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Volumn 47, Issue 1, 2012, Pages 76-86

A Mutually Inhibitory Feedback Loop between the 20S Proteasome and Its Regulator, NQO1

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; NADPH QUINONE OXIDOREDUCTASE 1; PROTEASOME; PROTEASOME 20S; UNCLASSIFIED DRUG;

EID: 84863816082     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.05.049     Document Type: Article
Times cited : (92)

References (44)
  • 1
    • 77955286666 scopus 로고    scopus 로고
    • C-Fos proteasomal degradation is activated by a default mechanism, and its regulation by NAD(P)H:quinone oxidoreductase 1 determines c-Fos serum response kinetics
    • Adler J., Reuven N., Kahana C., Shaul Y. c-Fos proteasomal degradation is activated by a default mechanism, and its regulation by NAD(P)H:quinone oxidoreductase 1 determines c-Fos serum response kinetics. Mol. Cell. Biol. 2010, 30:3767-3778.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3767-3778
    • Adler, J.1    Reuven, N.2    Kahana, C.3    Shaul, Y.4
  • 2
    • 75749106648 scopus 로고    scopus 로고
    • NAD(P)H quinone-oxydoreductase 1 protects eukaryotic translation initiation factor 4GI from degradation by the proteasome
    • Alard A., Fabre B., Anesia R., Marboeuf C., Pierre P., Susini C., Bousquet C., Pyronnet S. NAD(P)H quinone-oxydoreductase 1 protects eukaryotic translation initiation factor 4GI from degradation by the proteasome. Mol. Cell. Biol. 2010, 30:1097-1105.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1097-1105
    • Alard, A.1    Fabre, B.2    Anesia, R.3    Marboeuf, C.4    Pierre, P.5    Susini, C.6    Bousquet, C.7    Pyronnet, S.8
  • 3
    • 0013080216 scopus 로고    scopus 로고
    • Interaction of human NAD(P)H:quinone oxidoreductase 1 (NQO1) with the tumor suppressor protein p53 in cells and cell-free systems
    • Anwar A., Dehn D., Siegel D., Kepa J.K., Tang L.J., Pietenpol J.A., Ross D. Interaction of human NAD(P)H:quinone oxidoreductase 1 (NQO1) with the tumor suppressor protein p53 in cells and cell-free systems. J. Biol. Chem. 2003, 278:10368-10373.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10368-10373
    • Anwar, A.1    Dehn, D.2    Siegel, D.3    Kepa, J.K.4    Tang, L.J.5    Pietenpol, J.A.6    Ross, D.7
  • 4
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • Asher G., Tsvetkov P., Kahana C., Shaul Y. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev. 2005, 19:316-321.
    • (2005) Genes Dev. , vol.19 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 5
    • 33646857902 scopus 로고    scopus 로고
    • The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol
    • Asher G., Dym O., Tsvetkov P., Adler J., Shaul Y. The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry 2006, 45:6372-6378.
    • (2006) Biochemistry , vol.45 , pp. 6372-6378
    • Asher, G.1    Dym, O.2    Tsvetkov, P.3    Adler, J.4    Shaul, Y.5
  • 6
    • 59649115172 scopus 로고    scopus 로고
    • Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination
    • Baugh J.M., Viktorova E.G., Pilipenko E.V. Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J. Mol. Biol. 2009, 386:814-827.
    • (2009) J. Mol. Biol. , vol.386 , pp. 814-827
    • Baugh, J.M.1    Viktorova, E.G.2    Pilipenko, E.V.3
  • 7
    • 0019142866 scopus 로고
    • Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity
    • Benson A.M., Hunkeler M.J., Talalay P. Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity. Proc. Natl. Acad. Sci. USA 1980, 77:5216-5220.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5216-5220
    • Benson, A.M.1    Hunkeler, M.J.2    Talalay, P.3
  • 8
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom J., Amador V., Bartolini F., DeMartino G., Pagano M. Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 2003, 115:71-82.
