메뉴 건너뛰기




Volumn 232, Issue 3, 2008, Pages 408-417

Reciprocal regulation of extracellular signal regulated kinase 1/2 and mitogen activated protein kinase phosphatase-3

Author keywords

Extracellular signal regulated kinase; Mitogen activated protein kinase phosphatase 3; Ras

Indexed keywords

DUAL SPECIFICITY PHOSPHATASE 6; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 1; RAF PROTEIN; RAS PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 53349180575     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2008.08.007     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 0020586334 scopus 로고
    • Mouse skin carcinomas induced in vivo by chemical carcinogens have a transforming Harvey-ras oncogene
    • Balmain A., and Pragnell I.B. Mouse skin carcinomas induced in vivo by chemical carcinogens have a transforming Harvey-ras oncogene. Nature 303 (1983) 72-74
    • (1983) Nature , vol.303 , pp. 72-74
    • Balmain, A.1    Pragnell, I.B.2
  • 3
    • 0032571535 scopus 로고    scopus 로고
    • Induction of the mitogen-activated protein kinase phosphatase MKP3 by nerve growth factor in differentiating PC12
    • Camps M., Chabert C., Muda M., Boschert U., Gillieron C., and Arkinstall S. Induction of the mitogen-activated protein kinase phosphatase MKP3 by nerve growth factor in differentiating PC12. FEBS Lett. 425 (1998) 271-276
    • (1998) FEBS Lett. , vol.425 , pp. 271-276
    • Camps, M.1    Chabert, C.2    Muda, M.3    Boschert, U.4    Gillieron, C.5    Arkinstall, S.6
  • 4
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: a gene family for control of MAP kinase function
    • Camps M., Nichols A., and Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB. J. 14 (2000) 6-16
    • (2000) FASEB. J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 5
    • 7244254418 scopus 로고    scopus 로고
    • MAP kinase phosphatase 3 (MKP3) interacts with and is phosphorylated by protein kinase CK2alpha
    • Castelli M., Camps M., Gillieron C., Leroy D., Arkinstall S., Rommel C., and Nichols A. MAP kinase phosphatase 3 (MKP3) interacts with and is phosphorylated by protein kinase CK2alpha. J. Biol. Chem. 279 (2004) 44731-44739
    • (2004) J. Biol. Chem. , vol.279 , pp. 44731-44739
    • Castelli, M.1    Camps, M.2    Gillieron, C.3    Leroy, D.4    Arkinstall, S.5    Rommel, C.6    Nichols, A.7
  • 7
    • 0029918680 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation
    • Chu Y., Solski P.A., Khosravi-Far R., Der C.J., and Kelly K. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J. Biol. Chem. 271 (1996) 6497-6501
    • (1996) J. Biol. Chem. , vol.271 , pp. 6497-6501
    • Chu, Y.1    Solski, P.A.2    Khosravi-Far, R.3    Der, C.J.4    Kelly, K.5
  • 8
    • 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., and 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 102 (2003) 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
  • 10
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon A.S., Hagan S., Rath O., and Kolch W. MAP kinase signalling pathways in cancer. Oncogene 26 (2007) 3279-3290
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 11
    • 0031775763 scopus 로고    scopus 로고
    • Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases
    • Dowd S., Sneddon A.A., and Keyse S.M. Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases. J. Cell. Sci. 111 (1998) 3389-3399
    • (1998) J. Cell. Sci. , vol.111 , pp. 3389-3399
    • Dowd, S.1    Sneddon, A.A.2    Keyse, S.M.3
  • 12
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat. Rev. Cancer 3 (2003) 11-22
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 13
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A., and Zhou M.M. Structure and regulation of MAPK phosphatases. Cell Signal 16 (2004) 769-779
    • (2004) Cell Signal , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 14
    • 0030794511 scopus 로고    scopus 로고
    • Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells
    • Franklin C.C., and Kraft A.S. Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells. J. Biol. Chem. 272 (1997) 16917-16923
    • (1997) J. Biol. Chem. , vol.272 , pp. 16917-16923
    • Franklin, C.C.1    Kraft, A.S.2
  • 15
