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Volumn 1803, Issue 9, 2010, Pages 1003-1012

DUSP26 negatively affects the proliferation of epithelial cells, an effect not mediated by dephosphorylation of MAPKs

Author keywords

Dual specificity phosphatase; MAP kinase; Phosphatase

Indexed keywords

DUAL SPECIFICITY PHOSPHATASE; DUAL SPECIFICITY PHOSPHATASE 26; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; DUSP26 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE;

EID: 77954951974     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.03.014     Document Type: Article
Times cited : (27)

References (57)
  • 2
    • 70350103909 scopus 로고    scopus 로고
    • A brief introduction to the protein phosphatase Families
    • Humana Press, Totowa, NJ, G. Moorhead (Ed.)
    • Mustelin T. A brief introduction to the protein phosphatase Families. Protein Phosphatase Protocols 2006, 9-22. Humana Press, Totowa, NJ. G. Moorhead (Ed.).
    • (2006) Protein Phosphatase Protocols , pp. 9-22
    • Mustelin, T.1
  • 3
    • 0028955176 scopus 로고
    • An emerging family of dual specificity MAP kinase phosphatases
    • Keyse S.M. An emerging family of dual specificity MAP kinase phosphatases. Biochim. Biophys. Acta 1995, 1265:152-160.
    • (1995) Biochim. Biophys. Acta , vol.1265 , pp. 152-160
    • Keyse, S.M.1
  • 4
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks N.K. Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell. Biol. 2006, 7:833-846.
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 5
    • 38949123682 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease
    • Pulido R., van Huijsduijnen R.H. Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease. FEBS J. 2008, 275:848-866.
    • (2008) FEBS J. , vol.275 , pp. 848-866
    • Pulido, R.1    van Huijsduijnen, R.H.2
  • 6
    • 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
  • 7
    • 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
  • 8
    • 33845693412 scopus 로고    scopus 로고
    • Diverse physiological functions for dual-specificity MAP kinase phosphatases
    • Dickinson R.J., Keyse S.M. Diverse physiological functions for dual-specificity MAP kinase phosphatases. J. Cell Sci. 2006, 119:4607-4615.
    • (2006) J. Cell Sci. , vol.119 , pp. 4607-4615
    • Dickinson, R.J.1    Keyse, S.M.2
  • 9
    • 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
  • 10
    • 34248210189 scopus 로고    scopus 로고
    • Targeting dual-specificity phosphatases: manipulating MAP kinase signalling and immune responses
    • Jeffrey K.L., Camps M., Rommel C., Mackay C.R. Targeting dual-specificity phosphatases: manipulating MAP kinase signalling and immune responses. Nat. Rev. Drug Discov. 2007, 6:391-403.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 391-403
    • Jeffrey, K.L.1    Camps, M.2    Rommel, C.3    Mackay, C.R.4
  • 11
    • 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
  • 13
    • 0030848639 scopus 로고    scopus 로고
    • Loss of heterozygosity at chromosomes 8p, 9p, and 14q is associated with stage and grade of non-papillary renal cell carcinomas
    • Schullerus D., Herbers J., Chudek J., Kanamaru H., Kovacs G. Loss of heterozygosity at chromosomes 8p, 9p, and 14q is associated with stage and grade of non-papillary renal cell carcinomas. J. Pathol. 1997, 183:151-155.
    • (1997) J. Pathol. , vol.183 , pp. 151-155
    • Schullerus, D.1    Herbers, J.2    Chudek, J.3    Kanamaru, H.4    Kovacs, G.5
  • 16
    • 0344873757 scopus 로고    scopus 로고
    • MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation
    • Hoornaert I., Marynen P., Goris J., Sciot R., Baens M. MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation. Oncogene 2003, 22:7728-7736.
    • (2003) Oncogene , vol.22 , pp. 7728-7736
    • Hoornaert, I.1    Marynen, P.2    Goris, J.3    Sciot, R.4    Baens, M.5
  • 17
    • 11244266433 scopus 로고    scopus 로고
    • Loss of heterozygosity analysis and DNA copy number measurement on 8p in bladder cancer reveals two mechanisms of allelic loss
