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Volumn 63, Issue , 2013, Pages 313-324

Thioredoxin inhibits MPK38-induced ASK1, TGF?ß, and p53 function in a phosphorylation-dependent manner

Author keywords

ASK1; Free radicals; MPK38 MELK; P53; TGF ; Trx

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN P53; THIOREDOXIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 84879490199     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.05.020     Document Type: Article
Times cited : (36)

References (42)
  • 1
    • 0030878634 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells
    • DOI 10.1016/S0378-1119(97)00181-9, PII S0378111997001819
    • Gil, M.; Yang, Y.; Lee, Y.; Choi, I.; Ha, H. Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells. Gene 195: 295-301; 1997. (Pubitemid 27354707)
    • (1997) Gene , vol.195 , Issue.2 , pp. 295-301
    • Gil, M.1    Yang, Y.2    Lee, Y.3    Choi, I.4    Ha, H.5
  • 2
    • 0030898486 scopus 로고    scopus 로고
    • New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse egg and preimplantation embryo
    • Heyer, B. S.; Warsowe, J.; Solter, D.; Knowles, B. B.; Ackerman, S. L. New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse egg and preimplantation embryo. Mol. Reprod. Dev. 47: 148-156; 1997. (Pubitemid 27188223)
    • (1997) Molecular Reproduction and Development , vol.47 , Issue.2 , pp. 148-156
    • Heyer, B.S.1    Warsowe, J.2    Solter, D.3    Knowles, B.B.4    Ackerman, S.L.5
  • 3
    • 58049199391 scopus 로고    scopus 로고
    • Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr838 phosphorylation
    • Jung, H.; Seong, H.-A.; Ha, H. Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr838 phosphorylation. J. Biol. Chem 283: 34541-34553; 2008.
    • (2008) J. Biol. Chem , vol.283 , pp. 34541-34553
    • Jung, H.1    Seong, H.-A.2    Ha, H.3
  • 4
    • 80052418531 scopus 로고    scopus 로고
    • Positive regulation of apoptosis signal-regulating kinase 1 by ZPR9 protein, a zinc finger protein
    • Seong, H.-A.; Jung, H.; Manoharan, R.; Ha, H. Positive regulation of apoptosis signal-regulating kinase 1 by ZPR9 protein, a zinc finger protein. J. Biol. Chem. 286: 31123-31135; 2011.
    • (2011) J. Biol. Chem , vol.286 , pp. 31123-31135
    • Seong, H.-A.1    Jung, H.2    Manoharan, R.3    Ha, H.4
  • 5
    • 0036471923 scopus 로고    scopus 로고
    • Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine protein serine/threonine kinase 38 (MPK38)
    • DOI 10.1042/0264-6021:3610597
    • Seong, H.-A.; Gil, M.; Kim, K.-T.; Kim, S. J.; Ha, H. Phosphorylation of a novel zinc finger like protein, ZPR9, by murine protein serine/threonine kinase 38 (MPK38). Biochem.J. 361: 597-604; 2002. (Pubitemid 34177828)
    • (2002) Biochemical Journal , vol.361 , Issue.3 , pp. 597-604
    • Seong, H.-A.1    Gil, M.2    Kim, K.-T.3    Kim, S.-J.4    Ha, H.5
  • 6
    • 77957280982 scopus 로고    scopus 로고
    • Murine protein serine/threonine kinase 38 stimulates TGF-p signaling in a kinase-dependent manner via direct phosphorylation of Smad proteins
    • Seong, H.-A.; Jung, H.; Ha, H. Murine protein serine/threonine kinase 38 stimulates TGF-p signaling in a kinase-dependent manner via direct phosphorylation of Smad proteins. J. Biol. Chem 285: 30959-30970; 2010.
