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Volumn 28, Issue 8, 2008, Pages 2758-2770

Physiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activity

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; OXIDIZING AGENT; TRANSCRIPTION FACTOR NRF2; UBIQUITIN PROTEIN LIGASE E3;

EID: 42149196050     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01704-07     Document Type: Article
Times cited : (441)

References (40)
  • 1
    • 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., J. D. Gordan, J. Jin, J. W. Harper, and J. A. Diehl. 2004. 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. 24:8477-8486.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 2
    • 0025261680 scopus 로고
    • Preparation of extracts from higher eukaryotes
    • Dignam, J. D. 1990. Preparation of extracts from higher eukaryotes. Methods Enzymol. 182:194-203.
    • (1990) Methods Enzymol , vol.182 , pp. 194-203
    • Dignam, J.D.1
  • 3
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova, A. T., W. D. Holtzclaw, R. N. Cole, K. Itoh, N. Wakabayashi, Y. Katoh, M. Yamamoto, and P. Talalay. 2002. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. USA 99:11908-11913.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 4
    • 22544464124 scopus 로고    scopus 로고
    • Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2
    • Eggler, A. L., G. Liu, J. M. Pezzuto, R. B. V. Breemen, and A. D. Mesecar. 2005. Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc. Natl. Acad. Sci. USA 102:10070-10075.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10070-10075
    • Eggler, A.L.1    Liu, G.2    Pezzuto, J.M.3    Breemen, R.B.V.4    Mesecar, A.D.5
  • 5
    • 36349019109 scopus 로고    scopus 로고
    • Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent
    • in press
    • Eggler, A. L., Y. Luo, R. B. Breeman, and A. D. Mesecar. 2007. Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent. Chem. Res. Toxicol. in press.
    • (2007) Chem. Res. Toxicol
    • Eggler, A.L.1    Luo, Y.2    Breeman, R.B.3    Mesecar, A.D.4
  • 6
    • 0025145723 scopus 로고
    • Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element
    • Frilling, R. S., A. Bensimon, Y. Tichauer, and V. Daniel. 1990. Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc. Natl. Acad. Sci. USA 87:6258-6262.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6258-6262
    • Frilling, R.S.1    Bensimon, A.2    Tichauer, Y.3    Daniel, V.4
  • 7
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa, M., and Y. Xiong. 2005. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 25:162-171.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 8
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • Hong, F., K. R. Sekhar, M. L. Freeman, and D. C. Liebler. 2005. Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation. J. Biol. Chem. 280:31768-31775.
    • (2005) J. Biol. Chem , vol.280 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.R.2    Freeman, M.L.3    Liebler, D.C.4
  • 9
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • Hong, F., M. L. Freeman, and D. C. Liebler. 2005. Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane. Chem. Res. Toxicol. 18:1917-1926.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 11
    • 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., N. Wakabayashi, Y. Katoh, T. Ishii, K. Igarashi, J. D. Engel, and M. Yamamoto. 1999. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13:76-86.
    • (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
  • 12
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang, M. I., A. Kobayashi, N. Wakabayashi, S. G. Kim, and M. Yamamoto. 2004. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc. Natl. Acad. Sci. USA 101:2046-2051.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 14
    • 24344479164 scopus 로고    scopus 로고
    • Genetic evidence that small Maf proteins are essential for the activation of antioxidant response element-dependent genes
    • Katsuoka, F., H. Motohashi, T. Ishii, H. Aburatani, J. D. Engel, and M. Yamamoto. 2005. Genetic evidence that small Maf proteins are essential for the activation of antioxidant response element-dependent genes. Mol. Cell. Biol. 25:8044-8051.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8044-8051
    • Katsuoka, F.1    Motohashi, H.2    Ishii, T.3    Aburatani, H.4    Engel, J.D.5    Yamamoto, M.6
  • 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., M. I. Kang, H. Okawa, M. Ohtsuji, Y. Zenke, T. Chiba, K. Igarashi, and M. Yamamoto. 2004. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 24:7130-7139.
    • (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
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi, A., M. I. Kang, Y. Watai, K. I. Tong, T. Shibata, K. Uchida, and M. Yamamoto. 2006. Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol. Cell. Biol. 26:221-229.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3    Tong, K.I.4    Shibata, T.5    Uchida, K.6    Yamamoto, M.7
  • 18
    • 33748052967 scopus 로고    scopus 로고
    • Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species
    • Kobayashi, M., and M. Yamamoto. 2006. Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Adv. Enzyme Regul. 46:113-140.
    • (2006) Adv. Enzyme Regul , vol.46 , pp. 113-140
    • Kobayashi, M.1    Yamamoto, M.2
  • 19
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signaling: Role of cysteine modification in controlling antioxidant defense in response to electrophilic lipid oxidation products