    • Adams J., Williams S.V., Aveyard J.S., Knowles M.A. Loss of heterozygosity analysis and DNA copy number measurement on 8p in bladder cancer reveals two mechanisms of allelic loss. Cancer. Res 2005, 65:66-75.
    • (2005) Cancer. Res , vol.65 , pp. 66-75
    • Adams, J.1    Williams, S.V.2    Aveyard, J.S.3    Knowles, M.A.4
  • 18
    • 0028840684 scopus 로고
    • The dual-specificity phosphatase encoded by vaccinia virus, VH1, is essential for viral transcription in vivo and in vitro
    • Liu K., Lemon B., Traktman P. The dual-specificity phosphatase encoded by vaccinia virus, VH1, is essential for viral transcription in vivo and in vitro. J. Virol. 1995, 69:7823-7834.
    • (1995) J. Virol. , vol.69 , pp. 7823-7834
    • Liu, K.1    Lemon, B.2    Traktman, P.3
  • 19
    • 0034911991 scopus 로고    scopus 로고
    • A growing family of dual specificity phosphatases with low molecular masses
    • Aoki N., Aoyama K., Nagata M., Matsuda T. A growing family of dual specificity phosphatases with low molecular masses. J. Biochem. (Tokyo) 2001, 130:133-140.
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 133-140
    • Aoki, N.1    Aoyama, K.2    Nagata, M.3    Matsuda, T.4
  • 20
    • 62149114138 scopus 로고    scopus 로고
    • Dual-specificity phosphatases: critical regulators with diverse cellular targets
    • Patterson K.I., Brummer T., O'Brien P.M., Daly R.J. Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem. J. 2009, 418:475-489.
    • (2009) Biochem. J. , vol.418 , pp. 475-489
    • Patterson, K.I.1    Brummer, T.2    O'Brien, P.M.3    Daly, R.J.4
  • 22
    • 33645817920 scopus 로고    scopus 로고
    • Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26
    • Hu Y., Mivechi N.F. Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26. Mol. Cell. Biol. 2006, 26:3282-3294.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3282-3294
    • Hu, Y.1    Mivechi, N.F.2
  • 23
    • 33847219580 scopus 로고    scopus 로고
    • A novel amplification target, DUSP26, promotes anaplastic thyroid cancer cell growth by inhibiting p38 MAPK activity
    • Yu W., Imoto I., Inoue J., Onda M., Emi M., Inazawa J. A novel amplification target, DUSP26, promotes anaplastic thyroid cancer cell growth by inhibiting p38 MAPK activity. Oncogene 2006, 26:1178-1187.
    • (2006) Oncogene , vol.26 , pp. 1178-1187
    • Yu, W.1    Imoto, I.2    Inoue, J.3    Onda, M.4    Emi, M.5    Inazawa, J.6
  • 24
    • 34447520289 scopus 로고    scopus 로고
    • Characterization of a novel low-molecular-mass dual specificity phosphatase-4 (LDP-4) expressed in brain
    • Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M., Kikuchi K. Characterization of a novel low-molecular-mass dual specificity phosphatase-4 (LDP-4) expressed in brain. Mol. Cell. Biochem. 2006, 296:177-184.
    • (2006) Mol. Cell. Biochem. , vol.296 , pp. 177-184
    • Takagaki, K.1    Shima, H.2    Tanuma, N.3    Nomura, M.4    Satoh, T.5    Watanabe, M.6    Kikuchi, K.7
  • 25
    • 33745092405 scopus 로고    scopus 로고
    • Biochemical and biological characterization of a neuroendocrine-associated phosphatase
    • Wang J.Y., Lin C.H., Yang C.H., Tan T.H., Chen Y.R. Biochemical and biological characterization of a neuroendocrine-associated phosphatase. J. Neurochem. 2006, 98:89-101.
    • (2006) J. Neurochem. , vol.98 , pp. 89-101
    • Wang, J.Y.1    Lin, C.H.2    Yang, C.H.3    Tan, T.H.4    Chen, Y.R.5
  • 26
    • 56749177443 scopus 로고    scopus 로고
    • NEAP causes down-regulation of EGFR, subsequently induces the suppression of NGF-induced differentiation in PC12 cells
    • Wang J.Y., Yang C.H., Yeh C.L., Lin C.H., Chen Y.R. NEAP causes down-regulation of EGFR, subsequently induces the suppression of NGF-induced differentiation in PC12 cells. J. Neurochem. 2008, 107(6):1544-1555.
    • (2008) J. Neurochem. , vol.107 , Issue.6 , pp. 1544-1555
    • Wang, J.Y.1    Yang, C.H.2    Yeh, C.L.3    Lin, C.H.4    Chen, Y.R.5
  • 28