    • (2010) J. Biol. Chem , vol.285 , pp. 30959-30970
    • Seong, H.-A.1    Jung, H.2    Ha, H.3
  • 7
    • 84862270330 scopus 로고    scopus 로고
    • Murine protein serine/threonine kinase 38 activates p53 function through Ser15 phosphorylation
    • Seong, H.-A.; Ha, H. Murine protein serine/threonine kinase 38 activates p53 function through Ser15 phosphorylation. J. Biol. Chem. 287: 20797-20810; 2012.
    • (2012) J. Biol. Chem , vol.287 , pp. 20797-20810
    • Seong, H.-A.1    Ha, H.2
  • 8
    • 0037984272 scopus 로고    scopus 로고
    • Enhancement of B-MYB transcriptional activity by ZPR9, a novel zinc finger protein
    • DOI 10.1074/jbc.M207478200
    • Seong, H.-A.; Kim, K.-T.; Ha, H. Enhancement of B-myb transcriptional activity by ZPR9, a novel zinc finger protein. J. Biol. Chem. 278: 9655-9662; 2003. (Pubitemid 36800462)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9655-9662
    • Seong, H.-A.1    Kim, K.-T.2    Ha, H.3
  • 10
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264: 13963-13966; 1985. (Pubitemid 19214215)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.24 , pp. 13963-13966
    • Holmgren, A.1
  • 11
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • DOI 10.1146/annurev.pharmtox.41.1.261
    • Powis, G.; Montfort, W. R. Properties and biological activities of thioredoxins. Annu. Rev. Pharmacol. Toxicol. 41: 261-295; 2001. (Pubitemid 32385890)
    • (2001) Annual Review of Pharmacology and Toxicology , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 13
    • 0028106431 scopus 로고
    • Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide
    • DOI 10.1016/0165-2478(94)90038-8
    • Nakamura, H.; Matsuda, M.; Furuke, K.; Kitaoka, Y; Iwata, S.; Toda, K.; Inamoto, T.; Yamaoka, Y; Ozawa, K.; Yodoi, J. Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide. Immunol. Lett. 42: 75-80; 1994. (Pubitemid 24305198)
    • (1994) Immunology Letters , vol.42 , Issue.1-2 , pp. 75-80
    • Nakamura, H.1    Matsuda, M.2    Furuke, K.3    Kitaoka, Y.4    Iwata, S.5    Toda, K.6    Inamoto, T.7    Yamaoka, Y.8    Ozawa, K.9    Yodoi, J.10
  • 14
    • 0029976986 scopus 로고    scopus 로고
    • Redox control of resistance to cis-diamminedichloroplatinum(II) (CDDP): Protective effect of human thioredoxin against CDDP-induced cytotoxicity
    • Sasada, T.; Iwata, S.; Sato, N.; Kitaoka, Y; Hirota, K.; Nakamura, K.; Nishiyama, A.; Taniguchi, Y; Takabayashi, A.; Yodoi, J. Redox control of resistance to cis-diamminedichloroplatinum (II) (CDDP): protective effect of human thioredoxin against CDDP-induced cytotoxicity. J. Clin. Invest. 97: 2268-2276; 1996.
    • (1996) J. Clin. Invest , vol.97 , pp. 2268-2276
    • Sasada, T.1    Iwata, S.2    Sato, N.3    Kitaoka, Y.4    Hirota, K.5    Nakamura, K.6    Nishiyama, A.7    Taniguchi, Y.8    Takabayashi, A.9    Yodoi, J.10
  • 16
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund, H.; Gleason, F. K.; Holmgren, A. Structural and functional relations among thioredoxins of different species. Proteins 11: 13-28; 1991.
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 17
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren, A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3: 239-243; 1995.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 18
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis, G.; Mustacich, D.; Coon, A. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic. Biol. Med. 29: 312-322; 2000.
