메뉴 건너뛰기




Volumn 57, Issue 3, 2011, Pages 440-448

Modulation of protein kinase signaling cascades by palytoxin

Author keywords

Dual specificity phosphatase; Mitogen activated protein kinase; Na+, K+ ATPase; Palytoxin; Tumor promoter

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); DUAL SPECIFICITY PHOSPHATASE 6; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE P38; PALYTOXIN; PROTEIN SERINE THREONINE KINASE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN;

EID: 79952317589     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2010.11.003     Document Type: Article
Times cited : (21)

References (91)
  • 1
    • 0029896250 scopus 로고    scopus 로고
    • Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase
    • Abe J., Kusuhara M., Ulevitch R.J., Berk B.C., Lee J.D. Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase. J. Biol. Chem. 1996, 271:16586-16590.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16586-16590
    • Abe, J.1    Kusuhara, M.2    Ulevitch, R.J.3    Berk, B.C.4    Lee, J.D.5
  • 2
    • 0035418622 scopus 로고    scopus 로고
    • Activated extracellular signal-regulated kinases: association with epidermal growth factor receptor/transforming growth factor alpha expression in head and neck squamous carcinoma and inhibition by anti-epidermal growth factor receptor treatments
    • Albanell J., Codony-Servat J., Rojo F., Del Campo J.M., Sauleda S., Anido J., Raspall G., Giralt J., Rosello J., Nicholson R.I., Mendelsohn J., Baselga J. Activated extracellular signal-regulated kinases: association with epidermal growth factor receptor/transforming growth factor alpha expression in head and neck squamous carcinoma and inhibition by anti-epidermal growth factor receptor treatments. Cancer Res. 2001, 61:6500-6510.
    • (2001) Cancer Res. , vol.61 , pp. 6500-6510
    • Albanell, J.1    Codony-Servat, J.2    Rojo, F.3    Del Campo, J.M.4    Sauleda, S.5    Anido, J.6    Raspall, G.7    Giralt, J.8    Rosello, J.9    Nicholson, R.I.10    Mendelsohn, J.11    Baselga, J.12
  • 3
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
    • Angel P., Karin M. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1991, 1072:129-157.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 4
    • 0020586334 scopus 로고
    • Mouse skin carcinomas induced in vivo by chemical carcinogens have a transforming Harvey-ras oncogene
    • Balmain A., Pragnell I.B. Mouse skin carcinomas induced in vivo by chemical carcinogens have a transforming Harvey-ras oncogene. Nature 1983, 303:72-74.
    • (1983) Nature , vol.303 , pp. 72-74
    • Balmain, A.1    Pragnell, I.B.2
  • 6
    • 0024210669 scopus 로고
    • Effects of palytoxin or ouabain on growth and squamous differentiation of human bronchial epithelial cells in vitro
    • Bonnard C., Lechner J.F., Gerwin B.I., Fujiki H., Harris C.C. Effects of palytoxin or ouabain on growth and squamous differentiation of human bronchial epithelial cells in vitro. Carcinogenesis 1988, 9:2245-2249.
    • (1988) Carcinogenesis , vol.9 , pp. 2245-2249
    • Bonnard, C.1    Lechner, J.F.2    Gerwin, B.I.3    Fujiki, H.4    Harris, C.C.5
  • 7
    • 33645072441 scopus 로고    scopus 로고
    • P44 mitogen-activated protein kinase (extracellular signal-regulated kinase 1)-dependent signaling contributes to epithelial skin carcinogenesis
    • Bourcier C., Jacquel A., Hess J., Peyrottes I., Angel P., Hofman P., Auberger P., Pouyssegur J., Pages G. p44 mitogen-activated protein kinase (extracellular signal-regulated kinase 1)-dependent signaling contributes to epithelial skin carcinogenesis. Cancer Res. 2006, 66:2700-2707.
    • (2006) Cancer Res. , vol.66 , pp. 2700-2707
    • Bourcier, C.1    Jacquel, A.2    Hess, J.3    Peyrottes, I.4    Angel, P.5    Hofman, P.6    Auberger, P.7    Pouyssegur, J.8    Pages, G.9
  • 8
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: a gene family for control of MAP kinase function
    • Camps M., Nichols A., Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. Faseb J. 2000, 14:6-16.