    • Levonen, A. L., A. Landar, A. Ramachandran, E. K. Ceaser, D. A. Dickinson, G. Zanoni, J. D. Morrow, and V. M. Darley-Usmar. 2004. Cellular mechanisms of redox cell signaling: role of cysteine modification in controlling antioxidant defense in response to electrophilic lipid oxidation products. Biochem. J. 378:373-382.
    • (2004) Biochem. J , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 20
    • 33747728194 scopus 로고    scopus 로고
    • Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: A two-site interaction model for the Nrf2-Keap1 complex
    • McMahon, M., N. Thomas, K. Itoh, M. Yamamoto, and J. D. Hayes. 2006. Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J. Biol. Chem. 281:24756-24768.
    • (2006) J. Biol. Chem , vol.281 , pp. 24756-24768
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 21
    • 0024991898 scopus 로고
    • pEF-BOS, a powerful mammalian expression vector
    • Mizushima, S., and S. Nagata. 1990. pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 18:5322.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 22
    • 7244253081 scopus 로고    scopus 로고
    • Nrf2-Keap1 defines a physiologically important stress response mechanism
    • Motohashi, H., and M. Yamamoto. 2004. Nrf2-Keap1 defines a physiologically important stress response mechanism. Trends Mol. Med. 10:549-557.
    • (2004) Trends Mol. Med , vol.10 , pp. 549-557
    • Motohashi, H.1    Yamamoto, M.2
  • 23
    • 2342511435 scopus 로고    scopus 로고
    • Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway
    • Motohashi, H., F. Katsuoka, J. D. Engel, and M. Yamamoto. 2004. Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway. Proc. Natl. Acad. Sci. USA 101:6379-6384.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6379-6384
    • Motohashi, H.1    Katsuoka, F.2    Engel, J.D.3    Yamamoto, M.4
  • 24
    • 28144445947 scopus 로고    scopus 로고
    • Hepatic-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity
    • Okawa, H., H. Motohashi, A. Kobayashi, H. Aburatani, T. W. Kensler, and M. Yamamoto. 2005. Hepatic-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity. Biochem. Biophys. Res. Commun. 339:79-88.
    • (2005) Biochem. Biophys. Res. Commun , vol.339 , pp. 79-88
    • Okawa, H.1    Motohashi, H.2    Kobayashi, A.3    Aburatani, H.4    Kensler, T.W.5    Yamamoto, M.6
  • 26
    • 0025948113 scopus 로고
    • Transcriptional regulation of the rat NAD(P)H:quinone reductase gene
    • Rushmore, T. H., M. R. Morton, and C. B. Pickett. 1991. Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. J. Biol. Chem. 266:11632-11639.
    • (1991) J. Biol. Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 29
    • 0035903475 scopus 로고    scopus 로고
    • In vivo requirements for GATA-1 functional domains during primitive and definitive erythropoiesis
    • Shimizu, R., S. Takahashi, K. Ohneda, J. D. Engel, and M. Yamamoto. 2001. In vivo requirements for GATA-1 functional domains during primitive and definitive erythropoiesis. EMBO J. 20:5250-5260.
    • (2001) EMBO J , vol.20 , pp. 5250-5260
    • Shimizu, R.1    Takahashi, S.2    Ohneda, K.3    Engel, J.D.4    Yamamoto, M.5
  • 31
    • 0028225421 scopus 로고
    • Immortalization of BALB/c mouse embryo fibroblasts alters SV40 large T-antigen interactions with the tumor suppressor p53 and results in a reduced SV40 transformation-efficiency
    • Tiemann, F., and W. Deppert. 1994. Immortalization of BALB/c mouse embryo fibroblasts alters SV40 large T-antigen interactions with the tumor suppressor p53 and results in a reduced SV40 transformation-efficiency. Oncogene 9:1907-1915.
    • (1994) Oncogene , vol.9 , pp. 1907-1915
    • Tiemann, F.1    Deppert, W.2
  • 32
    • 33344463325 scopus 로고    scopus 로고
    • Keap1 recruits Neh2 through binding to ETGE and DLG motifs: Characterization of the two-site molecular recognition model
    • Tong, K. I., Y. Katoh, H. Kusunoki, K. Itoh, T. Tanaka, and M. Yamamoto. 2006. Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. Mol. Cell. Biol. 26:2887-2900.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2887-2900
    • Tong, K.I.1    Katoh, Y.2    Kusunoki, H.3    Itoh, K.4    Tanaka, T.5    Yamamoto, M.6
  • 33
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
    • Tong, K. I., A. Kobayashi, F. Katsuoka, and M. Yamamoto. 2006. Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol. Chem. 387:1311-1320.
    • (2006) Biol. Chem , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 34
    • 35648970026 scopus 로고    scopus 로고
    • Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response
    • Tong, K. I., B. Padmanabhan, A. Kobayashi, C. Shang, Y. Hirotsu, S. Yokoyama, and M. Yamamoto. 2007. Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Mol. Cell. Biol. 27:7511-7521.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 7511-7521
    • Tong, K.I.1    Padmanabhan, B.2    Kobayashi, A.3    Shang, C.4    Hirotsu, Y.5    Yokoyama, S.6    Yamamoto, M.7
  • 38
    • 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 M. Hannink. 2003. 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. 23:8137-8151.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 39
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang, D. D., S. C. Lo, J. V. Cross, D. J. Templeton, and M. Hannink. 2004. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol. Cell. Biol. 24:10941-10953.
    • (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
  • 40
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • Zipper, L. M., and R. T. Mulcahy. 2002. The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm. J. Biol. Chem. 277:36544-36552.
    • (2002) J. Biol. Chem , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, R.T.2


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