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Volumn 1807, Issue 11, 2011, Pages 1474-1481

Characteristics of the turnover of uncoupling protein 3 by the ubiquitin proteasome system in isolated mitochondria

Author keywords

26S proteasome; In vitro; Mitochondrion; Ubiquitin; UCP3; Uncoupling protein

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOCHROME C; PROTEASOME; UBIQUITIN PROTEASOME SYSTEM; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 3;

EID: 80052710701     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.07.011     Document Type: Article
Times cited : (14)

References (23)
  • 1
    • 1942468196 scopus 로고    scopus 로고
    • The role and structure of mitochondrial carriers
    • DOI 10.1016/S0014-5793(04)00242-X, PII S001457930400242X
    • E.R.S. Kunji The role and structure of mitochondrial carriers FEBS Lett. 564 2004 239 244 (Pubitemid 38520927)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 239-244
    • Kunji, E.R.S.1
  • 2
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • DOI 10.1038/nature02056
    • E. Pebay-Peyroula, C. Dahout-Gonzalez, R. Kahn, V. Trézé guet, G.J. Lauquin, and G. Brandolin Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside Nature 426 2003 39 44 (Pubitemid 37432535)
    • (2003) Nature , vol.426 , Issue.6962 , pp. 39-44
    • Pebay-Peyroula, E.1    Dahout-Gonzalez, C.2    Kahn, R.3    Trezeguet, V.4    Lauquin, G.J.-M.5    Brandolin, G.6
  • 3
    • 33644555509 scopus 로고    scopus 로고
    • Mitochondrial carriers in the cytoplasmic state have a common substrate binding site
    • A.J. Robinson, and E.R.S. Kunji Mitochondrial carriers in the cytoplasmic state have a common substrate binding site Proc. Natl. Acad. Sci. U S A 103 2006 2617 2622
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 2617-2622
    • Robinson, A.J.1    Kunji, E.R.S.2
  • 5
    • 0031560941 scopus 로고    scopus 로고
    • UCP3: An uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue
    • DOI 10.1006/bbrc.1997.6740
    • A.J. Vidal-Puig, G. Solanes, D. Grujic, J.S. Flier, and B.B. Lowell UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue Biochem. Biophys. Res. Commun. 235 1997 79 82 (Pubitemid 27302688)
    • (1997) Biochemical and Biophysical Research Communications , vol.235 , Issue.1 , pp. 79-82
    • Vidal-Puig, A.1    Solanes, G.2    Grujic, D.3    Flier, J.S.4    Lowell, B.B.5
  • 6
    • 25144476923 scopus 로고    scopus 로고
    • Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
    • M.D. Brand, and T.C. Esteves Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3 Cell Metab. 2 2005 85 93
    • (2005) Cell Metab. , vol.2 , pp. 85-93
    • Brand, M.D.1    Esteves, T.C.2
  • 7
    • 33846446089 scopus 로고    scopus 로고
    • UCP2 is a mitochondrial transporter with an unusual very short half-life
    • DOI 10.1016/j.febslet.2007.01.010, PII S0014579307000312
    • S. Rousset, J. Mozo, G. Dujardin, Y. Emre, S. Masscheleyn, D. Ricquier, and A. Cassardoulcier UCP2 is a mitochondrial transporter with an unusual very short half-life FEBS Lett. 581 2007 479 482 (Pubitemid 46149624)
    • (2007) FEBS Letters , vol.581 , Issue.3 , pp. 479-482
    • Rousset, S.1    Mozo, J.2    Dujardin, G.3    Emre, Y.4    Masscheleyn, S.5    Ricquier, D.6    Cassard-Doulcier, A.-M.7
  • 8
    • 76649093912 scopus 로고    scopus 로고
    • Degradation of an intramitochondrial protein by the cytosolic proteasome
    • V. Azzu, and M.D. Brand Degradation of an intramitochondrial protein by the cytosolic proteasome J. Cell Sci. 123 2010 578 585
    • (2010) J. Cell Sci. , vol.123 , pp. 578-585
    • Azzu, V.1    Brand, M.D.2
  • 9
    • 76549091356 scopus 로고    scopus 로고
    • Rapid turnover of mitochondrial uncoupling protein 3
    • V. Azzu, S.A. Mookerjee, and M.D. Brand Rapid turnover of mitochondrial uncoupling protein 3 Biochem. J. 426 2010 13 17
    • (2010) Biochem. J. , vol.426 , pp. 13-17
    • Azzu, V.1    Mookerjee, S.A.2    Brand, M.D.3
  • 10
    • 0035988014 scopus 로고    scopus 로고
    • Differentiation-dependent expression of cathepsin D and importance of lysosomal proteolysis in the degradation of UCP1 in brown adipocytes
    • DOI 10.1139/y02-067
