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Volumn 305, Issue 5, 2013, Pages

Altered mitochondrial morphology and defective protein import reveal novel roles for Bax and/or Bak in skeletal muscle

Author keywords

Apoptosis; Exercise; Gene expression; Mitochondrial biogenesis; Unfolded protein response

Indexed keywords

GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 90; MITOCHONDRIAL PROTEIN; PROTEIN BAK; PROTEIN BAX;

EID: 84883331042     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00058.2013     Document Type: Article
Times cited : (20)

References (65)
  • 1
    • 33947186240 scopus 로고    scopus 로고
    • Effect of chronic contractile activity on SS and IMF mitochondrial apoptotic susceptibility in skeletal muscle
    • Adhihetty PJ, Ljubicic V, Hood DA. Effect of chronic contractile activity on SS and IMF mitochondrial apoptotic susceptibility in skeletal muscle. Am J Physiol Endocrinol Metab 292: E748-E755, 2007.
    • (2007) Am J Physiol Endocrinol Metab , vol.292
    • Adhihetty, P.J.1    Ljubicic, V.2    Hood, D.A.3
  • 2
    • 25444500448 scopus 로고    scopus 로고
    • Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli
    • Adhihetty PJ, Ljubicic V, Menzies KJ, Hood DA. Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli. Am J Physiol Cell Physiol 289: C994-C1001, 2005.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Adhihetty, P.J.1    Ljubicic, V.2    Menzies, K.J.3    Hood, D.A.4
  • 6
    • 34249897492 scopus 로고    scopus 로고
    • A dynamic machinery for import of mitochondrial precursor proteins
    • Bohnert M, Pfanner N, van der Laan M. A dynamic machinery for import of mitochondrial precursor proteins. FEBS Lett 581: 2802-2810, 2007.
    • (2007) FEBS Lett , vol.581 , pp. 2802-2810
    • Bohnert, M.1    Pfanner, N.2    van der Laan, M.3
  • 8
    • 34547442346 scopus 로고    scopus 로고
    • Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
    • Brooks C, Wei Q, Feng L, Dong G, Tao Y, Mei L. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc Natl Acad Sci USA 104: 11649-11654, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11649-11654
    • Brooks, C.1    Wei, Q.2    Feng, L.3    Dong, G.4    Tao, Y.5    Mei, L.6
  • 11
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • Chan DC. Mitochondrial fusion and fission in mammals. Annu Rev Cell Dev Biol 22: 79-99, 2006.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 12
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H, Chan DC. Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 14: R283-R289, 2005.
    • (2005) Hum Mol Genet , vol.14
    • Chen, H.1    Chan, D.C.2
  • 13
    • 0027532691 scopus 로고
    • Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions
    • Cogswell AM, Stevens RJ, Hood DA. Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions. Am J Physiol Cell Physiol 264: C383-C389, 1993.
    • (1993) Am J Physiol Cell Physiol , vol.264
    • Cogswell, A.M.1    Stevens, R.J.2    Hood, D.A.3
  • 14
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondrial as the central control point of apoptosis
    • Desagher S, Martinou JC. Mitochondrial as the central control point of apoptosis. Trends Cell Biol 10: 369-377, 2000.
    • (2000) Trends Cell Biol , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 16
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10: 465-472, 1999.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 17
    • 78149359658 scopus 로고    scopus 로고
    • Multistep and multitask Bax activation
    • Ghibelli L, Diederich M. Multistep and multitask Bax activation. Mitochondrion 10: 604-613, 2010.
    • (2010) Mitochondrion , vol.10 , pp. 604-613
    • Ghibelli, L.1    Diederich, M.2
  • 18
    • 0035168996 scopus 로고    scopus 로고
    • Effects of contractile activity on mitochondrial transcription factor A expression in skeletal muscle
    • Gordon Rungi AA JW, Inagaki H, Hood DA. Effects of contractile activity on mitochondrial transcription factor A expression in skeletal muscle. J Appl Physiol 90: 389-396, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 389-396
    • Gordon Rungi, A.A.J.W.1    Inagaki, H.2    Hood, D.A.3
  • 21
    • 0018894352 scopus 로고
    • Temporal analysis of the nuclear cycle by serial section electron microscopy of the fungus, Saprolegnia ferax
    • Heath IB, Rethoret K. Temporal analysis of the nuclear cycle by serial section electron microscopy of the fungus, Saprolegnia ferax. Eur J Cell Biol 21: 208-213, 1980.
    • (1980) Eur J Cell Biol , vol.21 , pp. 208-213
    • Heath, I.B.1    Rethoret, K.2
  • 23
    • 33746009957 scopus 로고    scopus 로고
    • Coordination of metabolic plasticity in skeletal muscle
    • Hood DA, Irrcher I, Ljubicic V, Joseph AM. Coordination of metabolic plasticity in skeletal muscle. J Exp Biol 209: 2265-2275, 2006.
    • (2006) J Exp Biol , vol.209 , pp. 2265-2275