    • (2000) Faseb J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 9
    • 0033579552 scopus 로고    scopus 로고
    • MEKK3 directly regulates MEK5 activity as part of the big mitogen-activated protein kinase 1 (BMK1) signaling pathway
    • Chao T.H., Hayashi M., Tapping R.I., Kato Y., Lee J.D. MEKK3 directly regulates MEK5 activity as part of the big mitogen-activated protein kinase 1 (BMK1) signaling pathway. J. Biol. Chem. 1999, 274:36035-36038.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36035-36038
    • Chao, T.H.1    Hayashi, M.2    Tapping, R.I.3    Kato, Y.4    Lee, J.D.5
  • 10
    • 70350214528 scopus 로고    scopus 로고
    • Extracellular signal regulated kinase 5 mediates signals triggered by the novel tumor promoter palytoxin
    • Charlson A.T., Zeliadt N.A., Wattenberg E.V. Extracellular signal regulated kinase 5 mediates signals triggered by the novel tumor promoter palytoxin. Toxicol. Appl. Pharmacol. 2009, 241:143-153.
    • (2009) Toxicol. Appl. Pharmacol. , vol.241 , pp. 143-153
    • Charlson, A.T.1    Zeliadt, N.A.2    Wattenberg, E.V.3
  • 13
    • 0141481982 scopus 로고    scopus 로고
    • Gene profiling of a myeloma cell line reveals similarities and unique signatures among IL-6 response, N-ras-activating mutations, and coculture with bone marrow stromal cells
    • Croonquist P.A., Linden M.A., Zhao F., Van Ness B.G. Gene profiling of a myeloma cell line reveals similarities and unique signatures among IL-6 response, N-ras-activating mutations, and coculture with bone marrow stromal cells. Blood 2003, 102:2581-2592.
    • (2003) Blood , vol.102 , pp. 2581-2592
    • Croonquist, P.A.1    Linden, M.A.2    Zhao, F.3    Van Ness, B.G.4
  • 14
    • 34248563299 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase kinase kinases in signal integration
    • Cuevas B.D., Abell A.N., Johnson G.L. Role of mitogen-activated protein kinase kinase kinases in signal integration. Oncogene 2007, 26:3159-3171.
    • (2007) Oncogene , vol.26 , pp. 3159-3171
    • Cuevas, B.D.1    Abell, A.N.2    Johnson, G.L.3
  • 15
    • 0028073283 scopus 로고
    • MAPKs: new JNK expands the group
    • Davis R.J. MAPKs: new JNK expands the group. Trends Biochem. Sci. 1994, 19:470-473.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 470-473
    • Davis, R.J.1
  • 16
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • Derijard B., Raingeaud J., Barrett T., Wu I.H., Han J., Ulevitch R.J., Davis R.J. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 1995, 267:682-685.
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 17
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon A.S., Hagan S., Rath O., Kolch W. MAP kinase signalling pathways in cancer. Oncogene 2007, 26:3279-3290.
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 18
    • 0034769309 scopus 로고    scopus 로고
    • Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells
    • Dinev D., Jordan B.W., Neufeld B., Lee J.D., Lindemann D., Rapp U.R., Ludwig S. Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells. EMBO Rep. 2001, 2:829-834.
    • (2001) EMBO Rep. , vol.2 , pp. 829-834
    • Dinev, D.1    Jordan, B.W.2    Neufeld, B.3    Lee, J.D.4    Lindemann, D.5    Rapp, U.R.6    Ludwig, S.7
  • 19
    • 3042522892 scopus 로고    scopus 로고
    • Stress-activated protein kinases-tumor suppressors or tumor initiators?
    • Engelberg D. Stress-activated protein kinases-tumor suppressors or tumor initiators?. Semin. Cancer Biol. 2004, 14:271-282.
    • (2004) Semin. Cancer Biol. , vol.14 , pp. 271-282
    • Engelberg, D.1
  • 20
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A., Zhou M.M. Structure and regulation of MAPK phosphatases. Cell Signal. 2004, 16:769-779.
    • (2004) Cell Signal. , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 23
    • 0022965231 scopus 로고
    • Palytoxin is a non-12-O-tetradecanoylphorbol-13-acetate type tumor promoter in two-stage mouse skin carcinogenesis
    • Fujiki H., Suganuma M., Nakayasu M., Hakii H., Horiuchi T., Takayama S., Sugimura T. Palytoxin is a non-12-O-tetradecanoylphorbol-13-acetate type tumor promoter in two-stage mouse skin carcinogenesis. Carcinogenesis 1986, 7:707-710.
