메뉴 건너뛰기




Volumn 3, Issue 1, 2013, Pages 237-245

Complementary RNA and Protein Profiling Identifies Iron as a Key Regulator of Mitochondrial Biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY RNA; IRON; MITOCHONDRIAL PROTEIN; REGULATOR PROTEIN;

EID: 84873162025     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2012.11.029     Document Type: Article
Times cited : (69)

References (39)
  • 1
    • 0035016566 scopus 로고    scopus 로고
    • Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells
    • Andersson U., Scarpulla R.C. Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells. Mol. Cell. Biol. 2001, 21:3738-3749.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3738-3749
    • Andersson, U.1    Scarpulla, R.C.2
  • 2
    • 78149359713 scopus 로고    scopus 로고
    • Mitochondria in response to nutrients and nutrient-sensitive pathways
    • Baltzer C., Tiefenböck S.K., Frei C. Mitochondria in response to nutrients and nutrient-sensitive pathways. Mitochondrion 2010, 10:589-597.
    • (2010) Mitochondrion , vol.10 , pp. 589-597
    • Baltzer, C.1    Tiefenböck, S.K.2    Frei, C.3
  • 4
    • 66149118241 scopus 로고    scopus 로고
    • Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans
    • Calvo S.E., Pagliarini D.J., Mootha V.K. Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans. Proc. Natl. Acad. Sci. USA 2009, 106:7507-7512.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7507-7512
    • Calvo, S.E.1    Pagliarini, D.J.2    Mootha, V.K.3
  • 5
    • 0037631496 scopus 로고    scopus 로고
    • Iron chelators for the treatment of iron overload disease: relationship between structure, redox activity, and toxicity
    • Chaston T.B., Richardson D.R. Iron chelators for the treatment of iron overload disease: relationship between structure, redox activity, and toxicity. Am. J. Hematol. 2003, 73:200-210.
    • (2003) Am. J. Hematol. , vol.73 , pp. 200-210
    • Chaston, T.B.1    Richardson, D.R.2
  • 6
    • 73349099034 scopus 로고    scopus 로고
    • Specific iron chelators determine the route of ferritin degradation
    • De Domenico I., Ward D.M., Kaplan J. Specific iron chelators determine the route of ferritin degradation. Blood 2009, 114:4546-4551.
    • (2009) Blood , vol.114 , pp. 4546-4551
    • De Domenico, I.1    Ward, D.M.2    Kaplan, J.3
  • 7
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S., Schon E.A. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 2003, 348:2656-2668.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 8
    • 0038332156 scopus 로고    scopus 로고
    • Novel roles for iron regulatory proteins in the adaptive response to iron deficiency
    • Eisenstein R.S., Ross K.L. Novel roles for iron regulatory proteins in the adaptive response to iron deficiency. J. Nutr. 2003, 133(5, Suppl 1):1510S-1516S.
    • (2003) J. Nutr. , vol.133 , Issue.5 SUPPL 1
    • Eisenstein, R.S.1    Ross, K.L.2
  • 9
    • 4344693235 scopus 로고    scopus 로고
    • Mitochondrial signaling pathways: a receiver/integrator organelle
    • Goldenthal M.J., Marín-García J. Mitochondrial signaling pathways: a receiver/integrator organelle. Mol. Cell. Biochem. 2004, 262:1-16.
    • (2004) Mol. Cell. Biochem. , vol.262 , pp. 1-16
    • Goldenthal, M.J.1    Marín-García, J.2
  • 10
    • 67651159365 scopus 로고    scopus 로고
    • Transcriptional control of mitochondrial biogenesis and function
    • Hock M.B., Kralli A. Transcriptional control of mitochondrial biogenesis and function. Annu. Rev. Physiol. 2009, 71:177-203.
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 177-203
    • Hock, M.B.1    Kralli, A.2
  • 12
    • 0037134493 scopus 로고    scopus 로고
    • The PGC-1-related protein PERC is a selective coactivator of estrogen receptor alpha
    • Kressler D., Schreiber S.N., Knutti D., Kralli A. The PGC-1-related protein PERC is a selective coactivator of estrogen receptor alpha. J. Biol. Chem. 2002, 277:13918-13925.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13918-13925
    • Kressler, D.1    Schreiber, S.N.2    Knutti, D.3    Kralli, A.4
  • 13
    • 84857546393 scopus 로고    scopus 로고
    • Control of mitochondrial activity by miRNAs
    • Li P., Jiao J., Gao G., Prabhakar B.S. Control of mitochondrial activity by miRNAs. J. Cell. Biochem. 2012, 113:1104-1110.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 1104-1110
    • Li, P.1    Jiao, J.2    Gao, G.3    Prabhakar, B.S.4
  • 14
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 15
    • 0037127204 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta ), a novel PGC-1-related transcription coactivator associated with host cell factor
