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Volumn 287, Issue 15, 2012, Pages 11649-11655

NADPH inhibits [2Fe-2S] cluster protein transfer from diabetes drug target MitoNEET to an Apo-acceptor protein

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR FUNCTION; CLUSTER TRANSFER; CYTOSOLIC; DRUG TARGETS; ELECTRON TRANSFER; INHIBITION CONSTANTS; OXIDATIVE DAMAGE; PHYSIOLOGICAL CONDITION; PROTEIN TRANSFER; THIAZOLIDINEDIONES;

EID: 84859489753     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.319731     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • DOI 10.1146/annurev.biochem.74.082803.133518
    • Johnson, D. C., Dean, D. R., Smith, A. D., and Johnson, M. K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74, 247-281 (Pubitemid 40995508)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 2
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R., and Mühlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77, 669-700
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 3
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill, R. (2009) Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 4
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T. A., and Tong, W. H. (2008) Iron-sulfur cluster biogenesis and human disease. Trends Genet. 24, 398-407
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 6
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • DOI 10.1182/blood-2004-10-3856
    • Napier, I., Ponka, P., and Richardson, D. R. (2005) Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood 105, 1867-1874 (Pubitemid 40731766)
    • (2005) Blood , vol.105 , Issue.5 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 7
    • 34548013116 scopus 로고    scopus 로고
    • The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload
    • DOI 10.1182/blood-2007-02-072520
    • Camaschella, C., Campanella, A., De Falco, L., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., and Iolascon, A. (2007) The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood 110, 1353-1358 (Pubitemid 47281436)
    • (2007) Blood , vol.110 , Issue.4 , pp. 1353-1358
    • Camaschella, C.1    Campanella, A.2    De Falco, L.3    Boschetto, L.4    Merlini, R.5    Silvestri, L.6    Levi, S.7    Iolascon, A.8
  • 8
    • 38949197818 scopus 로고    scopus 로고
    • Redistribution of accumulated cell iron: A modality of chelation with therapeutic implications
    • DOI 10.1182/blood-2007-07-102335
    • Sohn, Y. S., Breuer, W., Munnich, A., and Cabantchik, Z. I. (2008) Redistribution of accumulated cell iron: a modality of chelation with therapeutic implications. Blood 111, 1690-1699 (Pubitemid 351213461)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1690-1699
    • Sohn, Y.-S.1    Breuer, W.2    Munnich, A.3    Cabantchik, Z.I.4
  • 9
    • 43749114744 scopus 로고    scopus 로고
    • Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
    • Hausmann, A., Samans, B., Lill, R., andMühlenhoff, U. (2008) Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis. J. Biol. Chem. 283, 8318-8330
    • (2008) J. Biol. Chem. , vol.283 , pp. 8318-8330
    • Hausmann, A.1    Samans, B.2    Lill, R.A.3    Mühlenhoff, U.4
  • 10
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • DOI 10.1016/S0092-8674(04)00343-5, PII S0092867404003435
    • Hentze, M. W., Muckenthaler, M. U., and Andrews, N. C. (2004) Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285-297 (Pubitemid 38534536)
    • (2004) Cell , vol.117 , Issue.3 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 11
    • 0042477560 scopus 로고    scopus 로고
    • AIF: A multifunctional cog in the life and death machine
    • Hansen, T. M., and Nagley, P. (2003) AIF: a multifunctional cog in the life and death machine. Sci. STKE 2003, PE31
    • (2003) Sci. STKE , vol.2003
    • Hansen, T.M.1    Nagley, P.2
  • 13
    • 52649149879 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, insulin resistance, and type 2 diabetes mellitus
    • Abdul-Ghani, M. A., and DeFronzo, R. A. (2008) Mitochondrial dysfunction, insulin resistance, and type 2 diabetes mellitus. Curr. Diab. Rep. 8, 173-178
    • (2008) Curr. Diab. Rep. , vol.8 , pp. 173-178
    • Abdul-Ghani, M.A.1    DeFronzo, R.A.2
  • 14
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • DOI 10.1126/science.1104343
    • Lowell, B. B., and Shulman, G. I. (2005) Mitochondrial dysfunction and type 2 diabetes. Science 307, 384-387 (Pubitemid 40139974)
    • (2005) Science , vol.307 , Issue.5708 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2
  • 17
    • 33644754001 scopus 로고    scopus 로고
    • What has prevented the expansion of insulin sensitisers?