    • (1986) Carcinogenesis , vol.7 , pp. 707-710
    • Fujiki, H.1    Suganuma, M.2    Nakayasu, M.3    Hakii, H.4    Horiuchi, T.5    Takayama, S.6    Sugimura, T.7
  • 24
    • 0038243934 scopus 로고    scopus 로고
    • Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer
    • Furukawa T., Sunamura M., Motoi F., Matsuno S., Horii A. Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer. Am. J. Pathol. 2003, 162:1807-1815.
    • (2003) Am. J. Pathol. , vol.162 , pp. 1807-1815
    • Furukawa, T.1    Sunamura, M.2    Motoi, F.3    Matsuno, S.4    Horii, A.5
  • 25
    • 0029379778 scopus 로고
    • Activation of ternary complex factor Elk-1 by stress-activated protein kinases
    • Gille H., Strahl T., Shaw P.E. Activation of ternary complex factor Elk-1 by stress-activated protein kinases. Curr. Biol. 1995, 5:1191-1200.
    • (1995) Curr. Biol. , vol.5 , pp. 1191-1200
    • Gille, H.1    Strahl, T.2    Shaw, P.E.3
  • 26
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • Griner E.M., Kazanietz M.G. Protein kinase C and other diacylglycerol effectors in cancer. Nat. Rev. Cancer 2007, 7:281-294.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 281-294
    • Griner, E.M.1    Kazanietz, M.G.2
  • 27
    • 0024470756 scopus 로고
    • Palytoxin acts through Na+, K+-ATPase
    • Habermann E. Palytoxin acts through Na+, K+-ATPase. Toxicon 1989, 27:1171-1187.
    • (1989) Toxicon , vol.27 , pp. 1171-1187
    • Habermann, E.1
  • 28
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAP kinase kinase (MKK6)
    • Han J., Lee J.D., Jiang Y., Li Z., Feng L., Ulevitch R.J. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J. Biol. Chem. 1996, 271:2886-2891.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2886-2891
    • Han, J.1    Lee, J.D.2    Jiang, Y.3    Li, Z.4    Feng, L.5    Ulevitch, R.J.6
  • 29
    • 12444285810 scopus 로고    scopus 로고
    • Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice
    • Hayashi M., Lee J.D. Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice. J. Mol. Med. 2004, 82:800-808.
    • (2004) J. Mol. Med. , vol.82 , pp. 800-808
    • Hayashi, M.1    Lee, J.D.2
  • 32
    • 0032488926 scopus 로고    scopus 로고
    • Loss of cellular K+ mimics ribotoxic stress. Inhibition of protein synthesis and activation of the stress kinases SEK1/MKK4, stress-activated protein kinase/c-Jun NH2-terminal kinase 1, and p38/HOG1 by palytoxin
    • Iordanov M.S., Magun B.E. Loss of cellular K+ mimics ribotoxic stress. Inhibition of protein synthesis and activation of the stress kinases SEK1/MKK4, stress-activated protein kinase/c-Jun NH2-terminal kinase 1, and p38/HOG1 by palytoxin. J. Biol. Chem. 1998, 273:3528-3534.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3528-3534
    • Iordanov, M.S.1    Magun, B.E.2
  • 33
    • 0033543549 scopus 로고    scopus 로고
    • Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus
    • Kamakura S., Moriguchi T., Nishida E. Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus. J. Biol. Chem. 1999, 274:26563-26571.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26563-26571
    • Kamakura, S.1    Moriguchi, T.2    Nishida, E.3
  • 35
    • 0030694387 scopus 로고    scopus 로고
    • BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C
    • Kato Y., Kravchenko V.V., Tapping R., Han J., Ulevitch R.J., Lee J.D. BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. EMBO J. 1997, 16:7054-7066.
    • (1997) EMBO J. , vol.16 , pp. 7054-7066
    • Kato, Y.1    Kravchenko, V.V.2    Tapping, R.3    Han, J.4    Ulevitch, R.J.5    Lee, J.D.6
  • 36
    • 0032531881 scopus 로고    scopus 로고
    • Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor
    • Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., Lee J.D. Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor. Nature 1998, 395:713-716.