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 9
    • 0033805383 scopus 로고    scopus 로고
    • Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2)
    • Chen S., Wu K., Knox R. Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2). Free Radic. Biol. Med. 2000, 29:276-284.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 276-284
    • Chen, S.1    Wu, K.2    Knox, R.3
  • 10
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chernushevich I.V., Thomson B.A. Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 2004, 76:1754-1760.
    • (2004) Anal. Chem. , vol.76 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 11
    • 0001075830 scopus 로고
    • Induction of NAD(P)H:quinone reductase in murine hepatoma cells by phenolic antioxidants, azo dyes, and other chemoprotectors: a model system for the study of anticarcinogens
    • De Long M.J., Prochaska H.J., Talalay P. Induction of NAD(P)H:quinone reductase in murine hepatoma cells by phenolic antioxidants, azo dyes, and other chemoprotectors: a model system for the study of anticarcinogens. Proc. Natl. Acad. Sci. USA 1986, 83:787-791.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 787-791
    • De Long, M.J.1    Prochaska, H.J.2    Talalay, P.3
  • 12
    • 37449024702 scopus 로고    scopus 로고
    • The biology of cancer: metabolic reprogramming fuels cell growth and proliferation
    • DeBerardinis R.J., Lum J.J., Hatzivassiliou G., Thompson C.B. The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metab. 2008, 7:11-20.
    • (2008) Cell Metab. , vol.7 , pp. 11-20
    • DeBerardinis, R.J.1    Lum, J.J.2    Hatzivassiliou, G.3    Thompson, C.B.4
  • 13
    • 77956171147 scopus 로고    scopus 로고
    • NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector
    • Dinkova-Kostova A.T., Talalay P. NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector. Arch. Biochem. Biophys. 2010, 501:116-123.
    • (2010) Arch. Biochem. Biophys. , vol.501 , pp. 116-123
    • Dinkova-Kostova, A.T.1    Talalay, P.2
  • 14
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6:197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 15
    • 0000964637 scopus 로고
    • Soluble diaphorase in animal tissues
    • Ernster L., Navazioi F. Soluble diaphorase in animal tissues. Acta Chem. Scand. 1958, 12:595.
    • (1958) Acta Chem. Scand. , vol.12 , pp. 595
    • Ernster, L.1    Navazioi, F.2
  • 17
    • 44649168869 scopus 로고    scopus 로고
    • NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of the tumour suppressor p33(ING1b)
    • Garate M., Wong R.P., Campos E.I., Wang Y., Li G. NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of the tumour suppressor p33(ING1b). EMBO Rep. 2008, 9:576-581.
    • (2008) EMBO Rep. , vol.9 , pp. 576-581
    • Garate, M.1    Wong, R.P.2    Campos, E.I.3    Wang, Y.4    Li, G.5
  • 18
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 1998, 94:615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 19
    • 0016017019 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells
    • Goldberg A.L., Dice J.F. Intracellular protein degradation in mammalian and bacterial cells. Annu. Rev. Biochem. 1974, 43:835-869.
    • (1974) Annu. Rev. Biochem. , vol.43 , pp. 835-869
    • Goldberg, A.L.1    Dice, J.F.2
  • 20
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer J., Futschik M.E., Teichmann S.A., Babu M.M. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 2008, 322:1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 21
    • 0442276567 scopus 로고    scopus 로고
    • Under non-denaturing solvent conditions, the mean charge state of a multiply charged protein ion formed by electrospray is linearly correlated with the macromolecular surface
    • Hautreux M., Hue N., de Kerdaniel A.D., Zahir A., Malec V., Laprévote O. Under non-denaturing solvent conditions, the mean charge state of a multiply charged protein ion formed by electrospray is linearly correlated with the macromolecular surface. Int. J. Mass Spectrom. 2004, 231:131-137.