    • 0038243934 scopus 로고    scopus 로고
    • Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer
    • Furukawa T., Sunamura M., Motoi F., Matsuno S., and Horii A. Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer. Am. J. Pathol. 162 (2003) 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
  • 17
    • 0029905354 scopus 로고    scopus 로고
    • Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase
    • Groom L.A., Sneddon A.A., Alessi D.R., Dowd S., and Keyse S.M. Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase. EMBO J. 15 (1996) 3621-3632
    • (1996) EMBO J. , vol.15 , pp. 3621-3632
    • Groom, L.A.1    Sneddon, A.A.2    Alessi, D.R.3    Dowd, S.4    Keyse, S.M.5
  • 18
    • 0028921905 scopus 로고
    • Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase
    • Guan K.L., and Butch E. Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase. J. Biol. Chem. 270 (1995) 7197-7203
    • (1995) J. Biol. Chem. , vol.270 , pp. 7197-7203
    • Guan, K.L.1    Butch, E.2
  • 19
    • 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., and 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. 274 (1999) 26563-26571
    • (1999) J. Biol. Chem. , vol.274 , pp. 26563-26571
    • Kamakura, S.1    Moriguchi, T.2    Nishida, E.3
  • 20
    • 4744365623 scopus 로고    scopus 로고
    • Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal
    • Karlsson M., Mathers J., Dickinson R.J., Mandl M., and Keyse S.M. Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal. J. Biol. Chem. 279 (2004) 41882-41891
    • (2004) J. Biol. Chem. , vol.279 , pp. 41882-41891
    • Karlsson, M.1    Mathers, J.2    Dickinson, R.J.3    Mandl, M.4    Keyse, S.M.5
  • 22
    • 37549016809 scopus 로고    scopus 로고
    • Single and combined silencing of ERK1 and ERK2 reveals their positive contribution to growth signaling depending on their expression levels
    • Lefloch R., Pouyssegur J., and Lenormand P. Single and combined silencing of ERK1 and ERK2 reveals their positive contribution to growth signaling depending on their expression levels. Mol. Cell. Biol. 28 (2008) 511-527
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 511-527
    • Lefloch, R.1    Pouyssegur, J.2    Lenormand, P.3
  • 23
    • 0037474320 scopus 로고    scopus 로고
    • JAK/STAT but not ERK1/ERK2 pathway mediates interleukin (IL)-6/soluble IL-6R down-regulation of Type II collagen, aggrecan core, and link protein transcription in articular chondrocytes. Association with a down-regulation of SOX9 expression
    • Legendre F., Dudhia J., Pujol J.P., and Bogdanowicz P. JAK/STAT but not ERK1/ERK2 pathway mediates interleukin (IL)-6/soluble IL-6R down-regulation of Type II collagen, aggrecan core, and link protein transcription in articular chondrocytes. Association with a down-regulation of SOX9 expression. J. Biol. Chem. 278 (2003) 2903-2912
    • (2003) J. Biol. Chem. , vol.278 , pp. 2903-2912
    • Legendre, F.1    Dudhia, J.2    Pujol, J.P.3    Bogdanowicz, P.4
  • 24
    • 33846472047 scopus 로고    scopus 로고
    • Dusp6 (Mkp3) is a negative feedback regulator of FGF-stimulated ERK signaling during mouse development
    • Li C., Scott D.A., Hatch E., Tian X., and Mansour S.L. Dusp6 (Mkp3) is a negative feedback regulator of FGF-stimulated ERK signaling during mouse development. Development 134 (2007) 167-176
    • (2007) Development , vol.134 , pp. 167-176
    • Li, C.1    Scott, D.A.2    Hatch, E.3    Tian, X.4    Mansour, S.L.5
  • 26
    • 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., and 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. 25 (2005) 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
  • 27
    • 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 80 (1995) 179-185
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 28
    • 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., and 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. 274 (1999) 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
  • 29
    • 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., and Arkinstall S. MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase. J. Biol. Chem. 271 (1996) 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
  • 31
