메뉴 건너뛰기




Volumn 42, Issue 12, 2007, Pages 1797-1806

Molecular mechanism of human Nrf2 activation and degradation: Role of sequential phosphorylation by protein kinase CK2

Author keywords

Arsenic; CK2; Nrf2; Oxidative stress; Phosphorylation

Indexed keywords

CALCIUM; CALMODULIN; CASEIN KINASE II; PROTEIN KINASE INHIBITOR; TRANSCRIPTION FACTOR NRF2;

EID: 34248593492     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.03.001     Document Type: Article
Times cited : (180)

References (41)
  • 1
    • 0037043822 scopus 로고    scopus 로고
    • c-Maf negatively regulates ARE-mediated detoxifying enzyme genes expression and anti-oxidant induction
    • Dhakshinamoorthy S., and Jaiswal A.K. c-Maf negatively regulates ARE-mediated detoxifying enzyme genes expression and anti-oxidant induction. Oncogene 21 (2002) 5301-5312
    • (2002) Oncogene , vol.21 , pp. 5301-5312
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 2
    • 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 26 S 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 26 S 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
  • 3
    • 1942455887 scopus 로고    scopus 로고
    • Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
    • Itoh K., Tong K.I., and Yamamoto M. Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles. Free Radic. Biol. Med. 36 (2004) 1208-1213
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1208-1213
    • Itoh, K.1    Tong, K.I.2    Yamamoto, M.3
  • 4
    • 13044304201 scopus 로고    scopus 로고
    • Nrf2 is essential for protection against acute pulmonary injury in mice
    • Chan K., and Kan Y.W. Nrf2 is essential for protection against acute pulmonary injury in mice. Proc. Natl. Acad. Sci. USA 96 (1999) 12731-12736
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12731-12736
    • Chan, K.1    Kan, Y.W.2
  • 5
    • 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. USA 98 (2001) 3410-5415
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3410-5415
    • 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
  • 6
    • 0035836698 scopus 로고    scopus 로고
    • An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen
    • Chan K., Han X.D., and Kan Y.W. An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen. Proc. Natl. Acad. Sci. USA 98 (2001) 4611-4616
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4611-4616
    • Chan, K.1    Han, X.D.2    Kan, Y.W.3
  • 7
    • 3142570440 scopus 로고    scopus 로고
    • The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress
    • Nguyen T., Yang C.S., and Pickett C.B. The pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress. Free Radic. Biol. Med. 37 (2004) 433-441
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 433-441
    • Nguyen, T.1    Yang, C.S.2    Pickett, C.B.3
  • 8
    • 0142058235 scopus 로고    scopus 로고
    • Transcription factor Nrf2 activation by inorganic arsenic in cultured keratinocytes: involvement of hydrogen peroxide
    • Pi J., Qu W., Reece J.M., Kumagai Y., and Waalkes M.P. Transcription factor Nrf2 activation by inorganic arsenic in cultured keratinocytes: involvement of hydrogen peroxide. Exp. Cell Res. 290 (2003) 234-245
    • (2003) Exp. Cell Res. , vol.290 , pp. 234-245
    • Pi, J.1    Qu, W.2    Reece, J.M.3    Kumagai, Y.4    Waalkes, M.P.5
  • 10
    • 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
  • 11
    • 0242666198 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression
    • Bloom D.A., and Jaiswal A.K. Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression. J. Biol. Chem. 278 (2003) 44675-44682
    • (2003) J. Biol. Chem. , vol.278 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 12
    • 0036436025 scopus 로고    scopus 로고
    • Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction
    • Kang K.W., Choi S.H., and Kim S.G. Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction. Nitric Oxide 7 (2002) 244-253
    • (2002) Nitric Oxide , vol.7 , pp. 244-253
    • Kang, K.W.1    Choi, S.H.2    Kim, S.G.3
  • 13
    • 0034704079 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism
    • Yu R., Chen C., Mo Y.Y., Hebbar V., Owuor E.D., Tan T.H., and Kong A.N. Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism. J. Biol. Chem. 275 (2000) 39907-39913
