Sion, A.1    Marietta, P.2    Koller, E.3    Wolf, D.4    Van Den Berg, C.5
  • 18
    • 0032724021 scopus 로고    scopus 로고
    • Defective neural tube morphogenesis and altered apoptosis in the absence of both JNK1 and JNK2
    • Sabapathy K, Jochum W, Hochedlinger K, Chang L, Karin M, Wagner EF. Defective neural tube morphogenesis and altered apoptosis in the absence of both JNK1 and JNK2. Mech Dev 1999; 89:115-24.
    • (1999) Mech Dev , vol.89 , pp. 115-124
    • Sabapathy, K.1    Jochum, W.2    Hochedlinger, K.3    Chang, L.4    Karin, M.5    Wagner, E.F.6
  • 19
    • 0035808769 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase (JNK)1 and JNK2 have similar and stage-dependent roles in regulating T cell apoptosis and proliferation
    • Sabapathy K, Kallunki T, David JP, Graef I, Karin M, Wagner EF. c-Jun NH2-terminal kinase (JNK)1 and JNK2 have similar and stage-dependent roles in regulating T cell apoptosis and proliferation. J Exp Med 2001; 193:317-28.
    • (2001) J Exp Med , vol.193 , pp. 317-328
    • Sabapathy, K.1    Kallunki, T.2    David, J.P.3    Graef, I.4    Karin, M.5    Wagner, E.F.6
  • 22
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002; 298:1911-2.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 23
    • 0344393408 scopus 로고    scopus 로고
    • Regulation of MAP kinase signaling modules by scaffold proteins in mammals
    • Morrison DK, Davis RJ. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu Rev Cell Dev Biol 2003; 19:91-118.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 91-118
    • Morrison, D.K.1    Davis, R.J.2
  • 24
    • 0033081066 scopus 로고    scopus 로고
    • Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry
    • Brunet A, Roux D, Lenormand P, Dowd S, Keyse S, Pouysségur J. Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry. EMBO J 1999; 18:664-74.
    • (1999) EMBO J , vol.18 , pp. 664-674
    • Brunet, A.1    Roux, D.2    Lenormand, P.3    Dowd, S.4    Keyse, S.5    Pouysségur, J.6
  • 25
    • 0035877590 scopus 로고    scopus 로고
    • Regulation of nuclear localization during signaling
    • Cyert MS. Regulation of nuclear localization during signaling. J Biol Chem 2001; 276:20805-8.
    • (2001) J Biol Chem , vol.276 , pp. 20805-20808
    • Cyert, M.S.1
  • 26
    • 0031852068 scopus 로고    scopus 로고
    • Growth factor-induced p42/p44 MAPK nuclear translocation and retention requires both MAPK activation and neosynthesis of nuclear anchoring proteins
    • Lenormand P, Brondello JM, Brunet A, Pouyssegur J. Growth factor-induced p42/p44 MAPK nuclear translocation and retention requires both MAPK activation and neosynthesis of nuclear anchoring proteins. J Cell Biol 1998; 142:625-33.
    • (1998) J Cell Biol , vol.142 , pp. 625-633
    • Lenormand, P.1    Brondello, J.M.2    Brunet, A.3    Pouyssegur, J.4
  • 27
    • 0036983115 scopus 로고    scopus 로고
    • The Ras-Raf-MEK-ERK pathway in the treatment of cancer
    • Hilger R, Scheulen M, Strumberg D. The Ras-Raf-MEK-ERK pathway in the treatment of cancer. Onkologie 2002; 25:511-8.
    • (2002) Onkologie , vol.25 , pp. 511-518
    • Hilger, R.1    Scheulen, M.2    Strumberg, D.3
  • 28
    • 0035908493 scopus 로고    scopus 로고
    • Blocking oncogenic Ras signaling for cancer therapy
    • Adjei AA. Blocking oncogenic Ras signaling for cancer therapy. J Natl Cancer Inst 2001; 93:1062-74.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 1062-1074
    • Adjei, A.A.1
  • 32
    • 0033848878 scopus 로고    scopus 로고
    • 1 phase cell cycle machinery
    • 1 phase cell cycle machinery. Bioessays 2000; 22:818-26.