    • (2000) Free Radic. Biol. Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 19
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • DOI 10.1093/emboj/17.9.2596
    • Saitoh, M.; Nishitoh, H.; Fujii, M.; Takeda, K.; Tobiume, K.; Sawada, Y; Kawabata, M.; Miyazono, K.; Ichijo, H. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBOJ. 17: 2596-2606; 1998. (Pubitemid 28221195)
    • (1998) EMBO Journal , vol.17 , Issue.9 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6    Kawabata, M.7    Miyazono, K.8    Ichijo, H.9
  • 20
    • 84870294580 scopus 로고    scopus 로고
    • Thioredoxin-1 functions as a molecular switch regulating the oxidative stress-induced activation of MST1
    • Chae, J. S.; Hwang, S. G.; Lim, D.-S.; Choi, E.-J. Thioredoxin-1 functions as a molecular switch regulating the oxidative stress-induced activation of MST1. Free Radic. Biol. Med. 53: 2335-2343; 2012.
    • (2012) Free Radic. Biol. Med , vol.53 , pp. 2335-2343
    • Chae, J.S.1    Hwang, S.G.2    Lim, D.-S.3    Choi, E.-J.4
  • 22
    • 19444381651 scopus 로고    scopus 로고
    • Direct association of hepatopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-̊B
    • DOI 10.1016/j.cellsig.2004.11.016, PII S0898656804002669
    • Li, Y; Liu, W.; Xing, G.; Tian, C; Zhu, Y; He, F. Direct association of hepatopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-kB. Cell. Signalling 17: 985-996; 2005. (Pubitemid 40723587)
    • (2005) Cellular Signalling , vol.17 , Issue.8 , pp. 985-996
    • Li, Y.1    Liu, W.2    Xing, G.3    Tian, C.4    Zhu, Y.5    He, F.6
  • 23
    • 0033618398 scopus 로고    scopus 로고
    • Identification of thioredoxin-binding protein-2/vitamin D3 up-regulated protein 1 as a negative regulator of thioredoxin function and expression
    • Nishiyama, A.; Matsui, M.; Iwata, S.; Hirota, K.; Masutani, H.; Nakamura, H.; Takagi, Y; Sono, H.; Gon, Y; Yodoi, J. Identification of thioredoxin-binding protein-2/vitamin D3 up-regulated protein 1 as a negative regulator of thioredoxin function and expression. J. Biol. Chem. 274: 21645-21650; 1999.
    • (1999) J. Biol. Chem , vol.274 , pp. 21645-21650
    • Nishiyama, A.1    Matsui, M.2    Iwata, S.3    Hirota, K.4    Masutani, H.5    Nakamura, H.6    Takagi, Y.7    Sono, H.8    Gon, Y.9    Yodoi, J.10
  • 24
    • 10644245123 scopus 로고    scopus 로고
    • Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1
    • DOI 10.1038/sj.onc.1208116
    • Hwang, C. Y.; Ryu, Y. S.; Chung, M.-S.; Kim, K. D.; Park, S. S.; Chae, S.-K.; Chae, H. Z.; Kwon, K.-S. Thioredoxin modulates activator protein 1 activity and p27Kip1 degradation through direct interaction with Jab1. Oncogene 23: 8868-8875; 2004. (Pubitemid 39657777)
    • (2004) Oncogene , vol.23 , Issue.55 , pp. 8868-8875
    • Hwang, C.Y.1    Ryu, Y.S.2    Chung, M.-S.3    Kim, K.D.4    Park, S.S.5    Chae, S.-K.6    Chae, H.Z.7    Kwon, K.-S.8
  • 25
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • DOI 10.1074/jbc.274.5.3182
    • Makino, Y.; Yoshikawa, N.; Okamoto, K.; Hirota, K.; Yodoi, J.; Makino, I.; Tanaka, H. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem. 274: 3182-3188; 1999. (Pubitemid 29075407)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 27