    • Hood, D.A.1    Irrcher, I.2    Ljubicic, V.3    Joseph, A.M.4
  • 25
    • 84858004448 scopus 로고    scopus 로고
    • Plasticity of TOM complex assembly in skeletal muscle mitochondria in response to chromic contractile activity
    • Joseph AM, Hood DA. Plasticity of TOM complex assembly in skeletal muscle mitochondria in response to chromic contractile activity. Mitochondrion 12: 305-312, 2012.
    • (2012) Mitochondrion , vol.12 , pp. 305-312
    • Joseph, A.M.1    Hood, D.A.2
  • 28
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler M, Pfaller R, Sollner T, Griffiths G, Horstmann H, Pfanner N, Neupert W. Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348: 610-616, 1990.
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1    Pfaller, R.2    Sollner, T.3    Griffiths, G.4    Horstmann, H.5    Pfanner, N.6    Neupert, W.7
  • 29
    • 0030045427 scopus 로고    scopus 로고
    • Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria
    • Komiya T, Sakaguchi M, Mihara K. Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. EMBO J 15: 399-407, 1996.
    • (1996) EMBO J , vol.15 , pp. 399-407
    • Komiya, T.1    Sakaguchi, M.2    Mihara, K.3
  • 31
    • 79952700828 scopus 로고    scopus 로고
    • Bcl-2 proteins and mitochondria-specificity in membrane targeting for death
    • Lindsay J, Esposti MD, Gilmore AP. Bcl-2 proteins and mitochondria-specificity in membrane targeting for death. Biochim Biophys Acta 1813: 532-539, 2011.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 532-539
    • Lindsay, J.1    Esposti, M.D.2    Gilmore, A.P.3
  • 33
    • 4344705049 scopus 로고    scopus 로고
    • Role of UCP3 in state 4 respiration during contractile activity-induced mitochondrial biogenesis
    • Ljubicic V, Adhihetty PJ, Hood DA. Role of UCP3 in state 4 respiration during contractile activity-induced mitochondrial biogenesis. J Appl Physiol 97: 976-983, 2004.
    • (2004) J Appl Physiol , vol.97 , pp. 976-983
    • Ljubicic, V.1    Adhihetty, P.J.2    Hood, D.A.3
  • 35
    • 34247127747 scopus 로고    scopus 로고
    • Mitochondrial protein import and human health and disease
    • Mackenzie JA, Payne RM. Mitochondrial protein import and human health and disease. Biochim Biophys Acta 1772: 509-523, 2007.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 509-523
    • McKenzie, J.A.1    Payne, R.M.2
  • 36
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg UC, Scherer PE, Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J 10: 3273-3280, 1991.
    • (1991) EMBO J , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.C.1    Scherer, P.E.2    Schatz, G.3
  • 37
    • 18744382408 scopus 로고    scopus 로고
    • Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha
    • Marcu MG, Doyle M, Bertolotti A, Ron D, Hendershot L, Neckers L. Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha. Mol Cell Biol 22: 8506-8513, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 8506-8513
    • Marcu, M.G.1    Doyle, M.2    Bertolotti, A.3    Ron, D.4    Hendershot, L.5    Neckers, L.6
  • 38
    • 0036977273 scopus 로고    scopus 로고
    • Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane
    • Motz C, Martin H, Krimmer T, Rassow J. Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane. J Mol Biol 323: 729-738, 2002.
    • (2002) J Mol Biol , vol.323 , pp. 729-738
    • Motz, C.1    Martin, H.2    Krimmer, T.3    Rassow, J.4
  • 39
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78-kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro S, Pelham HR. An Hsp70-like protein in the ER: identity with the 78-kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46: 291-300, 1986.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.2
  • 40
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund AM, Pellegrino MW, Fiorese CJ, Baker BM, Haynes CM. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337: 587-590, 2012.
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 41
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu Rev Biochem 66: 863-917, 1997.
    • (1997) Annu Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 42
    • 84865109297 scopus 로고    scopus 로고
    • Denervation-induced mitochondrial dysfunction and autophagy in skeletal muscle of apoptosis-deficient animals
    • O'Leary MF, Vainshtein A, Carter HN, Zhang Y, Hood DA. Denervation-induced mitochondrial dysfunction and autophagy in skeletal muscle of apoptosis-deficient animals. Am J Physiol Cell Physiol 303: C447-C454, 2012.
    • (2012) Am J Physiol Cell Physiol , vol.303
    • O'Leary, M.F.1    Vainshtein, A.2    Carter, H.N.3    Zhang, Y.4    Hood, D.A.5
  • 43
    • 0029157324 scopus 로고
    • Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle
    • Ornatsky OI, Connor MK, Hood DA. Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle. Biochem J 311: 119-123, 1995.
    • (1995) Biochem J , vol.311 , pp. 119-123