    • 62649160891 scopus 로고    scopus 로고
    • NSC-87877, inhibitor of SHP-1/2 PTPs, inhibits dual-specificity phosphatase 26 (DUSP26)
    • Song M., Park J.E., Park S.G., Lee Test H. NSC-87877, inhibitor of SHP-1/2 PTPs, inhibits dual-specificity phosphatase 26 (DUSP26). Biochem. Biophys. Res. Commun. 2009, 381:491-495.
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 491-495
    • Song, M.1    Park, J.E.2    Park, S.G.3    Lee Test, H.4
  • 31
    • 0036963241 scopus 로고    scopus 로고
    • Chromosome 8 genetic analysis and phenotypic characterization of 21 ovarian cancer cell lines
    • Arnold J.M., Woollatt E., Chenevix-Trench G. Chromosome 8 genetic analysis and phenotypic characterization of 21 ovarian cancer cell lines. Cancer Genet. Cytogenet. 2002, 139:109-114.
    • (2002) Cancer Genet. Cytogenet. , vol.139 , pp. 109-114
    • Arnold, J.M.1    Woollatt, E.2    Chenevix-Trench, G.3
  • 32
    • 33644850529 scopus 로고    scopus 로고
    • Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein
    • Brummer T., Schramek D., Hayes V.M., Bennett H.L., Caldon C.E., Musgrove E.A., Daly R.J. Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein. J. Biol. Chem. 2006, 281:626-637.
    • (2006) J. Biol. Chem. , vol.281 , pp. 626-637
    • Brummer, T.1    Schramek, D.2    Hayes, V.M.3    Bennett, H.L.4    Caldon, C.E.5    Musgrove, E.A.6    Daly, R.J.7
  • 34
    • 0033199317 scopus 로고    scopus 로고
    • Uncoupling IL-2 signals that regulate T cell proliferation, survival, and Fas-mediated activation-induced cell death
    • Van Parijs L., Refaeli Y., Lord J.D., Nelson B.H., Abbas A.K., Baltimore D. Uncoupling IL-2 signals that regulate T cell proliferation, survival, and Fas-mediated activation-induced cell death. Immunity 1999, 11:281-288.
    • (1999) Immunity , vol.11 , pp. 281-288
    • Van Parijs, L.1    Refaeli, Y.2    Lord, J.D.3    Nelson, B.H.4    Abbas, A.K.5    Baltimore, D.6
  • 36
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost J.A., Steen H., Shapiro P., Lewis T., Ahn N., Shaw P.E., Cobb M.H. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 1997, 16:6426-6438.
    • (1997) EMBO J. , vol.16 , pp. 6426-6438
    • Frost, J.A.1    Steen, H.2    Shapiro, P.3    Lewis, T.4    Ahn, N.5    Shaw, P.E.6    Cobb, M.H.7
  • 37
    • 0037603113 scopus 로고    scopus 로고
    • Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures
    • Debnath J., Muthuswamy S.K., Brugge J.S. Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures. Methods 2003, 30:256-268.
    • (2003) Methods , vol.30 , pp. 256-268
    • Debnath, J.1    Muthuswamy, S.K.2    Brugge, J.S.3
  • 39
    • 34948820665 scopus 로고    scopus 로고
    • PAC1 is a direct transcription target of E2F-1 in apoptotic signaling
    • Wu J., Jin Y.J., Calaf G.M., Huang W.L., Yin Y. PAC1 is a direct transcription target of E2F-1 in apoptotic signaling. Oncogene 2007, 26:6526-6535.
    • (2007) Oncogene , vol.26 , pp. 6526-6535
    • Wu, J.1    Jin, Y.J.2    Calaf, G.M.3    Huang, W.L.4    Yin, Y.5
  • 40
    • 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., 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. 1996, 271:6497-6501.
    • (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
  • 41
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C., Cobb M.H., Shaw P.E. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J. 1995, 14:951-962.
    • (1995) EMBO J. , vol.14 , pp. 951-962
    • Gille, H.1    Kortenjann, M.2    Thomae, O.3    Moomaw, C.4    Slaughter, C.5    Cobb, M.H.6    Shaw, P.E.7
  • 42
    • 0033599014 scopus 로고    scopus 로고
    • ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry
    • Cruzalegui F.H., Cano E., Treisman R. ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry. Oncogene 1999, 18:7948-7957.
    • (1999) Oncogene , vol.18 , pp. 7948-7957
    • Cruzalegui, F.H.1    Cano, E.2    Treisman, R.3
  • 43
    • 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
  • 44
    • 0030906520 scopus 로고    scopus 로고
    • Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors
    • Whitmarsh A.J., Yang S.H., Su M.S., Sharrocks A.D., Davis R.J. Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors. Mol. Cell. Biol. 1997, 17:2360-2371.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2360-2371
    • Whitmarsh, A.J.1    Yang, S.H.2    Su, M.S.3    Sharrocks, A.D.4    Davis, R.J.5
  • 46
    • 31344466008 scopus 로고    scopus 로고
    • DNA methylation and gene silencing in cancer
    • Baylin S.B. DNA methylation and gene silencing in cancer. Nat. Clin. Pract. 2005, 2(Suppl 1):S4-11.
    • (2005) Nat. Clin. Pract. , vol.2 , Issue.SUPPL 1
    • Baylin, S.B.1
  • 47
    • 0040953269 scopus 로고    scopus 로고
    • A novel cytosolic dual specificity phosphatase, interacting with glucokinase, increases glucose phosphorylation rate
    • Munoz-Alonso M.J., Guillemain G., Kassis N., Girard J., Burnol A.F., Leturque A. A novel cytosolic dual specificity phosphatase, interacting with glucokinase, increases glucose phosphorylation rate. J. Biol. Chem. 2000, 275:32406-32412.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32406-32412
    • Munoz-Alonso, M.J.1    Guillemain, G.2    Kassis, N.3    Girard, J.4    Burnol, A.F.5    Leturque, A.6
  • 48
    • 35748980594 scopus 로고    scopus 로고
    • Cutting edge: selective tyrosine dephosphorylation of interferon-activated nuclear STAT5 by the VHR phosphatase
    • Hoyt R., Zhu W., Cerignoli F., Alonso A., Mustelin T., David M. Cutting edge: selective tyrosine dephosphorylation of interferon-activated nuclear STAT5 by the VHR phosphatase. J. Immunol. 2007, 179:3402-3406.
    • (2007) J. Immunol. , vol.179 , pp. 3402-3406
    • Hoyt, R.1    Zhu, W.2    Cerignoli, F.3    Alonso, A.4    Mustelin, T.5    David, M.6
  • 51
    • 0032493642 scopus 로고    scopus 로고
    • PIR1, a novel phosphatase that exhibits high affinity to RNA. ribonucleoprotein complexes
    • Yuan Y., Li D.M., Sun H. PIR1, a novel phosphatase that exhibits high affinity to RNA. ribonucleoprotein complexes. J. Biol. Chem. 1998, 273:20347-20353.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20347-20353
    • Yuan, Y.1    Li, D.M.2    Sun, H.3
  • 54
    • 33845973017 scopus 로고    scopus 로고
    • Mapping ERK2-MKP3 binding interfaces by hydrogen/deuterium exchange mass spectrometry
    • Zhou B., Zhang J., Liu S., Reddy S., Wang F., Zhang Z.Y. Mapping ERK2-MKP3 binding interfaces by hydrogen/deuterium exchange mass spectrometry. J. Biol. Chem. 2006, 281:38834-38844.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38834-38844
    • Zhou, B.1    Zhang, J.2    Liu, S.3    Reddy, S.4    Wang, F.5    Zhang, Z.Y.6
  • 56
    • 0032877013 scopus 로고    scopus 로고
    • Human DU145 prostate cancer cells overexpressing mitogen-activated protein kinase phosphatase-1 are resistant to Fas ligand-induced mitochondrial perturbations and cellular apoptosis
    • Srikanth S., Franklin C.C., Duke R.C., Kraft R.S. Human DU145 prostate cancer cells overexpressing mitogen-activated protein kinase phosphatase-1 are resistant to Fas ligand-induced mitochondrial perturbations and cellular apoptosis. Mol. Cell. Biochem. 1999, 199:169-178.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 169-178
    • Srikanth, S.1    Franklin, C.C.2    Duke, R.C.3    Kraft, R.S.4
  • 57
    • 0346059592 scopus 로고    scopus 로고
    • MKP-1-induced dephosphorylation of extracellular signal-regulated kinase is essential for triggering nitric oxide-induced apoptosis in human breast cancer cell lines: implications in breast cancer
    • Pervin S., Singh R., Freije W.A., Chaudhuri G. MKP-1-induced dephosphorylation of extracellular signal-regulated kinase is essential for triggering nitric oxide-induced apoptosis in human breast cancer cell lines: implications in breast cancer. Cancer Res. 2003, 63:8853-8860.
    • (2003) Cancer Res. , vol.63 , pp. 8853-8860
    • Pervin, S.1    Singh, R.2    Freije, W.A.3    Chaudhuri, G.4


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