    • (2000) Bioessays , vol.22 , pp. 818-826
    • Roovers, K.1    Assoian, R.2
  • 33
    • 0031028381 scopus 로고    scopus 로고
    • Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway
    • Pumiglia KM, Decker SJ. Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway. Proc Natl Acad Sci USA 1997; 94:448-52.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 448-452
    • Pumiglia, K.M.1    Decker, S.J.2
  • 34
    • 0027938209 scopus 로고
    • Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
    • Hunter T, Pines J. Cyclins and cancer II: Cyclin D and CDK inhibitors come of age. Cell 1994; 79:573.
    • (1994) Cell , vol.79 , pp. 573
    • Hunter, T.1    Pines, J.2
  • 35
    • 0142068802 scopus 로고    scopus 로고
    • Cyclin-dependent kinases and S phase control in mammalian cells
    • Woo R, Poon R. Cyclin-dependent kinases and S phase control in mammalian cells. Cell Cycle 2003; 2:316-24.
    • (2003) Cell Cycle , vol.2 , pp. 316-324
    • Woo, R.1    Poon, R.2
  • 36
    • 4043064372 scopus 로고    scopus 로고
    • Mammalian pyrimidine biosynthesis: Fresh insights into an ancient pathway
    • Evans DR, Guy HI. Mammalian pyrimidine biosynthesis: Fresh insights into an ancient pathway. J Biol Chem 2004; 279:33035-8.
    • (2004) J Biol Chem , vol.279 , pp. 33035-33038
    • Evans, D.R.1    Guy, H.I.2
  • 37
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M, Clifton A, Lucocq J, Alessi D. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J 1998; 17:4426-41.
    • (1998) EMBO J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.2    Lucocq, J.3    Alessi, D.4
  • 38
    • 0141613756 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3, what for?
    • Prigent C, Dimitrov S. Phosphorylation of serine 10 in histone H3, what for? J Cell Sci 2003; 116:3677-85.
    • (2003) J Cell Sci , vol.116 , pp. 3677-3685
    • Prigent, C.1    Dimitrov, S.2
  • 39
    • 1242272924 scopus 로고    scopus 로고
    • The MAP kinase pathway is required for entry into mitosis and cell survival
    • Liu X, Yan S, Zhou T, Terada Y, Erikson R. The MAP kinase pathway is required for entry into mitosis and cell survival. oncogene 2004; 23:763-76.
    • (2004) Oncogene , vol.23 , pp. 763-776
    • Liu, X.1    Yan, S.2    Zhou, T.3    Terada, Y.4    Erikson, R.5
  • 40
    • 0037066686 scopus 로고    scopus 로고
    • ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53
    • Tang D. ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53. J Biol Chem 2002; 277:12710-7.
    • (2002) J Biol Chem , vol.277 , pp. 12710-12717
    • Tang, D.1
  • 41
    • 0032555891 scopus 로고    scopus 로고
    • Activation of the MKK/ERK pathway during somatic cell mitosis: Direct interactions of active ERK with kinetochores and regulation of the mitotic 3F3/2 phosphoantigen
    • Shapiro PS, Vaisberg E, Hunt AJ, Tolwinski NS, Whalen AM, McIntosh JR, Ahn NG. Activation of the MKK/ERK pathway during somatic cell mitosis: Direct interactions of active ERK with kinetochores and regulation of the mitotic 3F3/2 phosphoantigen. J Cell Biol 1998; 142:1533-45.
    • (1998) J Cell Biol , vol.142 , pp. 1533-1545
    • Shapiro, P.S.1    Vaisberg, E.2    Hunt, A.J.3    Tolwinski, N.S.4    Whalen, A.M.5    McIntosh, J.R.6    Ahn, N.G.7
  • 42
    • 0034910662 scopus 로고    scopus 로고
    • MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: A role for the MAP kinase pathway in regulating mitotic exit
    • Willard FS, Crouch MF. MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: A role for the MAP kinase pathway in regulating mitotic exit. Cell Signal 2001; 13:653-64.