    • 0142137134 scopus 로고    scopus 로고
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN
    • DOI 10.1093/emboj/cdg513
    • Leslie, N. R.; Bennett, D.; Lindsay, Y. E.; Stewart, H.; Gray, A.; Downes, C. P. Redox regulation of PI 3-kinase signalling via inactivation of PTEN. EMBO J. 22: 5501-5510; 2003. (Pubitemid 37279959)
    • (2003) EMBO Journal , vol.22 , Issue.20 , pp. 5501-5510
    • Leslie, N.R.1    Bennett, D.2    Lindsay, Y.E.3    Stewart, H.4    Gray, A.5    Downes, C.P.6
  • 28
    • 34249737498 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-β-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins
    • DOI 10.1074/jbc.M609279200
    • Seong, H.-A.; Jung, H.; Kim, K.-T.; Ha, H. 3-Phosphoinositide-dependent protein kinase-1 (PDK1) negatively regulates TGF-ß-induced signaling in a kinase-dependent manner through physical interaction with SMAD proteins. J. Biol. Chem 282: 12272-12289; 2007. (Pubitemid 47100723)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12272-12289
    • Seong, H.-A.1    Jung, H.2    Kim, K.-T.3    Ha, H.4
  • 29
    • 34249674439 scopus 로고    scopus 로고
    • Nm23-h1 tumor suppressor physically interacts with strap a tgf-ß receptor interacting protein and negatively regulates tgf-ß signaling
    • Seong, H.-A.; Jung, H.; Ha, H. Nm23-H1 tumor suppressor physically interacts with STRAP, a TGF-ß receptor interacting protein, and negatively regulates TGF-ß signaling. J. Biol. Chem 282: 12075-12096; 2007.
    • (2007) J. Biol. Chem , vol.282 , pp. 12075-12096
    • Seong, H.-A.1    Jung, H.2    Ha, H.3
  • 30
    • 67649229153 scopus 로고    scopus 로고
    • Thrombin-induced connective tissue growth factor expression in human lung fibroblasts requires the ASK1/JNK/AP-1 pathway
    • Yu, C.-C.; Hsu, M.-J.; Kuo, M.-L.; Chen, R. F.-C.; Chen, M.-C.; Bai, K.-J.; Yu, M.-C.; Chen, B.-C.; Lin, C.-H. Thrombin-induced connective tissue growth factor expression in human lung fibroblasts requires the ASK1/JNK/AP-1 pathway. J. Immunol. 182: 7916-7927; 2009.
    • (2009) J. Immunol , vol.182 , pp. 7916-7927
    • Yu, C.-C.1    Hsu, M.-J.2    Kuo, M.-L.3    Chen, R.F.-C.4    Chen, M.-C.5    Bai, K.-J.6    Yu, M.-C.7    Chen, B.-C.8    Lin, C.-H.9
  • 32
    • 36849054976 scopus 로고    scopus 로고
    • NM23-H1 tumor suppressor and its interacting partner STRAP activate p53 function
    • DOI 10.1074/jbc.M705181200
    • Jung, H.; Seong, H.-A.; Ha, H. Nm23-H1 tumor suppressor and its interacting partner STRAP activate p53 function. J. Biol. Chem. 282: 35293-35307; 2007. (Pubitemid 350232484)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 35293-35307
    • Jung, H.1    Seong, H.-A.2    Ha, H.3
  • 33
    • 73649126190 scopus 로고    scopus 로고
    • Serine-threonine kinase receptor-associated protein inhibits apoptosis signal-regulating kinase 1 function through direct interaction
    • Jung, H.; Seong, H.-A.; Manoharan, R.; Ha, H. Serine-threonine kinase receptor-associated protein inhibits apoptosis signal-regulating kinase 1 function through direct interaction. J. Biol. Chem. 285: 54-70; 2010.