    • Lin J., Puigserver P., Donovan J., Tarr P., Spiegelman B.M. Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta ), a novel PGC-1-related transcription coactivator associated with host cell factor. J. Biol. Chem. 2002, 277:1645-1648.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1645-1648
    • Lin, J.1    Puigserver, P.2    Donovan, J.3    Tarr, P.4    Spiegelman, B.M.5
  • 16
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • Lowell B.B., Shulman G.I. Mitochondrial dysfunction and type 2 diabetes. Science 2005, 307:384-387.
    • (2005) Science , vol.307 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2
  • 17
    • 65449184945 scopus 로고    scopus 로고
    • Worldwide prevalence of anaemia, WHO Vitamin and Mineral Nutrition Information System, 1993-2005
    • McLean E., Cogswell M., Egli I., Wojdyla D., de Benoist B. Worldwide prevalence of anaemia, WHO Vitamin and Mineral Nutrition Information System, 1993-2005. Public Health Nutr. 2009, 12:444-454.
    • (2009) Public Health Nutr. , vol.12 , pp. 444-454
    • McLean, E.1    Cogswell, M.2    Egli, I.3    Wojdyla, D.4    de Benoist, B.5
  • 18
    • 78650483039 scopus 로고    scopus 로고
    • Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation
    • Mick D.U., Fox T.D., Rehling P. Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation. Nat. Rev. Mol. Cell Biol. 2011, 12:14-20.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 14-20
    • Mick, D.U.1    Fox, T.D.2    Rehling, P.3
  • 21
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., Tuttle M.S., Powelson J., Vaughn M.B., Donovan A., Ward D.M., Ganz T., Kaplan J. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004, 306:2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 23
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong S.E., Mann M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 2006, 1:2650-2660.
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 27
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • Puigserver P., Wu Z., Park C.W., Graves R., Wright M., Spiegelman B.M. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 1998, 92:829-839.
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5    Spiegelman, B.M.6
  • 29
    • 42049114034 scopus 로고    scopus 로고
    • Transcriptional paradigms in mammalian mitochondrial biogenesis and function
    • Scarpulla R.C. Transcriptional paradigms in mammalian mitochondrial biogenesis and function. Physiol. Rev. 2008, 88:611-638.
    • (2008) Physiol. Rev. , vol.88 , pp. 611-638
    • Scarpulla, R.C.1
  • 30
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: from proteomics to functional mechanisms
    • Schmidt O., Pfanner N., Meisinger C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat. Rev. Mol. Cell Biol. 2010, 11:655-667.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 32
    • 33646124709 scopus 로고    scopus 로고
    • Complementary action of the PGC-1 coactivators in mitochondrial biogenesis and brown fat differentiation
    • Uldry M., Yang W., St-Pierre J., Lin J., Seale P., Spiegelman B.M. Complementary action of the PGC-1 coactivators in mitochondrial biogenesis and brown fat differentiation. Cell Metab. 2006, 3:333-341.
    • (2006) Cell Metab. , vol.3 , pp. 333-341
    • Uldry, M.1    Yang, W.2    St-Pierre, J.3    Lin, J.4    Seale, P.5    Spiegelman, B.M.6
  • 33
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 35
    • 33749265862 scopus 로고    scopus 로고
    • Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1
    • Yoon Y.S., Yoon D.S., Lim I.K., Yoon S.H., Chung H.Y., Rojo M., Malka F., Jou M.J., Martinou J.C., Yoon G. Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1. J. Cell. Physiol. 2006, 209:468-480.
    • (2006) J. Cell. Physiol. , vol.209 , pp. 468-480
    • Yoon, Y.S.1    Yoon, D.S.2    Lim, I.K.3    Yoon, S.H.4    Chung, H.Y.5    Rojo, M.6    Malka, F.7    Jou, M.J.8    Martinou, J.C.9    Yoon, G.10
  • 37
    • 34548286520 scopus 로고    scopus 로고
    • Tuning cell cycle regulation with an iron key
    • Yu Y., Kovacevic Z., Richardson D.R. Tuning cell cycle regulation with an iron key. Cell Cycle 2007, 6:1982-1994.
    • (2007) Cell Cycle , vol.6 , pp. 1982-1994
    • Yu, Y.1    Kovacevic, Z.2    Richardson, D.R.3
  • 39
    • 34247614521 scopus 로고    scopus 로고
    • HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity
    • Zhang H., Gao P., Fukuda R., Kumar G., Krishnamachary B., Zeller K.I., Dang C.V., Semenza G.L. HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity. Cancer Cell 2007, 11:407-420.
    • (2007) Cancer Cell , vol.11 , pp. 407-420
    • Zhang, H.1    Gao, P.2    Fukuda, R.3    Kumar, G.4    Krishnamachary, B.5    Zeller, K.I.6    Dang, C.V.7    Semenza, G.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.