    • (2001) Cell Signal , vol.13 , pp. 653-664
    • Willard, F.S.1    Crouch, M.F.2
  • 44
    • 0042696987 scopus 로고    scopus 로고
    • Phosphorylation of Cdc20 is required for its inhibition by the spindle checkpoint
    • Chung E, Chen RH. Phosphorylation of Cdc20 is required for its inhibition by the spindle checkpoint. Nat Cell Biol 2003; 5:748-53.
    • (2003) Nat Cell Biol , vol.5 , pp. 748-753
    • Chung, E.1    Chen, R.H.2
  • 45
    • 0037009056 scopus 로고    scopus 로고
    • Rapid microtubule-independent dynamics of Cdc20 at kinetochores and centrosomes in mammalian cells
    • Kallio MJ, Beardmore VA, Weinstein J, Gorbsky GJ. Rapid microtubule-independent dynamics of Cdc20 at kinetochores and centrosomes in mammalian cells. J Cell Biol 2002; 158:841-7.
    • (2002) J Cell Biol , vol.158 , pp. 841-847
    • Kallio, M.J.1    Beardmore, V.A.2    Weinstein, J.3    Gorbsky, G.J.4
  • 47
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38β)
    • Jiang Y, Chen C, Li Z, Guo W, Gegner JA, Lin S, Han J. Characterization of the structure and function of a new mitogen-activated protein kinase (p38β). J Biol Chem 1996; 271:17920-6.
    • (1996) J Biol Chem , vol.271 , pp. 17920-17926
    • Jiang, Y.1    Chen, C.2    Li, Z.3    Guo, W.4    Gegner, J.A.5    Lin, S.6    Han, J.7
  • 48
    • 0030828701 scopus 로고    scopus 로고
    • Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38δ
    • Jiang Y, Gram H, Zhao M, New L, Gu J, Feng L, Di Padova F, Ulevitch RJ, Han J. Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38δ. J Biol Chem 1997; 272:30122-8.
    • (1997) J Biol Chem , vol.272 , pp. 30122-30128
    • Jiang, Y.1    Gram, H.2    Zhao, M.3    New, L.4    Gu, J.5    Feng, L.6    Di Padova, F.7    Ulevitch, R.J.8    Han, J.9
  • 49
    • 0030581626 scopus 로고    scopus 로고
    • The Primary Structure of p38γ: A new member of p38 group of MAP kinases
    • Li Z, Jiang Y, Ulevitch RJ, Han J. The Primary Structure of p38γ: A new member of p38 group of MAP kinases. Biochem Biophys Res Commun 1996; 228:334.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 334
    • Li, Z.1    Jiang, Y.2    Ulevitch, R.J.3    Han, J.4
  • 51
    • 0034610981 scopus 로고    scopus 로고
    • Deficiency of the stress kinase p38α results in embryonic lethality: Characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells
    • Allen M, Svensson L, Roach M, Hambor J, McNeish J, Gabel CA. Deficiency of the stress kinase p38α results in embryonic lethality: Characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells. J Exp Med 2000; 191:859-70.
    • (2000) J Exp Med , vol.191 , pp. 859-870
    • Allen, M.1    Svensson, L.2    Roach, M.3    Hambor, J.4    McNeish, J.5    Gabel, C.A.6
  • 54
    • 20444385832 scopus 로고    scopus 로고
    • Activation of p38 has opposing effects on the proliferation and migration of endothelial cells
    • McMullen ME, Bryant PW, Glembotski CC, Vincent PA, Pumiglia KM. Activation of p38 has opposing effects on the proliferation and migration of endothelial cells. J Biol Chem 2005; 280:20995-1003.
    • (2005) J Biol Chem , vol.280 , pp. 20995-21003
    • McMullen, M.E.1    Bryant, P.W.2    Glembotski, C.C.3    Vincent, P.A.4    Pumiglia, K.M.5
  • 55
    • 0034634574 scopus 로고    scopus 로고
    • Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2-dependent manner
    • Casanovas O, Miro F, Estanyol JM, Itarte E, Agell N, Bachs O. Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2-dependent manner. J Biol Chem 2000; 275:35091-7.