    • (2000) J. Biol. Chem. , vol.275 , pp. 39907-39913
    • Yu, R.1    Chen, C.2    Mo, Y.Y.3    Hebbar, V.4    Owuor, E.D.5    Tan, T.H.6    Kong, A.N.7
  • 14
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan S.B., and Diehl J.A. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J. Biol. Chem. 279 (2004) 20108-20117
    • (2004) J. Biol. Chem. , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 16
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: a challenge to canons
    • Pinna L.A. Protein kinase CK2: a challenge to canons. J. Cell Sci. 115 (2002) 3873-3878
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 17
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F., and Pinna L.A. One-thousand-and-one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 18
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: an emerging role for protein kinase CK2
    • Ahmed K., Gerber D.A., and Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol. 12 (2002) 226-230
    • (2002) Trends Cell Biol. , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 19
    • 0037716542 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive potent inhibitor of protein kinase CK2 from various sources
    • Zien P., Bretner M., Zastapilo K., Szyszka R., and Shugar D. Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive potent inhibitor of protein kinase CK2 from various sources. Biochem. Biophys. Res. Commun. 306 (2003) 129-133
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 129-133
    • Zien, P.1    Bretner, M.2    Zastapilo, K.3    Szyszka, R.4    Shugar, D.5
  • 21
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • Moi P., Chan K., Asunis I., Cao A., and Kan Y.W. Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc. Natl. Acad. Sci. USA 91 (1994) 9926-9930
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 22
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2')
    • Sarno S., Reddy H., Meggio F., Ruzzene M., Davies S.P., Donella-Deana A., Shugar D., and Pinna L.A. Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2'). FEBS Lett. 496 (2001) 44-48
    • (2001) FEBS Lett. , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3    Ruzzene, M.4    Davies, S.P.5    Donella-Deana, A.6    Shugar, D.7    Pinna, L.A.8
  • 23
    • 16844370286 scopus 로고    scopus 로고
    • Order or chaos? An evaluation of the regulation of protein kinase CK2
    • Olsten M.E., and Litchfield D.W. Order or chaos? An evaluation of the regulation of protein kinase CK2. Biochem. Cell. Biol. 82 (2004) 681-693
    • (2004) Biochem. Cell. Biol. , vol.82 , pp. 681-693
    • Olsten, M.E.1    Litchfield, D.W.2
  • 25
    • 0037024694 scopus 로고    scopus 로고
    • Ca2+-dependent dephosphorylation of kinesin heavy chain on beta-granules in pancreatic beta-cells. Implications for regulated beta-granule transport and insulin exocytosis
    • Donelan M.J., Morfini G., Julyan R., Sommers S., Hays L., Kajio H., Briaud I., Easom R.A., Molkentin J.D., Brady S.T., and Rhodes C.J. Ca2+-dependent dephosphorylation of kinesin heavy chain on beta-granules in pancreatic beta-cells. Implications for regulated beta-granule transport and insulin exocytosis. J. Biol. Chem. 277 (2002) 24232-24242
    • (2002) J. Biol. Chem. , vol.277 , pp. 24232-24242
    • Donelan, M.J.1    Morfini, G.2    Julyan, R.3    Sommers, S.4    Hays, L.5    Kajio, H.6    Briaud, I.7    Easom, R.A.8    Molkentin, J.D.9    Brady, S.T.10    Rhodes, C.J.11
  • 26
    • 0030861055 scopus 로고    scopus 로고
    • Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation
    • Leroy D., Heriche J.K., Filhol O., Chambaz E.M., and Cochet C. Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation. J. Biol. Chem. 272 (1997) 20820-20827
    • (1997) J. Biol. Chem. , vol.272 , pp. 20820-20827
    • Leroy, D.1    Heriche, J.K.2    Filhol, O.3    Chambaz, E.M.4    Cochet, C.5
  • 27
    • 0032839666 scopus 로고    scopus 로고
    • Dual effect of spermine on mast cell secretion exhibits different calcium and temperature requirements