    • DOI 10.1517/13543784.15.3.205
    • Colca, J. R., and Kletzien, R. F. (2006) What has prevented the expansion of insulin sensitisers? Expert Opin. Investig. Drugs 15, 205-210 (Pubitemid 43338142)
    • (2006) Expert Opinion on Investigational Drugs , vol.15 , Issue.3 , pp. 205-210
    • Colca, J.R.1    Kletzien, R.F.2
  • 18
    • 0026664271 scopus 로고
    • New oral thiazolidinedione antidiabetic agents act as insulin sensitizers
    • Hofmann, C. A., and Colca, J. R. (1992) New oral thiazolidinedione antidiabetic agents act as insulin sensitizers. Diabetes Care 8, 1075-1078
    • (1992) Diabetes Care , vol.8 , pp. 1075-1078
    • Hofmann, C.A.1    Colca, J.R.2
  • 19
    • 33847711060 scopus 로고    scopus 로고
    • The power to reduce: Pyridine nucleotides - Small molecules with a multitude of functions
    • DOI 10.1042/BJ20061638
    • Pollak, N., Dölle, C., and Ziegler, M. (2007) The power to reduce: pyridine nucleotides-small molecules with a multitude of functions. Biochem. J. 402, 205-218 (Pubitemid 46383418)
    • (2007) Biochemical Journal , vol.402 , Issue.2 , pp. 205-218
    • Pollak, N.1    Dolle, C.2    Ziegler, M.3
  • 24
    • 70350507369 scopus 로고    scopus 로고
    • Redox characterization of the FeS protein MitoNEET and impact of thiazolidinedione drug binding
    • Bak, D. W., Zuris, J. A., Paddock, M. L., Jennings, P. A., and Elliott, S. J. (2009) Redox characterization of the FeS protein MitoNEET and impact of thiazolidinedione drug binding. Biochemistry 48, 10193-10195
    • (2009) Biochemistry , vol.48 , pp. 10193-10195
    • Bak, D.W.1    Zuris, J.A.2    Paddock, M.L.3    Jennings, P.A.4    Elliott, S.J.5
  • 26
    • 78149308097 scopus 로고    scopus 로고
    • Binding of reduced nicotinamide adenine dinucleotide phosphate destabilizes the iron - Sulfur clusters of human mitoNEET
    • Zhou, T., Lin, J., Feng, Y., and Wang, J. (2010) Binding of reduced nicotinamide adenine dinucleotide phosphate destabilizes the iron - sulfur clusters of human mitoNEET. Biochemistry 49, 9604-9612
    • (2010) Biochemistry , vol.49 , pp. 9604-9612
    • Zhou, T.1    Lin, J.2    Feng, Y.3    Wang, J.4
  • 27
    • 0038629115 scopus 로고    scopus 로고
    • 2+ cluster transfer to an apoferredoxin target
    • 2+ cluster transfer to an apoferredoxin target. Biochemistry 42, 5784-5791
    • (2003) Biochemistry , vol.42 , pp. 5784-5791
    • Wu, S.P.1    Cowan, J.A.2
  • 28
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electrontransfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electrontransfer systems. Methods Enzymol. 54, 411-435
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 30
    • 0025276048 scopus 로고
    • Cellular concentrations of enzymes and their substrates
    • Albe, K. R., Butler, M. H., and Wright, B. E. (1990) Cellular concentrations of enzymes and their substrates. J. Theor. Biol. 143, 163-195 (Pubitemid 20141560)
    • (1990) Journal of Theoretical Biology , vol.143 , Issue.2 , pp. 163-195
    • Albe, K.R.1    Butler, M.H.2    Wright, B.E.3
  • 31
    • 0017397091 scopus 로고
    • Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli
    • Andersen, K. B., and von Meyenburg, K. (1977) Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli. J. Biol. Chem. 252, 4151-4156 (Pubitemid 8114436)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.12 , pp. 4151-4156
    • Andersen, K.B.1    Von Meyenburg, K.2
  • 33
    • 79955093351 scopus 로고    scopus 로고
    • Interdomain communication revealed in the diabetes drug target mitoNEET
    • Baxter, E. L., Jennings, P. A., and Onuchic, J. N. (2011) Interdomain communication revealed in the diabetes drug target mitoNEET. Proc. Natl. Acad. Sci. U.S.A. 108, 5266-5271