    • (2000) J Biol Chem , vol.275 , pp. 35091-35097
    • Casanovas, O.1    Miro, F.2    Estanyol, J.M.3    Itarte, E.4    Agell, N.5    Bachs, O.6
  • 56
    • 0037119470 scopus 로고    scopus 로고
    • The stress-activated protein kinases p38α and JNK1 stabilize p21Cip1 by phosphorylation
    • Kim GY, Mercer SE, Ewton DZ, Yan Z, Jin K, Friedman E. The stress-activated protein kinases p38α and JNK1 stabilize p21Cip1 by phosphorylation. J Biol Chem 2002; 277:29792-802.
    • (2002) J Biol Chem , vol.277 , pp. 29792-29802
    • Kim, G.Y.1    Mercer, S.E.2    Ewton, D.Z.3    Yan, Z.4    Jin, K.5    Friedman, E.6
  • 58
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOG MAPK pathway
    • Lavoie JN, L'Allemain G, Brunet A, Muller R, Pouyssegur J. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOG MAPK pathway. J Biol Chem 1996; 271:20608-16.
    • (1996) J Biol Chem , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3    Muller, R.4    Pouyssegur, J.5
  • 59
    • 0242721598 scopus 로고    scopus 로고
    • The transcriptional repressor HBP1 is a target of the p38 mitogen-activated protein kinase pathway in cell cycle regulation
    • Xiu M, Kim J, Sampson E, Huang CY, Davis RJ, Paulson KE, Yee AS. The transcriptional repressor HBP1 is a target of the p38 mitogen-activated protein kinase pathway in cell cycle regulation. Mol Cell Biol 2003; 23:8890-901.
    • (2003) Mol Cell Biol , vol.23 , pp. 8890-8901
    • Xiu, M.1    Kim, J.2    Sampson, E.3    Huang, C.Y.4    Davis, R.J.5    Paulson, K.E.6    Yee, A.S.7
  • 61
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta S, Campbell D, Derijard B, Davis RJ. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 1995; 267:389-93
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Derijard, B.3    Davis, R.J.4
  • 62
    • 0034725079 scopus 로고    scopus 로고
    • Activating transcription factor 2 is necessary for maximal activity and serum induction of the cyclin a promoter in chondrocytes
    • Beier F, Taylor AC, LuValle P. Activating transcription factor 2 is necessary for maximal activity and serum induction of the cyclin A promoter in chondrocytes. J Biol Chem 2000; 275:12948-53.
    • (2000) J Biol Chem , vol.275 , pp. 12948-12953
    • Beier, F.1    Taylor, A.C.2    Luvalle, P.3
  • 63
    • 0037034199 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor activates proliferation in melanoma cells through p38 MAPK, ATF-2 and cyclin D1
    • Recio JA, Merlino G. Hepatocyte growth factor/scatter factor activates proliferation in melanoma cells through p38 MAPK, ATF-2 and cyclin D1. Oncogene 2002; 21:1000-8.
    • (2002) Oncogene , vol.21 , pp. 1000-1008
    • Recio, J.A.1    Merlino, G.2
  • 64
    • 0141841682 scopus 로고    scopus 로고
    • Apoptotic and mitogenic stimuli inactivate Rb by differential utilization of p38 and cyclin-dependent kinases
    • Nath N, Wang S, Betts V, Knudsen E, Chellappan S. Apoptotic and mitogenic stimuli inactivate Rb by differential utilization of p38 and cyclin-dependent kinases. Oncogene 2003; 22:5986-894.
    • (2003) Oncogene , vol.22 , pp. 5986-6894
    • Nath, N.1    Wang, S.2    Betts, V.3    Knudsen, E.4    Chellappan, S.5
  • 67
    • 0032562716 scopus 로고    scopus 로고
    • Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest
    • Takenaka K, Moriguchi T, Nishida E. Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science 1998; 280:599-602.