    • (2004) Int. J. Mass Spectrom. , vol.231 , pp. 131-137
    • Hautreux, M.1    Hue, N.2    de Kerdaniel, A.D.3    Zahir, A.4    Malec, V.5    Laprévote, O.6
  • 23
    • 77955321215 scopus 로고    scopus 로고
    • NAD(P)H quinone oxidoreductase protects TAp63gamma from proteasomal degradation and regulates TAp63gamma-dependent growth arrest
    • Hershkovitz Rokah O., Shpilberg O., Granot G. NAD(P)H quinone oxidoreductase protects TAp63gamma from proteasomal degradation and regulates TAp63gamma-dependent growth arrest. PLoS ONE 2010, 5:e11401.
    • (2010) PLoS ONE , vol.5
    • Hershkovitz Rokah, O.1    Shpilberg, O.2    Granot, G.3
  • 24
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: an intriguing mode of multitasking
    • Huberts D.H., van der Klei I.J. Moonlighting proteins: an intriguing mode of multitasking. Biochim Biophys Acta 2010, 1803:520-525.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.1    van der Klei, I.J.2
  • 25
    • 0033025596 scopus 로고    scopus 로고
    • Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma by capillary electrophoresis and laser-induced fluorescence detection
    • Hustad S., Ueland P.M., Schneede J. Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma by capillary electrophoresis and laser-induced fluorescence detection. Clin. Chem. 1999, 45:862-868.
    • (1999) Clin. Chem. , vol.45 , pp. 862-868
    • Hustad, S.1    Ueland, P.M.2    Schneede, J.3
  • 26
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of proteins by the proteasome
    • Jariel-Encontre I., Bossis G., Piechaczyk M. Ubiquitin-independent degradation of proteins by the proteasome. Biochim. Biophys. Acta 2008, 1786:153-177.
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 27
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins-an update
    • Jeffery C.J. Moonlighting proteins-an update. Mol Biosyst 2009, 5:345-350.
    • (2009) Mol Biosyst , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 28
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface areas in solution by electrospray ionization mass spectrometry
    • Kaltashov I.A., Mohimen A. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 2005, 77:5370-5379.
    • (2005) Anal. Chem. , vol.77 , pp. 5370-5379
    • Kaltashov, I.A.1    Mohimen, A.2
  • 29
    • 0021943383 scopus 로고
    • Thyroid hormone regulation of flavocoenzyme biosynthesis
    • Lee S.S., McCormick D.B. Thyroid hormone regulation of flavocoenzyme biosynthesis. Arch. Biochem. Biophys. 1985, 237:197-201.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 197-201
    • Lee, S.S.1    McCormick, D.B.2
  • 30
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction
    • Li R., Bianchet M.A., Talalay P., Amzel L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. USA 1995, 92:8846-8850.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 31
    • 33645083492 scopus 로고    scopus 로고
    • Riboflavin deficiency causes protein and DNA damage in HepG2 cells, triggering arrest in G1 phase of the cell cycle
    • Manthey K.C., Rodriguez-Melendez R., Hoi J.T., Zempleni J. Riboflavin deficiency causes protein and DNA damage in HepG2 cells, triggering arrest in G1 phase of the cell cycle. J. Nutr. Biochem. 2006, 17:250-256.
    • (2006) J. Nutr. Biochem. , vol.17 , pp. 250-256
    • Manthey, K.C.1    Rodriguez-Melendez, R.2    Hoi, J.T.3    Zempleni, J.4
  • 33
    • 80055109876 scopus 로고    scopus 로고
    • T-wave ion mobility-mass spectrometry: basic experimental procedures for protein complex analysis
    • Michaelevski I., Kirshenbaum N., Sharon M. T-wave ion mobility-mass spectrometry: basic experimental procedures for protein complex analysis. J. Vis. Exp. 2010, (41).