    • Vliagoftis H., Mak L., Boucher W., and Theoharides T.C. Dual effect of spermine on mast cell secretion exhibits different calcium and temperature requirements. Int. J. Immunopharmacol. 21 (1999) 547-559
    • (1999) Int. J. Immunopharmacol. , vol.21 , pp. 547-559
    • Vliagoftis, H.1    Mak, L.2    Boucher, W.3    Theoharides, T.C.4
  • 28
    • 0036367031 scopus 로고    scopus 로고
    • Phosphorylation of calmodulin. Functional implications
    • Benaim G., and Villalobo A. Phosphorylation of calmodulin. Functional implications. Eur. J. Biochem. 269 (2002) 3619-3631
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3619-3631
    • Benaim, G.1    Villalobo, A.2
  • 29
    • 0347064006 scopus 로고    scopus 로고
    • Molecular identification of a calcium-inhibited catalytic subunit of casein kinase type 2 from Paramecium tetraurelia
    • Vetter D., Kissmehl R., Treptau T., Hauser K., Kellermann J., and Plattner H. Molecular identification of a calcium-inhibited catalytic subunit of casein kinase type 2 from Paramecium tetraurelia. Eukaryot. Cell 2 (2003) 1220-1233
    • (2003) Eukaryot. Cell , vol.2 , pp. 1220-1233
    • Vetter, D.1    Kissmehl, R.2    Treptau, T.3    Hauser, K.4    Kellermann, J.5    Plattner, H.6
  • 30
    • 4944249407 scopus 로고    scopus 로고
    • Phosphorylation of calmodulin fragments by protein kinase CK2. Mechanistic aspects and structural consequences
    • Arrigoni G., Marin O., Pagano M.A., Settimo L., Paolin B., Meggio F., and Pinna L.A. Phosphorylation of calmodulin fragments by protein kinase CK2. Mechanistic aspects and structural consequences. Biochemistry 43 (2004) 12788-12798
    • (2004) Biochemistry , vol.43 , pp. 12788-12798
    • Arrigoni, G.1    Marin, O.2    Pagano, M.A.3    Settimo, L.4    Paolin, B.5    Meggio, F.6    Pinna, L.A.7
  • 31
    • 0025883223 scopus 로고
    • Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin
    • Apel E.D., Litchfield D.W., Clark R.H., Krebs E.G., and Storm D.R. Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin. J. Biol. Chem. 266 (1991) 10544-10551
    • (1991) J. Biol. Chem. , vol.266 , pp. 10544-10551
    • Apel, E.D.1    Litchfield, D.W.2    Clark, R.H.3    Krebs, E.G.4    Storm, D.R.5
  • 32
    • 1542409972 scopus 로고    scopus 로고
    • Protein kinase CK2 as regulator of cell survival: implications for cancer therapy
    • Unger G.M., Davis A.T., Slaton J.W., and Ahmed K. Protein kinase CK2 as regulator of cell survival: implications for cancer therapy. Curr. Cancer Drug Targets 4 (2004) 77-84
    • (2004) Curr. Cancer Drug Targets , vol.4 , pp. 77-84
    • Unger, G.M.1    Davis, A.T.2    Slaton, J.W.3    Ahmed, K.4
  • 33
    • 34248588419 scopus 로고    scopus 로고
    • Role of protein kinase CK2 in peturbed Nrf2-mediated oxidative stress response in human keratinocytes during arsenic-induced malignant transformation (abstract)
    • Pi J., Diwan B.A., Qu W., Liu J., Bai Y., Fahl W.F., Yamauchi H., Collins S., and Waalkes M.P. Role of protein kinase CK2 in peturbed Nrf2-mediated oxidative stress response in human keratinocytes during arsenic-induced malignant transformation (abstract). Toxicologist 90 (2006) 58
    • (2006) Toxicologist , vol.90 , pp. 58
    • Pi, J.1    Diwan, B.A.2    Qu, W.3    Liu, J.4    Bai, Y.5    Fahl, W.F.6    Yamauchi, H.7    Collins, S.8    Waalkes, M.P.9
  • 35
    • 0035847102 scopus 로고    scopus 로고
    • The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation
    • Torres J., and Pulido R. The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J. Biol. Chem. 276 (2001) 993-998
    • (2001) J. Biol. Chem. , vol.276 , pp. 993-998
    • Torres, J.1    Pulido, R.2
  • 36
    • 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., Kobayashi A., Wakabayashi N., Kim S.G., and Yamamoto M. 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 (2004) 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
  • 37
    • 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
  • 40
    • 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
  • 41
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D., Killeen E., Naquin R., Alam S., and Alam J. Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J. Biol. Chem. 278 (2003) 2396-2402
    • (2003) J. Biol. Chem. , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.