    • (1998) Science , vol.280 , pp. 599-602
    • Takenaka, K.1    Moriguchi, T.2    Nishida, E.3
  • 68
    • 0037025073 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase during normal mitosis in the developing retina
    • Campos CB, Bedard PA, Linden R. Activation of p38 mitogen-activated protein kinase during normal mitosis in the developing retina. Neurosci 2002; 112:583-91.
    • (2002) Neurosci , vol.112 , pp. 583-591
    • Campos, C.B.1    Bedard, P.A.2    Linden, R.3
  • 70
    • 0036629349 scopus 로고    scopus 로고
    • Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases
    • Aplin AE, Hogan BP, Tomeu J, Juliano RL. Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases. J Cell Sci 2002; 115:2781-90.
    • (2002) J Cell Sci , vol.115 , pp. 2781-2790
    • Aplin, A.E.1    Hogan, B.P.2    Tomeu, J.3    Juliano, R.L.4
  • 71
    • 0031018424 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced E-selectin expression is activated by the nuclear factor-κB and c-JUN N-terminal kinase/p38 mitogen-activated protein kinase pathways
    • Read MA, Whitley MZ, Gupta S, Pierce JW, Best J, Davis RJ, Collins T. Tumor necrosis factor alpha-induced E-selectin expression is activated by the nuclear factor-κB and c-JUN N-terminal kinase/p38 mitogen-activated protein kinase pathways. J Biol Chem 1997; 272:2753-61.
    • (1997) J Biol Chem , vol.272 , pp. 2753-2761
    • Read, M.A.1    Whitley, M.Z.2    Gupta, S.3    Pierce, J.W.4    Best, J.5    Davis, R.J.6    Collins, T.7
  • 72
    • 11244280883 scopus 로고    scopus 로고
    • JNK2 translocates to the mitochondria and mediates cytochrome c release in PC12 cells in response to 6-hydroxydopamine
    • Eminel S, Klettner A, Roemer L, Herdegen T, Waetzig V. JNK2 translocates to the mitochondria and mediates cytochrome c release in PC12 cells in response to 6-hydroxydopamine. J Biol Chem 2004; 279:55385-92.
    • (2004) J Biol Chem , vol.279 , pp. 55385-55392
    • Eminel, S.1    Klettner, A.2    Roemer, L.3    Herdegen, T.4    Waetzig, V.5
  • 74
    • 0030922083 scopus 로고    scopus 로고
    • A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion
    • Mizukami Y, Yoshioka K, Morimoto S, Yoshida KI. A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion. J Biol Chem 1997; 272:16657-62.
    • (1997) J Biol Chem , vol.272 , pp. 16657-16662
    • Mizukami, Y.1    Yoshioka, K.2    Morimoto, S.3    Yoshida, K.I.4
  • 75
    • 0031693211 scopus 로고    scopus 로고
    • p21WAF1 is dynamically associated with JNK in human T-lymphocytes during cell cycle progression
    • Patel R, Bartosch B, Blank JL. p21WAF1 is dynamically associated with JNK in human T-lymphocytes during cell cycle progression. J Cell Sci 1998; 111:2247-55.
    • (1998) J Cell Sci , vol.111 , pp. 2247-2255
    • Patel, R.1    Bartosch, B.2    Blank, J.L.3
  • 76
    • 1642523573 scopus 로고    scopus 로고
    • Inhibition of cell proliferation and cell cycle progression by specific inhibition of basal JNK activity: Evidence that mitotic Bcl-2 phosphorylation is JNK-independent
    • Du L, Lyle CS, Obey TB, Gaarde WA, Muir JA, Bennett BL, Chambers TC. Inhibition of cell proliferation and cell cycle progression by specific inhibition of basal JNK activity: Evidence that mitotic Bcl-2 phosphorylation is JNK-independent. J Biol Chem 2004; 279:11957-66.
    • (2004) J Biol Chem , vol.279 , pp. 11957-11966
    • Du, L.1    Lyle, C.S.2    Obey, T.B.3    Gaarde, W.A.4    Muir, J.A.5    Bennett, B.L.6    Chambers, T.C.7
  • 77
    • 4544371122 scopus 로고    scopus 로고
    • Inhibition of JNK2 disrupts anaphase and produces aneuploidy in mammalian cells
    • MacCorkle RA, Tan TH. Inhibition of JNK2 disrupts anaphase and produces aneuploidy in mammalian cells. J Biol Chem 2004; 279:40112-21.