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5266-5271
    • Baxter, E.L.1    Jennings, P.A.2    Onuchic, J.N.3
  • 34
    • 66649113382 scopus 로고    scopus 로고
    • Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: Comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center
    • Tirrell, T. F., Paddock, M. L., Conlan, A. R., Smoll, E. J., Jr., Nechushtai, R., Jennings, P. A., and Kim, J. E. (2009) Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center. Biochemistry 48, 4747-4752
    • (2009) Biochemistry , vol.48 , pp. 4747-4752
    • Tirrell, T.F.1    Paddock, M.L.2    Conlan, A.R.3    Smoll Jr., E.J.4    Nechushtai, R.5    Jennings, P.A.6    Kim, J.E.7
  • 36
    • 26444433869 scopus 로고    scopus 로고
    • Intracellular redox state: Towards quantitative description
    • DOI 10.1007/s00249-005-0470-3
    • Martinovich, G. G., Cherenkevich, S. N., and Sauer, H. (2005) Intracellular redox state: towards quantitative description. Eur. Biophys. J. 34, 937-942 (Pubitemid 41428190)
    • (2005) European Biophysics Journal , vol.34 , Issue.7 , pp. 937-942
    • Martinovich, G.G.1    Cherenkevich, S.N.2    Sauer, H.3
  • 37
    • 0040442284 scopus 로고    scopus 로고
    • Relationship between iron stores and diabetes mellitus in patients infected by hepatitis C virus: A case-control study
    • Hernandez, C., Genesca, J., Ignasi Esteban, J., Garcia, L., and Simo, R. (2000) Relationship between iron stores and diabetes mellitus in patients infected by hepatitis C virus: a case-control study. Med. Clin. 115, 21-22
    • (2000) Med. Clin. , vol.115 , pp. 21-22
    • Hernandez, C.1    Genesca, J.2    Ignasi Esteban, J.3    Garcia, L.4    Simo, R.5
  • 39
    • 1342325377 scopus 로고    scopus 로고
    • Role of oxidative stress in the etiology of type 2 diabetes and the effect of antioxidant supplementation on glycemic control
    • Opara, E. C. (2004) Role of oxidative stress in the etiology of type 2 diabetes and the effect of antioxidant supplementation on glycemic control. J. Investig. Med. 52, 19-23
    • (2004) J. Investig. Med. , vol.52 , pp. 19-23
    • Opara, E.C.1
  • 40
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • DOI 10.2174/0929867053764635
    • Valko, M., Morris, H., and Cronin, M. T. (2005) Metals, toxicity and oxidative stress. Curr. Med. Chem. 12, 1161-1208 (Pubitemid 40655271)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.10 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.D.3
  • 41
    • 0027279232 scopus 로고
    • Diabetes mellitus and free radicals: Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications
    • Wolff, S. P. (1993) Diabetes mellitus and free radicals: free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications. Br. Med. Bull. 49, 642-652
    • (1993) Br. Med. Bull. , vol.49 , pp. 642-652
    • Wolff, S.P.1
  • 42
    • 77955284362 scopus 로고    scopus 로고
    • Arole for the CISD2 gene in lifespan control and human disease
    • Chen, Y. F., Wu, C. Y., Kirby, R., Kao, C. H., and Tsai, T. F. (2010)Arole for the CISD2 gene in lifespan control and human disease. Ann. N.Y. Acad. Sci. 1201, 58-64
    • (2010) Ann. N.Y. Acad. Sci. , vol.1201 , pp. 58-64
    • Chen, Y.F.1    Wu, C.Y.2    Kirby, R.3    Kao, C.H.4    Tsai, T.F.5
  • 44
    • 76349114046 scopus 로고    scopus 로고
    • Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1
    • Chang, N. C., Nguyen, M., Germain, M., and Shore, G. C. (2010) Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1. EMBO J. 29, 606-618
    • (2010) EMBO J. , vol.29 , pp. 606-618
    • Chang, N.C.1    Nguyen, M.2    Germain, M.3    Shore, G.C.4


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