    • (2010) J. Biol. Chem , vol.285 , pp. 54-70
    • Jung, H.1    Seong, H.-A.2    Manoharan, R.3    Ha, H.4
  • 34
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • DOI 10.1016/S0014-5793(97)01480-4, PII S0014579397014804
    • Honda, R.; Tanaka, H.; Yasuda, H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420: 25-27; 1997. (Pubitemid 28037193)
    • (1997) FEBS Letters , vol.420 , Issue.1 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 35
    • 2042470971 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene
    • DOI 10.1006/dbio.1996.0208
    • Matsui, M.; Oshima, M.; Oshima, H.; Takaku, K.; Maruyama, T.; Yodoi, J.; Taketo, M. M. Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev. Biol. 178: 17 9 -185; 1996. (Pubitemid 26297250)
    • (1996) Developmental Biology , vol.178 , Issue.1 , pp. 179-185
    • Matsui, M.1    Oshima, M.2    Oshima, H.3    Takaku, K.4    Maruyama, T.5    Yodoi, J.6    Taketo, M.M.7
  • 36
    • 22544432226 scopus 로고    scopus 로고
    • Melk-like kinase plays a role in hematopoiesis in the zebra fish
    • DOI 10.1128/MCB.25.15.6682-6693.2005
    • Saito, R.; Tabata, Y.; Muto, A.; Arai, K.; Watanabe, S. Melk-like kinase plays a role in hematopoiesis in the zebra fish. Mol. Cell. Biol. 25: 6682-6693; 2005. (Pubitemid 41023241)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6682-6693
    • Saito, R.1    Tabata, Y.2    Muto, A.3    Arai, K.-I.4    Watanabe, S.5
  • 38
    • 27544457677 scopus 로고    scopus 로고
    • Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers
    • DOI 10.1158/0008-5472.CAN-04-4531
    • Gray, D.; Jubb, A. M.; Hogue, D.; Dowd, P.; Kljavin, N.; Yi, S.; Bai, W.; Frantz, G.; Zhang, Z.; Koeppen, H.; de Sauvage, F. J.; Davis, D. P. Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers. Cancer Res. 65: 9751-9761; 2005. (Pubitemid 41541452)
    • (2005) Cancer Research , vol.65 , Issue.21 , pp. 9751-9761
    • Gray, D.1    Jubb, A.M.2    Hogue, D.3    Dowd, P.4    Kljavin, N.5    Yi, S.6    Bai, W.7    Frantz, G.8    Zhang, Z.9    Koeppen, H.10    De Sauvage, F.J.11    Davis, D.P.12
  • 39
    • 1542275529 scopus 로고    scopus 로고
    • Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase melk and involvement of splicing factor nipp1
    • DOI 10.1074/jbc.M311466200
    • Vulsteke, V.; Beullens, M.; Boudrez, A.; Keppens, S.; Van Eynde, A.; Rider, M. H.; Stalmans, W.; Bollen, M. Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1. J. Biol. Chem. 279: 8642-8647; 2004. (Pubitemid 38295919)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8642-8647
    • Vulsteke, V.1    Beullens, M.2    Boudrez, A.3    Keppens, S.4    Van Eynde, A.5    Rider, M.H.6    Stalmans, W.7    Bollen, M.8
  • 41
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • DOI 10.1161/01.RES.0000022160.64355.62
    • Liu, Y.; Min, W. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ. Res 90: 1259-1266; 2002. (Pubitemid 34787407)
    • (2002) Circulation Research , vol.90 , Issue.12 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 42
    • 77955274921 scopus 로고    scopus 로고
    • Thioredoxin-1 phosphorylated at T100 is needed for its anti-apoptotic activity in HepG2 cancer cells
    • Chen, X.; Tang, W.; Liu, S.; Yu, L.; Chen, Z. Thioredoxin-1 phosphorylated at T100 is needed for its anti-apoptotic activity in HepG2 cancer cells. Life Sci. 87: 254-260; 2010.
    • (2010) Life Sci , vol.87 , pp. 254-260
    • Chen, X.1    Tang, W.2    Liu, S.3    Yu, L.4    Chen, Z.5


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