    • (2004) J Biol Chem , vol.279 , pp. 40112-40121
    • MacCorkle, R.A.1    Tan, T.H.2
  • 79
    • 0037225749 scopus 로고    scopus 로고
    • Association of JNK1 with p21waf1 and p53: Modulation of JNK1 activity
    • Xue Y, Ramaswamy NT, Hong X, Pelling JC. Association of JNK1 with p21waf1 and p53: Modulation of JNK1 activity. Mol Carcinog 2003; 36:38-44.
    • (2003) Mol Carcinog , vol.36 , pp. 38-44
    • Xue, Y.1    Ramaswamy, N.T.2    Hong, X.3    Pelling, J.C.4
  • 81
    • 33745967219 scopus 로고    scopus 로고
    • Plumbagin induces apoptosis and cell cycle arrest in A549 cells through p53 accumulation via JNK-mediated phosphorylation at Serine 15 in vitro and in vivo
    • (jpet.105.098863)
    • Hsu YL, Cho CY, Kuo PL, Huang YT, Lin CC. Plumbagin induces apoptosis and cell cycle arrest in A549 cells through p53 accumulation via JNK-mediated phosphorylation at Serine 15 in vitro and in vivo. J Pharmacol Exp Ther 2006, (jpet.105.098863).
    • (2006) J Pharmacol Exp Ther
    • Hsu, Y.L.1    Cho, C.Y.2    Kuo, P.L.3    Huang, Y.T.4    Lin, C.C.5
  • 82
    • 4444341881 scopus 로고    scopus 로고
    • Distinct roles for JNK1 and JNK2 in regulating JNK activity and c-Jun-dependent cell proliferation
    • Sabapathy K, Hochedlinger K, Nam SY, Bauer A, Karin M, Wagner EF. Distinct roles for JNK1 and JNK2 in regulating JNK activity and c-Jun-dependent cell proliferation. Mol Cell 2004; 15:713-25.
    • (2004) Mol Cell , vol.15 , pp. 713-725
    • Sabapathy, K.1    Hochedlinger, K.2    Nam, S.Y.3    Bauer, A.4    Karin, M.5    Wagner, E.F.6
  • 83
    • 4644241390 scopus 로고    scopus 로고
    • JNKing revealed
    • Ronai Z. JNKing revealed. Mol Cell 2004; 15:843-4.
    • (2004) Mol Cell , vol.15 , pp. 843-844
    • Ronai, Z.1
  • 85
    • 0034096201 scopus 로고    scopus 로고
    • Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
    • Keyse SM. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr Opin Cell Biol 2000; 12:186-92.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 186-192
    • Keyse, S.M.1
  • 86
    • 0033800083 scopus 로고    scopus 로고
    • Extracellular signals and scores of phosphatases: All roads lead to MAP kinase
    • Saxena M, Mustelin T. Extracellular signals and scores of phosphatases: All roads lead to MAP kinase. Semin Immunol 2000; 12:387-96.
    • (2000) Semin Immunol , vol.12 , pp. 387-396
    • Saxena, M.1    Mustelin, T.2
  • 87
    • 1642355290 scopus 로고    scopus 로고
    • The dual-specific protein tyrosine phosphatase family
    • Alonso A, Rojas A, Godzik A, Mustelin T. The dual-specific protein tyrosine phosphatase family. Top Curr Genet 2003; 5:333-58.
    • (2003) Top Curr Genet , vol.5 , pp. 333-358
    • Alonso, A.1    Rojas, A.2    Godzik, A.3    Mustelin, T.4
  • 90
    • 0025865103 scopus 로고
    • A Tyr/Ser protein phosphatase encoded by Vaccinia virus
    • Guan KL, Bryoles SS, Dixon JE. A Tyr/Ser protein phosphatase encoded by Vaccinia virus. Nature 1991; 350:359-362.
