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Volumn 362, Issue 4, 2007, Pages 816-821

A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity

Author keywords

Antioxidant response element; Cullin 3; Keapl; Nrf2; Oxidative stress; Phase II drug metabolism; Redox active chemicals; Ubiquitylation

Indexed keywords

CULLIN; CULLIN 3; PROTEIN KEAP1; TRANSCRIPTION FACTOR NRF2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 34548577395     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.08.051     Document Type: Article
Times cited : (195)

References (34)
  • 1
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element Degradation of Nrf2 by the 26S proteasome
    • Nguyen T., Sherratt P.J., Huang H.-C., Yang C.S., and Pickett C.B. Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element Degradation of Nrf2 by the 26S proteasome. J. Biol. Chem. 278 (2003) 4536-4541
    • (2003) J. Biol. Chem. , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.-C.3    Yang, C.S.4    Pickett, C.B.5
  • 2
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon M., Itoh K., Yamamoto M., and Hayes J.D. Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 278 (2003) 21592-21600
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 3
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J., Stewart D., Touchard C., Boinapally S., Choi A.M., and Cook J.L. Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J. Biol. Chem. 274 (1999) 26071-26078
    • (1999) J. Biol. Chem. , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 5
    • 0035870298 scopus 로고    scopus 로고
    • The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes
    • McMahon M., Itoh K., Yamamoto M., Chanas S.A., Henderson C.J., McLellan L.I., Wolf C.R., Cavin C., and Hayes J.D. The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes. Cancer Res. 61 (2001) 3299-3307
    • (2001) Cancer Res. , vol.61 , pp. 3299-3307
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Chanas, S.A.4    Henderson, C.J.5    McLellan, L.I.6    Wolf, C.R.7    Cavin, C.8    Hayes, J.D.9
  • 6
    • 0042330074 scopus 로고    scopus 로고
    • Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence
    • Nioi P., McMahon M., Itoh K., Yamamoto M., and Hayes J.D. Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence. Biochem. J. 374 (2003) 337-348
    • (2003) Biochem. J. , vol.374 , pp. 337-348
    • Nioi, P.1    McMahon, M.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 7
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene
    • Venugopal R., and Jaiswal A.K. Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene. Proc. Natl. Acad. Sci. USA 93 (1996) 14960-14965
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 8
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of gamma-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • Wild A.C., Moinova H.R., and Mulcahy R.T. Regulation of gamma-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2. J. Biol. Chem. 274 (1999) 33627-33636
    • (1999) J. Biol. Chem. , vol.274 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 10
    • 0035153227 scopus 로고    scopus 로고
    • High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes
    • Enomoto A., Itoh K., Nagayoshi E., Haruta J., Kimura T., O'Conner T., Harada T., and Yamamoto M. High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes. Toxicol. Sci. 59 (2001) 169-177
    • (2001) Toxicol. Sci. , vol.59 , pp. 169-177
    • Enomoto, A.1    Itoh, K.2    Nagayoshi, E.3    Haruta, J.4    Kimura, T.5    O'Conner, T.6    Harada, T.7    Yamamoto, M.8
  • 11
    • 3042716482 scopus 로고    scopus 로고
    • Targeted disruption of Nrf2 causes regenerative immune-mediated hemolytic anemia
    • Lee J.M., Chan K., Kan Y.W., and Johnson J.A. Targeted disruption of Nrf2 causes regenerative immune-mediated hemolytic anemia. Proc. Natl. Acad. Sci. USA 101 (2004) 9751-9756
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9751-9756
    • Lee, J.M.1    Chan, K.2    Kan, Y.W.3    Johnson, J.A.4
  • 12
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • Ramos-Gomez M., Kwak M.K., Dolan P.M., Itoh K., Yamamoto M., Talalay P., and Kensler T.W. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc. Natl. Acad. Sci. 98 (2001) 3410-3415
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6    Kensler, T.W.7
  • 13
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan S.B., Gordon J.D., Jin J., Harper J.W., and Diehl J.A. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol. Cell. Biol. 24 (2004) 8477-8486
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordon, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 14
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitylation by the Cullin 3-Roc1 ligase
    • Furukawa M., and Xiong Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitylation by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 25 (2005) 162-171
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 15
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T., Igarashi K., and Yamamoto M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 24 (2004) 7130-7139
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 16