    • (2010) J. Vis. Exp. , Issue.41
    • Michaelevski, I.1    Kirshenbaum, N.2    Sharon, M.3
  • 34
    • 0026783268 scopus 로고
    • FAD-dependent regulation of transcription, translation, post-translational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron transfer flavoprotein and the site of holoenzyme formation
    • Nagao M., Tanaka K. FAD-dependent regulation of transcription, translation, post-translational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron transfer flavoprotein and the site of holoenzyme formation. J. Biol. Chem. 1992, 267:17925-17932.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17925-17932
    • Nagao, M.1    Tanaka, K.2
  • 35
    • 1242319559 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 (NQO1, DT-diaphorase), functions and pharmacogenetics
    • Ross D., Siegel D. NAD(P)H:quinone oxidoreductase 1 (NQO1, DT-diaphorase), functions and pharmacogenetics. Methods Enzymol. 2004, 382:115-144.
    • (2004) Methods Enzymol. , vol.382 , pp. 115-144
    • Ross, D.1    Siegel, D.2
  • 36
    • 0028919340 scopus 로고
    • Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria
    • Saijo T., Tanaka K. Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. J. Biol. Chem. 1995, 270:1899-1907.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1899-1907
    • Saijo, T.1    Tanaka, K.2
  • 37
    • 33646910002 scopus 로고    scopus 로고
    • 20S proteasomes have the potential to keep substrates in store for continual degradation
    • Sharon M., Witt S., Felderer K., Rockel B., Baumeister W., Robinson C.V. 20S proteasomes have the potential to keep substrates in store for continual degradation. J. Biol. Chem. 2006, 281:9569-9575.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9569-9575
    • Sharon, M.1    Witt, S.2    Felderer, K.3    Rockel, B.4    Baumeister, W.5    Robinson, C.V.6
  • 38
    • 0035135690 scopus 로고    scopus 로고
    • Rapid polyubiquitination and proteasomal degradation of a mutant form of NAD(P)H:quinone oxidoreductase 1
    • Siegel D., Anwar A., Winski S.L., Kepa J.K., Zolman K.L., Ross D. Rapid polyubiquitination and proteasomal degradation of a mutant form of NAD(P)H:quinone oxidoreductase 1. Mol. Pharmacol. 2001, 59:263-268.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 263-268
    • Siegel, D.1    Anwar, A.2    Winski, S.L.3    Kepa, J.K.4    Zolman, K.L.5    Ross, D.6
  • 40
    • 70350308428 scopus 로고    scopus 로고
    • Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response
    • Tsvetkov P., Reuven N., Prives C., Shaul Y. Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response. J. Biol. Chem. 2009, 284:26234-26242.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26234-26242
    • Tsvetkov, P.1    Reuven, N.2    Prives, C.3    Shaul, Y.4
  • 41
    • 79953181610 scopus 로고    scopus 로고
    • E3 ligase STUB1/CHIP regulates NAD(P)H:quinone oxidoreductase 1 (NQO1) accumulation in aged brain, a process impaired in certain Alzheimer disease patients
    • Tsvetkov P., Adamovich Y., Elliott E., Shaul Y. E3 ligase STUB1/CHIP regulates NAD(P)H:quinone oxidoreductase 1 (NQO1) accumulation in aged brain, a process impaired in certain Alzheimer disease patients. J. Biol. Chem. 2011, 286:8839-8845.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8839-8845
    • Tsvetkov, P.1    Adamovich, Y.2    Elliott, E.3    Shaul, Y.4
  • 42
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu B.P., Weissman J.S. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 2002, 10:983-994.
    • (2002) Mol. Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 43
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden M.G., Cantley L.C., Thompson C.B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 2009, 324:1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 44
    • 53449091477 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel human and rat riboflavin transporter, RFT1
    • Yonezawa A., Masuda S., Katsura T., Inui K. Identification and functional characterization of a novel human and rat riboflavin transporter, RFT1. Am. J. Physiol. Cell Physiol. 2008, 295:C632-C641.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Yonezawa, A.1    Masuda, S.2    Katsura, T.3    Inui, K.4


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