    • (1991) Nature , vol.350 , pp. 359-362
    • Guan, K.L.1    Bryoles, S.S.2    Dixon, J.E.3
  • 91
    • 0033532067 scopus 로고    scopus 로고
    • Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway
    • Todd JL, Tanner KG, Denu JM. Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway. J Biol Chem 1999; 274:13271-80.
    • (1999) J Biol Chem , vol.274 , pp. 13271-13280
    • Todd, J.L.1    Tanner, K.G.2    Denu, J.M.3
  • 92
    • 0035895980 scopus 로고    scopus 로고
    • Inhibitory role for dual-specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation
    • Alonso A, Saxena M, Williams S, Mustelin T. Inhibitory role for dual-specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. J Biol Chem 2001; 276:4766-71.
    • (2001) J Biol Chem , vol.276 , pp. 4766-4771
    • Alonso, A.1    Saxena, M.2    Williams, S.3    Mustelin, T.4
  • 94
    • 0029757347 scopus 로고    scopus 로고
    • Disruption of the erp/mkp-1 gene does not affect mouse development: Normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts
    • Dorfman K, Carrasco D, Gruda M, Ryan C, Lira SA, Bravo R. Disruption of the erp/mkp-1 gene does not affect mouse development: Normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene 1996; 13:925-31.
    • (1996) Oncogene , vol.13 , pp. 925-931
    • Dorfman, K.1    Carrasco, D.2    Gruda, M.3    Ryan, C.4    Lira, S.A.5    Bravo, R.6
  • 95
    • 18144384775 scopus 로고    scopus 로고
    • Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling
    • Wu JJ, Bennett AM. Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling. J Biol Chem 2005; 280:16461-6.
    • (2005) J Biol Chem , vol.280 , pp. 16461-16466
    • Wu, J.J.1    Bennett, A.M.2
  • 96
    • 31144452241 scopus 로고    scopus 로고
    • Essential role of MAPK phosphatase-1 in the negative control of innate immune responses
    • Salojin KV, Owusu IB, Millerchip KA, Potter M, Platt KA, Oravecz T. Essential role of MAPK phosphatase-1 in the negative control of innate immune responses. J Immunol 2006; 176:1899-1907.
    • (2006) J Immunol , vol.176 , pp. 1899-1907
    • Salojin, K.V.1    Owusu, I.B.2    Millerchip, K.A.3    Potter, M.4    Platt, K.A.5    Oravecz, T.6
  • 97
    • 33144460185 scopus 로고    scopus 로고
    • Dynamic regulation of pro- and anti-inflammatory cytokines by MAPK phosphatase 1 (MKP-1) in innate immune responses
    • Chi H, Barry SP, Roth RJ, Wu JJ, Jones EA, Bennett AM, Flavell RA. Dynamic regulation of pro- and anti-inflammatory cytokines by MAPK phosphatase 1 (MKP-1) in innate immune responses. Proc Natl Acad Sci USA 2006; 103:2274-9.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2274-2279
    • Chi, H.1    Barry, S.P.2    Roth, R.J.3    Wu, J.J.4    Jones, E.A.5    Bennett, A.M.6    Flavell, R.A.7
  • 103
    • 24344455502 scopus 로고    scopus 로고
    • The dual-specificity protein phosphatase DUSP9/MKP-4 is essential for placental function but is not required for normal embryonic development
    • Christie GR, Williams DJ, Macisaac F, Dickinson RJ, Rosewell I, Keyse SM. The dual-specificity protein phosphatase DUSP9/MKP-4 is essential for placental function but is not required for normal embryonic development. Mol Cell Biol 2005; 25:8323-33.
    • (2005) Mol Cell Biol , vol.25 , pp. 8323-8333
    • Christie, G.R.1    Williams, D.J.2    Macisaac, F.3    Dickinson, R.J.4    Rosewell, I.5    Keyse, S.M.6
  • 104
    • 0032519787 scopus 로고    scopus 로고
    • Puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila
    • Martin-Blanco E, Gampel A, Ring J, Virdee K, Kirov N, Tolkovsky AM, Martinez-Arias A. Puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila. Genes Dev 1998; 12:557-70.