    • Ornatsky, O.I.1    Connor, M.K.2    Hood, D.A.3
  • 45
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex?
    • Ott M, Norberg E, Zhivotovsky B, Orrenius S. Mitochondrial targeting of tBid/Bax: a role for the TOM complex? Cell Death Differ 16: 1075-1082, 2009.
    • (2009) Cell Death Differ , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 46
    • 35848939165 scopus 로고    scopus 로고
    • Mitochondrial protein import, a matter of death?
    • Paschen SA, Weber A, Hacker G. Mitochondrial protein import, a matter of death? Cell Cycle 20: 2434-2439, 2007.
    • (2007) Cell Cycle , vol.20 , pp. 2434-2439
    • Paschen, S.A.1    Weber, A.2    Hacker, G.3
  • 47
    • 0842302344 scopus 로고    scopus 로고
    • Mitochondrial morphology is dynamic and varied
    • Rube DA, van der Bliek AM. Mitochondrial morphology is dynamic and varied. Mol Cell Biochem 256-257: 331-339, 2004.
    • (2004) Mol Cell Biochem , vol.256-257 , pp. 331-339
    • Rube, D.A.1    van der Bliek, A.M.2
  • 48
    • 79959195166 scopus 로고    scopus 로고
    • Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides
    • Saitoh T, Igura M, Miyazaki Y, Ose T, Maita N, Kohda D. Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides. Biochemistry 50: 5487-5496, 2011.
    • (2011) Biochemistry , vol.50 , pp. 5487-5496
    • Saitoh, T.1    Igura, M.2    Miyazaki, Y.3    Ose, T.4    Maita, N.5    Kohda, D.6
  • 50
    • 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 11: 655-667, 2010.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 51
    • 0035166814 scopus 로고    scopus 로고
    • Dynaminrelated protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E, Griparic L, Shurland DL, Vander Bliek AM. Dynaminrelated protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12: 2245-2256, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    vander Bliek, A.M.4
  • 52
    • 79953270811 scopus 로고    scopus 로고
    • Traveling Bax and forth from mitochondria to control apoptosis
    • Soriano ME, Scorrano L. Traveling Bax and forth from mitochondria to control apoptosis. Cell 145: 15-17, 2011.
    • (2011) Cell , vol.145 , pp. 15-17
    • Soriano, M.E.1    Scorrano, L.2
  • 53
    • 1842479419 scopus 로고    scopus 로고
    • Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
    • Stojanovski D, Koutsopoulos OS, Okamoto K, Ryan MT. Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. J Cell Sci 117: 1201-1210, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 54
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 11: 621-632, 2010.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 55
    • 0027478067 scopus 로고
    • Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle
    • Takahashi M, Hood DA. Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle. J Appl Physiol 74: 934-941, 1993.
    • (1993) J Appl Physiol , vol.74 , pp. 934-941
    • Takahashi, M.1    Hood, D.A.2
  • 56
    • 0029914131 scopus 로고    scopus 로고
    • Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Differential import regulation in distinct subcellular regions
    • Takahashi M, Hood DA. Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Differential import regulation in distinct subcellular regions. J Biol Chem 271: 27285-27291, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 27285-27291
    • Takahashi, M.1    Hood, D.A.2
  • 57
    • 0031831491 scopus 로고    scopus 로고
    • Contractile activityinduced adaptations in the mitochondrial protein import system
    • Takahashi M, Chesley A, Freyssenet D, Hood DA. Contractile activityinduced adaptations in the mitochondrial protein import system. Am J Physiol Cell Physiol 274: C1380-C1387, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.274
    • Takahashi, M.1    Chesley, A.2    Freyssenet, D.3    Hood, D.A.4
  • 58
    • 34249894164 scopus 로고    scopus 로고
    • Pushing, pulling and trappingmodes of motor protein supported protein translocation
    • Tomkiewicz D, Nouwen N, Driessen AJ. Pushing, pulling and trappingmodes of motor protein supported protein translocation. FEBS Lett 581: 2820-2828, 2007.
    • (2007) FEBS Lett , vol.581 , pp. 2820-2828
    • Tomkiewicz, D.1    Nouwen, N.2    Driessen, A.J.3
  • 59
    • 56349153028 scopus 로고    scopus 로고
    • Protein transport machineries for precursor translocation across the inner mitochondrial membrane
    • Wagner K, Mick DU, Rehling P. Protein transport machineries for precursor translocation across the inner mitochondrial membrane. Biochim Biophys Acta 1793: 52-59, 2009.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 52-59
    • Wagner, K.1    Mick, D.U.2    Rehling, P.3
  • 63
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: How BH3-only proteins induce apoptosis
    • Willis SN, Adams JM. Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol 17: 617-625, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.