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., and Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13 (1999) 76-86
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 17
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang D.D., Lo S.C., Cross J.V., Templeton D.J., and Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol. Cell. Biol. 24 (2004) 10941-10953
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 18
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • Huang H.C., Nguyen T., and Pickett C.B. Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. J. Biol. Chem. 277 (2002) 42769-42774
    • (2002) J. Biol. Chem. , vol.277 , pp. 42769-42774
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 20
    • 25444449520 scopus 로고    scopus 로고
    • NRF2 controls constitutive and inducible expression of are-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by keap1
    • Nguyen T., Sherratt P.J., Nioi P., Yang C.S., and Pickett C.B. NRF2 controls constitutive and inducible expression of are-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by keap1. J. Biol. Chem. 280 (2005) 32485-32492
    • (2005) J. Biol. Chem. , vol.280 , pp. 32485-32492
    • Nguyen, T.1    Sherratt, P.J.2    Nioi, P.3    Yang, C.S.4    Pickett, C.B.5
  • 21
    • 23344452360 scopus 로고    scopus 로고
    • Nrf2 Possesses a redox-insensitive nuclear export signal overlapping with the leucine zipper motif
    • Li W., Jain M.R., Chen C., Yue X., Hebbar V., Zhou R., and Kong A.N. Nrf2 Possesses a redox-insensitive nuclear export signal overlapping with the leucine zipper motif. J. Biol. Chem. 280 (2005) 28430-28438
    • (2005) J. Biol. Chem. , vol.280 , pp. 28430-28438
    • Li, W.1    Jain, M.R.2    Chen, C.3    Yue, X.4    Hebbar, V.5    Zhou, R.6    Kong, A.N.7
  • 22
    • 18944373186 scopus 로고    scopus 로고
    • Keap1 regulates the oxidation-sensitive shuttling of Nrf2 into and out of the nucleus via a Crm1-dependent nuclear export mechanism
    • Velichkova M., and Hasson T. Keap1 regulates the oxidation-sensitive shuttling of Nrf2 into and out of the nucleus via a Crm1-dependent nuclear export mechanism. Mol. Cell. Biol. 25 (2005) 4501-4513
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4501-4513
    • Velichkova, M.1    Hasson, T.2
  • 25
    • 28544450507 scopus 로고    scopus 로고
    • The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation
    • Nioi P., Nguyen T., Sherratt P.J., and Pickett C.B. The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation. Mol. Cell. Biol. 25 (2005) 10895-10906
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10895-10906
    • Nioi, P.1    Nguyen, T.2    Sherratt, P.J.3    Pickett, C.B.4
  • 26
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore T.H., Morton M.R., and Pickett C.B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem. 266 (1991) 11632-11639
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 28
    • 33749260565 scopus 로고    scopus 로고
    • Activation of ubiquitin ligase SCF(Skp2) by Cks1: insights from hydrogen exchange mass spectrometry
    • Yao Z.P., Zhou M., Kelly S.E., Seeliger M.A., Robinson C.V., and Itzhaki L.S. Activation of ubiquitin ligase SCF(Skp2) by Cks1: insights from hydrogen exchange mass spectrometry. J. Mol. Biol. 363 (2006) 673-686
    • (2006) J. Mol. Biol. , vol.363 , pp. 673-686
    • Yao, Z.P.1    Zhou, M.2    Kelly, S.E.3    Seeliger, M.A.4    Robinson, C.V.5    Itzhaki, L.S.6
  • 29
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang D.D., and Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23 (2003) 8137-8151
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 30
    • 0025309794 scopus 로고
    • Free radicals and anticancer drug resistance: oxygen free radicals in the mechanisms of drug cytotoxicity and resistance by certain tumors
    • Sinha B.K., and Mimnaugh E.G. Free radicals and anticancer drug resistance: oxygen free radicals in the mechanisms of drug cytotoxicity and resistance by certain tumors. Free Radic. Biol. Med. 8 (1990) 567-581
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 567-581
    • Sinha, B.K.1    Mimnaugh, E.G.2
  • 31
    • 0031930390 scopus 로고    scopus 로고
    • Endogenous antioxidant enzymes and glutathione S-transferase in protection of mesothelioma cells against hydrogen peroxide and epirubicin toxicity
    • Kinnula K., Linnainmaa K., Raivio K.O., and Kinnula V.L. Endogenous antioxidant enzymes and glutathione S-transferase in protection of mesothelioma cells against hydrogen peroxide and epirubicin toxicity. Br. J. Cancer 77 (1998) 1097-1102
    • (1998) Br. J. Cancer , vol.77 , pp. 1097-1102
    • Kinnula, K.1    Linnainmaa, K.2    Raivio, K.O.3    Kinnula, V.L.4
  • 32
    • 0036281367 scopus 로고    scopus 로고
    • Exogenous cysteine and cystine promote cell proliferation in CaCo-2 cells
    • Noda T., Iwakiri R., Fujimoto K., Rhoads C.A., and Aw T.Y. Exogenous cysteine and cystine promote cell proliferation in CaCo-2 cells. Cell Prolif. 35 (2002) 117-129
    • (2002) Cell Prolif. , vol.35 , pp. 117-129
    • Noda, T.1    Iwakiri, R.2    Fujimoto, K.3    Rhoads, C.A.4    Aw, T.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.