    • (1998) Genes Dev , vol.12 , pp. 557-570
    • Martin-Blanco, E.1    Gampel, A.2    Ring, J.3    Virdee, K.4    Kirov, N.5    Tolkovsky, A.M.6    Martinez-Arias, A.7
  • 105
    • 0035137910 scopus 로고    scopus 로고
    • Notch inhibition of RAS signaling through MAP kinase phosphatase LIP-1 during C. elegans vulval development
    • Berset T, Hoier EF, Battu G, Canevascini S, Hajnal A. Notch inhibition of RAS signaling through MAP kinase phosphatase LIP-1 during C. elegans vulval development. Science 2001; 291:1055-8.
    • (2001) Science , vol.291 , pp. 1055-1058
    • Berset, T.1    Hoier, E.F.2    Battu, G.3    Canevascini, S.4    Hajnal, A.5
  • 107
    • 0033661415 scopus 로고    scopus 로고
    • mVH1, a dual-specificity phosphatase whose expression is cell cycle regulated
    • Zhang XM, Dormady SP, Chaung W, Basch RS. mVH1, a dual-specificity phosphatase whose expression is cell cycle regulated. Mamm Genome 2000; 11:1154-6.
    • (2000) Mamm Genome , vol.11 , pp. 1154-1156
    • Zhang, X.M.1    Dormady, S.P.2    Chaung, W.3    Basch, R.S.4
  • 108
    • 10944240060 scopus 로고    scopus 로고
    • Closing mitosis: The functions of the Cdc14 phosphatase and its regulation
    • Stegmeier F, Amon A. Closing mitosis: The functions of the Cdc14 phosphatase and its regulation. Annu Rev Genet 2004; 38:203-32.
    • (2004) Annu Rev Genet , vol.38 , pp. 203-232
    • Stegmeier, F.1    Amon, A.2
  • 109
    • 0027339731 scopus 로고
    • Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase
    • Honda R, Ohba Y, Nagata A, Okayama H, Yasuda H. Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase. FEBS Lett 1993; 318:331-4.
    • (1993) FEBS Lett , vol.318 , pp. 331-334
    • Honda, R.1    Ohba, Y.2    Nagata, A.3    Okayama, H.4    Yasuda, H.5
  • 111
    • 0027269711 scopus 로고
    • Deregulation of cyclins D1 and e and suppression of cdk2 and cdk4 in senescent fibroblasts
    • Lucibello FC, Sewing A, Büsselbach S, Bürger C, Müller R. Deregulation of cyclins D1 and E and suppression of cdk2 and cdk4 in senescent fibroblasts. J Cell Sci 1993; 105:123-33.
    • (1993) J Cell Sci , vol.105 , pp. 123-133
    • Lucibello, F.C.1    Sewing, A.2    Büsselbach, S.3    Bürger, C.4    Müller, R.5
  • 113
    • 50549218525 scopus 로고
    • The limited in vitro lifetime of human diploid cell strains
    • Hayflick L. The limited in vitro lifetime of human diploid cell strains. Exp Cell Res 1965; 37:614-36.
    • (1965) Exp Cell Res , vol.37 , pp. 614-636
    • Hayflick, L.1
  • 114
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman D. The biologic clock: The mitochondria? J Am Geriatr Soc 1972; 20:145-7.
    • (1972) J Am Geriatr Soc , vol.20 , pp. 145-147
    • Harman, D.1
  • 115
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley CB, Futcher B, Greider CW. Telomeres shorten during ageing of human fibroblasts. Nature 1990; 345:458-60.
    • (1990) Nature , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, B.2    Greider, C.W.3
  • 117
    • 33646745137 scopus 로고    scopus 로고
    • Lamin A-dependent nuclear defects in human aging
    • Scaffidi P, Misteli T. Lamin A-dependent nuclear defects in human aging. Science 2006; 312:1059-63.
    • (2006) Science , vol.312 , pp. 1059-1063
    • Scaffidi, P.1    Misteli, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.