    • (1998) Nature , vol.395 , 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
  • 37
    • 0034096201 scopus 로고    scopus 로고
    • Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
    • Keyse S.M. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr. Opin. Cell Biol. 2000, 12:186-192.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 186-192
    • Keyse, S.M.1
  • 38
    • 43049101029 scopus 로고    scopus 로고
    • Dual-specificity MAP kinase phosphatases (MKPs) and cancer
    • Keyse S.M. Dual-specificity MAP kinase phosphatases (MKPs) and cancer. Cancer Metastasis Rev. 2008, 27:253-261.
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 253-261
    • Keyse, S.M.1
  • 39
    • 0033151533 scopus 로고    scopus 로고
    • Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1
    • Kim S.C., Hahn J.S., Min Y.H., Yoo N.C., Ko Y.W., Lee W.J. Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1. Blood 1999, 93:3893-3899.
    • (1999) Blood , vol.93 , pp. 3893-3899
    • Kim, S.C.1    Hahn, J.S.2    Min, Y.H.3    Yoo, N.C.4    Ko, Y.W.5    Lee, W.J.6
  • 40
    • 0029664514 scopus 로고    scopus 로고
    • Activation of stress-activator protein kinase/c-Jun N-terminal kinase by the non-TPA-type tumor promoter palytoxin
    • Kuroki D.W., Bignami G.S., Wattenberg E.V. Activation of stress-activator protein kinase/c-Jun N-terminal kinase by the non-TPA-type tumor promoter palytoxin. Cancer Res. 1996, 56:637-644.
    • (1996) Cancer Res. , vol.56 , pp. 637-644
    • Kuroki, D.W.1    Bignami, G.S.2    Wattenberg, E.V.3
  • 41
    • 0030763913 scopus 로고    scopus 로고
    • Regulation of a c-Jun amino-terminal kinase/stress-activated protein kinase cascade by a sodium-dependent signal transduction pathway
    • Kuroki D.W., Minden A., Sanchez I., Wattenberg E.V. Regulation of a c-Jun amino-terminal kinase/stress-activated protein kinase cascade by a sodium-dependent signal transduction pathway. J. Biol. Chem. 1997, 272:23905-23911.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23905-23911
    • Kuroki, D.W.1    Minden, A.2    Sanchez, I.3    Wattenberg, E.V.4
  • 43
    • 0032135775 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinases by palytoxin and ouabain, two ligands for the Na+, K+-ATPase
    • Li S., Wattenberg E.V. Differential activation of mitogen-activated protein kinases by palytoxin and ouabain, two ligands for the Na+, K+-ATPase. Toxicol. Appl. Pharmacol. 1998, 151:377-384.
    • (1998) Toxicol. Appl. Pharmacol. , vol.151 , pp. 377-384
    • Li, S.1    Wattenberg, E.V.2
  • 44
    • 0032732969 scopus 로고    scopus 로고
    • Cell-type-specific activation of p38 protein kinase cascades by the novel tumor promoter palytoxin
    • Li S., Wattenberg E.V. Cell-type-specific activation of p38 protein kinase cascades by the novel tumor promoter palytoxin. Toxicol. Appl. Pharmacol. 1999, 160:109-119.
    • (1999) Toxicol. Appl. Pharmacol. , vol.160 , pp. 109-119
    • Li, S.1    Wattenberg, E.V.2
  • 46
    • 2342522780 scopus 로고    scopus 로고
    • Inducible expression of a MAP kinase phosphatase-3-GFP chimera specifically blunts fibroblast growth and ras-dependent tumor formation in nude mice
    • Marchetti S., Gimond C., Roux D., Gothie E., Pouyssegur J., Pages G. Inducible expression of a MAP kinase phosphatase-3-GFP chimera specifically blunts fibroblast growth and ras-dependent tumor formation in nude mice. J. Cell Physiol. 2004, 199:441-450.