    • B. Moazed, and M. Desaultes Differentiation-dependent expression of cathepsin D and importance of lysosomal proteolysis in the degradation of UCP1 in brown adipocytes Can. J. Physiol. Pharmacol. 80 2002 515 525 (Pubitemid 34743931)
    • (2002) Canadian Journal of Physiology and Pharmacology , vol.80 , Issue.6 , pp. 515-525
    • Moazed, B.1    Desautels, M.2
  • 11
    • 0026642858 scopus 로고
    • Induction and degradation of the uncoupling protein thermogenin in brown adipocytes in vitro and in vivo. Evidence for a rapidly degradable pool
    • P. Puigserver, D. Herron, M. Gianotti, A. Palou, B. Cannon, and J. Nedergaard Induction and degradation of the uncoupling protein thermogenin in brown adipocytes in vitro and in vivo. Evidence for a rapidly degradable pool Biochem. J. 284 1992 393 398
    • (1992) Biochem. J. , vol.284 , pp. 393-398
    • Puigserver, P.1    Herron, D.2    Gianotti, M.3    Palou, A.4    Cannon, B.5    Nedergaard, J.6
  • 12
    • 52949094588 scopus 로고    scopus 로고
    • Dynamic regulation of uncoupling protein 2 content in INS-1E insulinoma cells
    • V. Azzu, C. Affourtit, E. Breen, N. Parker, and M.D. Brand Dynamic regulation of uncoupling protein 2 content in INS-1E insulinoma cells Biochim. Biophys. Acta 1777 2008 1378 1383
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1378-1383
    • Azzu, V.1    Affourtit, C.2    Breen, E.3    Parker, N.4    Brand, M.D.5
  • 13
    • 70349971955 scopus 로고    scopus 로고
    • Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria
    • N. Parker, P.G. Crichton, A.J. Vidal-Puig, and M.D. Brand Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria J. Bioenerg. Biomembr. 41 2009 335 342
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 335-342
    • Parker, N.1    Crichton, P.G.2    Vidal-Puig, A.J.3    Brand, M.D.4
  • 14
    • 84934440444 scopus 로고    scopus 로고
    • Studies of thermogenesis and mitochondrial function in adipose tissues
    • B. Cannon, and J. Nedergaard Studies of thermogenesis and mitochondrial function in adipose tissues Methods Mol. Biol. 456 2008 109 121
    • (2008) Methods Mol. Biol. , vol.456 , pp. 109-121
    • Cannon, B.1    Nedergaard, J.2
  • 16
    • 36849059755 scopus 로고    scopus 로고
    • Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites
    • DOI 10.1038/nsmb1335, PII NSMB1335
    • M.F. Kleijnen, J. Roelofs, S. Park, N.A. Hathaway, M. Glickman, R.W. King, and D. Finley Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites Nat. Struct. Mol. Biol. 14 2007 1180 1188 (Pubitemid 350223335)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1180-1188
    • Kleijnen, M.F.1    Roelofs, J.2    Park, S.3    Hathaway, N.A.4    Glickman, M.5    King, R.W.6    Finley, D.7
  • 18
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 19
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • X. Wang, J. Yen, P. Kaiser, and L. Huang Regulation of the 26S proteasome complex during oxidative stress Sci. Signal 3 2010 ra88
    • (2010) Sci. Signal , vol.3 , pp. 88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 20
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • DOI 10.1074/jbc.M206279200
    • R. Shringarpure, T. Grune, J. Mehlhase, and K.J.A. Davies Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome J. Biol. Chem. 278 2003 311 318 (Pubitemid 36043578)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 21
    • 48249083981 scopus 로고    scopus 로고
    • Stimulation of mitochondrial proton conductance by hydroxynonenal requires a high membrane potential
    • N. Parker, A.J. Vidal-Puig, and M.D. Brand Stimulation of mitochondrial proton conductance by hydroxynonenal requires a high membrane potential Biosci. Rep. 28 2008 83 88
    • (2008) Biosci. Rep. , vol.28 , pp. 83-88
    • Parker, N.1    Vidal-Puig, A.J.2    Brand, M.D.3
  • 22
    • 43549101948 scopus 로고    scopus 로고
    • Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria
    • DOI 10.1042/BJ20080006
    • N. Parker, C. Affourtit, A. Vidal-Puig, and M.D. Brand Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria Biochem. J. 412 2008 131 139 (Pubitemid 351678343)
    • (2008) Biochemical Journal , vol.412 , Issue.1 , pp. 131-139
    • Parker, N.1    Affourtit, C.2    Vidal-Puig, A.3    Brand, M.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.