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy L.O., Smith S., Chen R.H., Fingar D.C., and Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell. Biol. 4 (2002) 556-564
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 32
    • 34248595035 scopus 로고    scopus 로고
    • Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases
    • Owens D.M., and Keyse S.M. Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases. Oncogene 26 (2007) 3203-3213
    • (2007) Oncogene , vol.26 , pp. 3203-3213
    • Owens, D.M.1    Keyse, S.M.2
  • 34
    • 34247888862 scopus 로고    scopus 로고
    • Dimerization in protein kinase signaling
    • Pelech S. Dimerization in protein kinase signaling. J. Biol. 5 (2006) 12.11-12.17
    • (2006) J. Biol. , vol.5
    • Pelech, S.1
  • 35
    • 0034672131 scopus 로고    scopus 로고
    • Compartment-specific regulation of extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) mitogen-activated protein kinases (MAPKs) by ERK-dependent and non-ERK-dependent inductions of MAPK phosphatase (MKP)-3 and MKP-1 in differentiating P19 cells
    • Reffas S., and Schlegel W. Compartment-specific regulation of extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) mitogen-activated protein kinases (MAPKs) by ERK-dependent and non-ERK-dependent inductions of MAPK phosphatase (MKP)-3 and MKP-1 in differentiating P19 cells. Biochem. J. 352 (2000) 701-708
    • (2000) Biochem. J. , vol.352 , pp. 701-708
    • Reffas, S.1    Schlegel, W.2
  • 38
    • 0027905014 scopus 로고
    • Altered growth of human colon cancer cell lines disrupted at activated Ki-ras
    • Shirasawa S., Furuse M., Yokoyama N., and Sasazuki T. Altered growth of human colon cancer cell lines disrupted at activated Ki-ras. Science 260 (1993) 85-88
    • (1993) Science , vol.260 , pp. 85-88
    • Shirasawa, S.1    Furuse, M.2    Yokoyama, N.3    Sasazuki, T.4
  • 41
    • 33845904217 scopus 로고    scopus 로고
    • ERK1 and ERK2 mitogen-activated protein kinases affect Ras-dependent cell signaling differentially
    • Vantaggiato C., Formentini I., Bondanza A., Bonini C., Naldini L., and Brambilla R. ERK1 and ERK2 mitogen-activated protein kinases affect Ras-dependent cell signaling differentially. J. Biol. 5 (2006) 14.1-14.15
    • (2006) J. Biol. , vol.5
    • Vantaggiato, C.1    Formentini, I.2    Bondanza, A.3    Bonini, C.4    Naldini, L.5    Brambilla, R.6
  • 42
    • 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., and Wattenberg E.V. Extracellular signal-regulated kinase transmits palytoxin-stimulated signals leading to altered gene expression in mouse keratinocytes. Toxicol. Appl. Pharmacol. 185 (2002) 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
  • 43
    • 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., and Wattenberg E.V. Mitogen-activated protein kinase phosphatase-3 is a tumor promoter target in initiated cells that express oncogenic Ras. J. Biol. Chem. 279 (2004) 33085-33092
    • (2004) J. Biol. Chem. , vol.279 , pp. 33085-33092
    • Warmka, J.K.1    Mauro, L.J.2    Wattenberg, E.V.3
  • 44
    • 33748748989 scopus 로고    scopus 로고
    • Phosphatase activation by EGF family ligands regulates Erk signaling in undifferentiated hen granulosa cells
    • Woods D.C., and Johnson A.L. Phosphatase activation by EGF family ligands regulates Erk signaling in undifferentiated hen granulosa cells. Endocrinology 336 (2006) 4931-4940
    • (2006) Endocrinology , vol.336 , pp. 4931-4940
    • Woods, D.C.1    Johnson, A.L.2
  • 46
    • 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. 17 (1998) 1-7
    • (1998) J. Dermatol. Sci. , vol.17 , pp. 1-7
    • Yuspa, S.H.1
  • 47
    • 0142219793 scopus 로고    scopus 로고
    • Mitogen activated protein kinases selectively regulate palytoxin-stimulated gene expression in mouse keratinocytes
    • Zeliadt N.A., Warmka J.K., and Wattenberg E.V. Mitogen activated protein kinases selectively regulate palytoxin-stimulated gene expression in mouse keratinocytes. Toxicol. Appl. Pharmacol. 192 (2003) 212-221
    • (2003) Toxicol. Appl. Pharmacol. , vol.192 , pp. 212-221
    • Zeliadt, N.A.1    Warmka, J.K.2    Wattenberg, E.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.