    • (2004) J. Cell Physiol. , vol.199 , pp. 441-450
    • Marchetti, S.1    Gimond, C.2    Roux, D.3    Gothie, E.4    Pouyssegur, J.5    Pages, G.6
  • 47
    • 11844294679 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases phosphorylate mitogen-activated protein kinase phosphatase 3/DUSP6 at serines 159 and 197, two sites critical for its proteasomal degradation
    • Marchetti S., Gimond C., Chambard J.C., Touboul T., Roux D., Pouyssegur J., Pages G. Extracellular signal-regulated kinases phosphorylate mitogen-activated protein kinase phosphatase 3/DUSP6 at serines 159 and 197, two sites critical for its proteasomal degradation. Mol. Cell. Biol. 2005, 25:854-864.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 854-864
    • Marchetti, S.1    Gimond, C.2    Chambard, J.C.3    Touboul, T.4    Roux, D.5    Pouyssegur, J.6    Pages, G.7
  • 48
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation
    • Marshall C.J. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 1995, 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 49
    • 0033548181 scopus 로고    scopus 로고
    • Sustained activation of the mitogen-activated protein kinase pathway. A mechanism underlying receptor tyrosine kinase specificity for matrix metalloproteinase-9 induction and cell migration
    • McCawley L.J., Li S., Wattenberg E.V., Hudson L.G. Sustained activation of the mitogen-activated protein kinase pathway. A mechanism underlying receptor tyrosine kinase specificity for matrix metalloproteinase-9 induction and cell migration. J. Biol. Chem. 1999, 274:4347-4353.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4347-4353
    • McCawley, L.J.1    Li, S.2    Wattenberg, E.V.3    Hudson, L.G.4
  • 50
    • 29544441533 scopus 로고    scopus 로고
    • Enhancement of transformed foci and induction of prostaglandins in Balb/c 3T3 cells by palytoxin: in vitro model reproduces carcinogenic responses in animal models regarding the inhibitory effect of indomethacin and reversal of indomethacin's effect by exogenous prostaglandins
    • Miura D., Kobayashi M., Kakiuchi S., Kasahara Y., Kondo S. Enhancement of transformed foci and induction of prostaglandins in Balb/c 3T3 cells by palytoxin: in vitro model reproduces carcinogenic responses in animal models regarding the inhibitory effect of indomethacin and reversal of indomethacin's effect by exogenous prostaglandins. Toxicol. Sci. 2006, 89:154-163.
    • (2006) Toxicol. Sci. , vol.89 , pp. 154-163
    • Miura, D.1    Kobayashi, M.2    Kakiuchi, S.3    Kasahara, Y.4    Kondo, S.5
  • 51
    • 0038000461 scopus 로고    scopus 로고
    • An analysis of the phosphorylation and activation of extracellular-signal-regulated protein kinase 5 (ERK5) by mitogen-activated protein kinase kinase 5 (MKK5) in vitro
    • Mody N., Campbell D.G., Morrice N., Peggie M., Cohen P. An analysis of the phosphorylation and activation of extracellular-signal-regulated protein kinase 5 (ERK5) by mitogen-activated protein kinase kinase 5 (MKK5) in vitro. Biochem. J. 2003, 372:567-575.
    • (2003) Biochem. J. , vol.372 , pp. 567-575
    • Mody, N.1    Campbell, D.G.2    Morrice, N.3    Peggie, M.4    Cohen, P.5
  • 52
    • 10244241798 scopus 로고    scopus 로고
    • Purification and identification of a major activator for p38 from osmotically shocked cells. Activation of mitogen-activated protein kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and H2O2
    • Moriguchi T., Toyoshima F., Gotoh Y., Iwamatsu A., Irie K., Mori E., Kuroyanagi N., Hagiwara M., Matsumoto K., Nishida E. Purification and identification of a major activator for p38 from osmotically shocked cells. Activation of mitogen-activated protein kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and H2O2. J. Biol. Chem. 1996, 271:26981-26988.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26981-26988
    • Moriguchi, T.1    Toyoshima, F.2    Gotoh, Y.3    Iwamatsu, A.4    Irie, K.5    Mori, E.6    Kuroyanagi, N.7    Hagiwara, M.8    Matsumoto, K.9    Nishida, E.10
  • 53
    • 0030028222 scopus 로고    scopus 로고
    • MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase
    • Muda M., Boschert U., Dickinson R., Martinou J.C., Martinou I., Camps M., Schlegel W., Arkinstall S. MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase. J. Biol. Chem. 1996, 271:4319-4326.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4319-4326
    • Muda, M.1    Boschert, U.2    Dickinson, R.3    Martinou, J.C.4    Martinou, I.5    Camps, M.6    Schlegel, W.7    Arkinstall, S.8
  • 54
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy L.O., Smith S., Chen R., Fingar D.C., Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 2002, 4:556-564.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.3    Fingar, D.C.4    Blenis, J.5
  • 55
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 1984, 308:693-698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 56
    • 0030051528 scopus 로고    scopus 로고
    • MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway
    • Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 1996, 16:1247-1255.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1247-1255
    • Raingeaud, J.1    Whitmarsh, A.J.2    Barrett, T.3    Derijard, B.4    Davis, R.J.5
  • 57
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman M., Chen W., Cobb M.H. Differential regulation and properties of MAPKs. Oncogene 2007, 26:3100-3112.
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 58
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions
    • Roux P.P., Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 2004, 68:320-344.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 59
    • 73849141896 scopus 로고    scopus 로고
    • The cytotoxic pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins
    • Sala G.L., Bellocci M., Rossini G.P. The cytotoxic pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins. Chem. Res. Toxicol. 2009, 22:2009-2016.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 2009-2016
    • Sala, G.L.1    Bellocci, M.2    Rossini, G.P.3
  • 62
    • 33749057086 scopus 로고    scopus 로고
    • Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role
    • Sasaki T., Kojima H., Kishimoto R., Ikeda A., Kunimoto H., Nakajima K. Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role. Mol. Cell 2006, 24:63-75.
    • (2006) Mol. Cell , vol.24 , pp. 63-75
    • Sasaki, T.1    Kojima, H.2    Kishimoto, R.3    Ikeda, A.4    Kunimoto, H.5    Nakajima, K.6
  • 64
    • 0037400975 scopus 로고    scopus 로고
    • A pivotal role for ERK in the oncogenic behaviour of malignant melanoma?
    • Smalley K.S. A pivotal role for ERK in the oncogenic behaviour of malignant melanoma?. Int. J. Cancer 2003, 104:527-532.
    • (2003) Int. J. Cancer , vol.104 , pp. 527-532
    • Smalley, K.S.1
  • 65
    • 46949085472 scopus 로고    scopus 로고
    • Non-redundant function of the MEK5-ERK5 pathway in thymocyte apoptosis
    • Sohn S.J., Lewis G.M., Winoto A. Non-redundant function of the MEK5-ERK5 pathway in thymocyte apoptosis. EMBO J. 2008, 27:1896-1906.
    • (2008) EMBO J. , vol.27 , pp. 1896-1906
    • Sohn, S.J.1    Lewis, G.M.2    Winoto, A.3
  • 66
    • 0030006618 scopus 로고    scopus 로고
    • Cloning and characterization of MEK6, a novel member of the mitogen-activated protein kinase kinase cascade
    • Stein B., Brady H., Yang M.X., Young D.B., Barbosa M.S. Cloning and characterization of MEK6, a novel member of the mitogen-activated protein kinase kinase cascade. J. Biol. Chem. 1996, 271:11427-11433.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11427-11433
    • Stein, B.1    Brady, H.2    Yang, M.X.3    Young, D.B.4    Barbosa, M.S.5
  • 67
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 1992, 313:307-313.
    • (1992) FEBS Lett. , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 68
    • 0023875418 scopus 로고
    • Development of murine epidermal cell lines which contain an activated rasHa oncogene and form papillomas in skin grafts on athymic nude mouse hosts
    • Strickland J.E., Greenhalgh D.A., Koceva-Chyla A., Hennings H., Restrepo C., Balaschak M., Yuspa S.H. Development of murine epidermal cell lines which contain an activated rasHa oncogene and form papillomas in skin grafts on athymic nude mouse hosts. Cancer Res. 1988, 48:165-169.
    • (1988) Cancer Res. , vol.48 , pp. 165-169
    • Strickland, J.E.1    Greenhalgh, D.A.2    Koceva-Chyla, A.3    Hennings, H.4    Restrepo, C.5    Balaschak, M.6    Yuspa, S.H.7
  • 70
    • 0345736001 scopus 로고    scopus 로고
    • Regulation of c-Fos and Fra-1 by the MEK5-ERK5 pathway
    • Terasawa K., Okazaki K., Nishida E. Regulation of c-Fos and Fra-1 by the MEK5-ERK5 pathway. Genes Cells 2003, 8:263-273.
    • (2003) Genes Cells , vol.8 , pp. 263-273
    • Terasawa, K.1    Okazaki, K.2    Nishida, E.3
  • 71
    • 34248572839 scopus 로고    scopus 로고
    • MAP kinases and the control of nuclear events
    • Turjanski A.G., Vaque J.P., Gutkind J.S. MAP kinases and the control of nuclear events. Oncogene 2007, 26:3240-3253.
    • (2007) Oncogene , vol.26 , pp. 3240-3253
    • Turjanski, A.G.1    Vaque, J.P.2    Gutkind, J.S.3
  • 72
    • 34948890457 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases regulate palytoxin-induced calcium influx and cytotoxicity in cultured neurons
    • Vale C., Gomez-Limia B., Vieytes M.R., Botana L.M. Mitogen-activated protein kinases regulate palytoxin-induced calcium influx and cytotoxicity in cultured neurons. Br. J. Pharmacol. 2007, 152:256-266.
    • (2007) Br. J. Pharmacol. , vol.152 , pp. 256-266
    • Vale, C.1    Gomez-Limia, B.2    Vieytes, M.R.3    Botana, L.M.4
  • 73
    • 32144436881 scopus 로고    scopus 로고
    • Regulation of cellular functions by the ERK5 signalling pathway
    • Wang X., Tournier C. Regulation of cellular functions by the ERK5 signalling pathway. Cell. Signal. 2006, 18:753-760.
    • (2006) Cell. Signal. , vol.18 , pp. 753-760
    • Wang, X.1    Tournier, C.2
  • 74
    • 0036444273 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase transmits palytoxin-stimulated signals leading to altered gene expression in mouse keratinocytes
    • Warmka J.K., Winston S.E., Zeliadt N.A., Wattenberg E.V. Extracellular signal-regulated kinase transmits palytoxin-stimulated signals leading to altered gene expression in mouse keratinocytes. Toxicol. Appl. Pharmacol. 2002, 185:8-17.
    • (2002) Toxicol. Appl. Pharmacol. , vol.185 , pp. 8-17
    • Warmka, J.K.1    Winston, S.E.2    Zeliadt, N.A.3    Wattenberg, E.V.4
  • 75
    • 4043182010 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase-3 is a tumor promoter target in initiated cells that express oncogenic Ras
    • Warmka J.K., Mauro L.J., Wattenberg E.V. Mitogen-activated protein kinase phosphatase-3 is a tumor promoter target in initiated cells that express oncogenic Ras. J. Biol. Chem. 2004, 279:33085-33092.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33085-33092
    • Warmka, J.K.1    Mauro, L.J.2    Wattenberg, E.V.3
  • 76
    • 0023278958 scopus 로고
    • Heterologous regulation of the epidermal growth factor receptor by palytoxin, a non-12-O-tetradecanoylphorbol-13-acetate-type tumor promoter
    • Wattenberg E.V., Fujiki H., Rosner M.R. Heterologous regulation of the epidermal growth factor receptor by palytoxin, a non-12-O-tetradecanoylphorbol-13-acetate-type tumor promoter. Cancer Res. 1987, 47:4618-4622.
    • (1987) Cancer Res. , vol.47 , pp. 4618-4622
    • Wattenberg, E.V.1    Fujiki, H.2    Rosner, M.R.3
  • 77
    • 0024467201 scopus 로고
    • Sodium as a mediator of non-phorbol tumor promoter action. Down-modulation of the epidermal growth factor receptor by palytoxin
    • Wattenberg E.V., Byron K.L., Villereal M.L., Fujiki H., Rosner M.R. Sodium as a mediator of non-phorbol tumor promoter action. Down-modulation of the epidermal growth factor receptor by palytoxin. J. Biol. Chem. 1989, 264:14668-14673.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14668-14673
    • Wattenberg, E.V.1    Byron, K.L.2    Villereal, M.L.3    Fujiki, H.4    Rosner, M.R.5
  • 78
    • 0024529251 scopus 로고
    • Palytoxin down-modulates the epidermal growth factor receptor through a sodium-dependent pathway
    • Wattenberg E.V., McNeil P.L., Fujiki H., Rosner M.R. Palytoxin down-modulates the epidermal growth factor receptor through a sodium-dependent pathway. J. Biol. Chem. 1989, 264:213-219.
    • (1989) J. Biol. Chem. , vol.264 , pp. 213-219
    • Wattenberg, E.V.1    McNeil, P.L.2    Fujiki, H.3    Rosner, M.R.4
  • 79
  • 80
    • 33846277239 scopus 로고    scopus 로고
    • Palytoxin: exploiting a novel skin tumor promoter to explore signal transduction and carcinogenesis
    • Wattenberg E.V. Palytoxin: exploiting a novel skin tumor promoter to explore signal transduction and carcinogenesis. Am. J. Physiol. Cell Physiol. 2007, 292:C24-C32.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Wattenberg, E.V.1
  • 81
    • 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. 1996, 74:589-607.
    • (1996) J. Mol. Med. , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 82
    • 0029125757 scopus 로고
    • Integration of MAP kinase signal transduction pathways at the serum response element
    • Whitmarsh A.J., Shore P., Sharrocks A.D., Davis R.J. Integration of MAP kinase signal transduction pathways at the serum response element. Science 1995, 269:403-407.
    • (1995) Science , vol.269 , pp. 403-407
    • Whitmarsh, A.J.1    Shore, P.2    Sharrocks, A.D.3    Davis, R.J.4
  • 83
    • 2342487353 scopus 로고    scopus 로고
    • Na+-K+-ATPase-mediated signal transduction: from protein interaction to cellular function
    • Xie Z., Cai T. Na+-K+-ATPase-mediated signal transduction: from protein interaction to cellular function. Mol. Interv. 2003, 3:157-168.
    • (2003) Mol. Interv. , vol.3 , pp. 157-168
    • Xie, Z.1    Cai, T.2
  • 84
    • 0038578665 scopus 로고    scopus 로고
    • Molecular mechanisms of Na/K-ATPase-mediated signal transduction
    • Xie Z. Molecular mechanisms of Na/K-ATPase-mediated signal transduction. Ann. N. Y. Acad. Sci. 2003, 986:497-503.
    • (2003) Ann. N. Y. Acad. Sci. , vol.986 , pp. 497-503
    • Xie, Z.1
  • 85
    • 0034813635 scopus 로고    scopus 로고
    • Pancreatic tumor cells with mutant K-ras suppress ERK activity by MEK-dependent induction of MAP kinase phosphatase-2
    • Yip-Schneider M.T., Lin A., Marshall M.S. Pancreatic tumor cells with mutant K-ras suppress ERK activity by MEK-dependent induction of MAP kinase phosphatase-2. Biochem. Biophys. Res.Commun. 2001, 280:992-997.
    • (2001) Biochem. Biophys. Res.Commun. , vol.280 , pp. 992-997
    • Yip-Schneider, M.T.1    Lin, A.2    Marshall, M.S.3
  • 87
    • 0032076149 scopus 로고    scopus 로고
    • The pathogenesis of squamous cell cancer: lessons learned from studies of skin carcinogenesis
    • Yuspa S.H. The pathogenesis of squamous cell cancer: lessons learned from studies of skin carcinogenesis. J. Dermatol. Sci. 1998, 17:1-7.
    • (1998) J. Dermatol. Sci. , vol.17 , pp. 1-7
    • Yuspa, S.H.1
  • 88
    • 0142219793 scopus 로고    scopus 로고
    • Mitogen activated protein kinases selectively regulate palytoxin-stimulated gene expression in mouse keratinocytes
    • Zeliadt N.A., Warmka J.K., Wattenberg E.V. Mitogen activated protein kinases selectively regulate palytoxin-stimulated gene expression in mouse keratinocytes. Toxicol. Appl. Pharmacol. 2003, 192:212-221.
    • (2003) Toxicol. Appl. Pharmacol. , vol.192 , pp. 212-221
    • Zeliadt, N.A.1    Warmka, J.K.2    Wattenberg, E.V.3
  • 90
    • 53349180575 scopus 로고    scopus 로고
    • Reciprocal regulation of extracellular signal regulated kinase 1/2 and mitogen activated protein kinase phosphatase-3
    • Zeliadt N.A., Mauro L.J., Wattenberg E.V. Reciprocal regulation of extracellular signal regulated kinase 1/2 and mitogen activated protein kinase phosphatase-3. Toxicol. Appl. Pharmacol. 2008, 232:408-417.
    • (2008) Toxicol. Appl. Pharmacol. , vol.232 , pp. 408-417
    • Zeliadt, N.A.1    Mauro, L.J.2    Wattenberg, E.V.3
  • 91
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou G., Bao Z., Dixon J.E. Components of a new human protein kinase signal transduction pathway. J. Biol. Chem. 1995, 270:12665-12669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.2    Dixon, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.