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Volumn 1850, Issue 10, 2015, Pages 2041-2047

Structural mechanisms of cyclophilin D-dependent control of the mitochondrial permeability transition pore

Author keywords

Cyclophilin D; Mitochondrial permeability transition; Peptidyl prolyl cis trans isomerase

Indexed keywords

CYCLOPHILIN D; LIGAND; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; CARRIER PROTEIN; CYCLOPHILIN; PPID PROTEIN, HUMAN;

EID: 84940535314     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.11.009     Document Type: Review
Times cited : (94)

References (66)
  • 2
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • D.R. Hunter, R.A. Haworth, and J.H. Southard Relationship between configuration, function, and permeability in calcium-treated mitochondria J. Biol. Chem. 251 1976 5069 5077
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 3
    • 0018332596 scopus 로고
    • 2 +-induced membrane transition in mitochondria. I. The protective mechanisms
    • 2 +-induced membrane transition in mitochondria. I. The protective mechanisms Arch. Biochem. Biophys. 195 1979 453 459
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 6
    • 77951920370 scopus 로고    scopus 로고
    • The cardiac mitochondrion: Nexus of stress
    • C.P. Baines The cardiac mitochondrion: nexus of stress Annu. Rev. Physiol. 72 2010 61 80
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 61-80
    • Baines, C.P.1
  • 7
    • 11144300815 scopus 로고    scopus 로고
    • Mitochondrial permeability transitions: How many doors to the house?
    • M. Zoratti, I. Szabo, and U. De Marchi Mitochondrial permeability transitions: how many doors to the house? Biochim. Biophys. Acta 1706 2005 40 52
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 40-52
    • Zoratti, M.1    Szabo, I.2    De Marchi, U.3
  • 8
    • 0023821864 scopus 로고
    • 2 +-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2 +-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress Biochem. J. 255 1988 357 360
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 10
    • 79957964641 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and cyclophilin D in cardioprotection
    • F. Di Lisa, A. Carpi, V. Giorgio, and P. Bernardi The mitochondrial permeability transition pore and cyclophilin D in cardioprotection Biochim. Biophys. Acta 1813 2011 1316 1322
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1316-1322
    • Di Lisa, F.1    Carpi, A.2    Giorgio, V.3    Bernardi, P.4
  • 11
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • N. Fournier, G. Ducet, and A. Crevat Action of cyclosporine on mitochondrial calcium fluxes J. Bioenerg. Biomembr. 19 1987 297 303
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 13
    • 0026696585 scopus 로고
    • Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
    • C.P. Connern, and A.P. Halestrap Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin Biochem. J. 284 Pt 2 1992 381 385
    • (1992) Biochem. J. , vol.284 , pp. 381-385
    • Connern, C.P.1    Halestrap, A.P.2
  • 14
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • M. Crompton, S. Virji, and J.M. Ward Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore Eur. J. Biochem. 258 1998 729 735
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 16
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • C.P. Baines, R.A. Kaiser, T. Sheiko, W.J. Craigen, and J.D. Molkentin Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 9 2007 550 555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 17
    • 46349097952 scopus 로고    scopus 로고
    • Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore
    • A.W. Leung, and A.P. Halestrap Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore Biochim. Biophys. Acta 1777 2008 946 952
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 946-952
    • Leung, A.W.1    Halestrap, A.P.2
  • 18
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • A.W. Leung, P. Varanyuwatana, and A.P. Halestrap The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition J. Biol. Chem. 283 2008 26312 26323
    • (2008) J. Biol. Chem. , vol.283 , pp. 26312-26323
    • Leung, A.W.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 19
    • 84856526180 scopus 로고    scopus 로고
    • The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore
    • P. Varanyuwatana, and A.P. Halestrap The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore Mitochondrion 12 2012 120 125
    • (2012) Mitochondrion , vol.12 , pp. 120-125
    • Varanyuwatana, P.1    Halestrap, A.P.2
  • 21
    • 84905042938 scopus 로고    scopus 로고
    • Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy
    • J.Q. Kwong, J. Davis, C.P. Baines, M.A. Sargent, J. Karch, X. Wang, T. Huang, and J.D. Molkentin Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy Cell Death Differ. 21 2014 1209 1217
    • (2014) Cell Death Differ. , vol.21 , pp. 1209-1217
    • Kwong, J.Q.1    Davis, J.2    Baines, C.P.3    Sargent, M.A.4    Karch, J.5    Wang, X.6    Huang, T.7    Molkentin, J.D.8
  • 24
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D
    • E. Basso, L. Fante, J. Fowlkes, V. Petronilli, M.A. Forte, and P. Bernardi Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D J. Biol. Chem. 280 2005 18558 18561
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 29
    • 0037823485 scopus 로고    scopus 로고
    • Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60 K peptide
    • U. Reidt, M.C. Wahl, D. Fasshauer, D.S. Horowitz, R. Lührmann, and R. Ficner Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60 K peptide J. Mol. Biol. 331 2003 45 56
    • (2003) J. Mol. Biol. , vol.331 , pp. 45-56
    • Reidt, U.1    Wahl, M.C.2    Fasshauer, D.3    Horowitz, D.S.4    Lührmann, R.5    Ficner, R.6
  • 30
    • 33744904998 scopus 로고    scopus 로고
    • Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP
    • C. Xu, J. Zhang, X. Huang, J. Sun, Y. Xu, Y. Tang, J. Wu, Y. Shi, Q. Huang, and Q. Zhang Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP J. Biol. Chem. 281 2006 15900 15908
    • (2006) J. Biol. Chem. , vol.281 , pp. 15900-15908
    • Xu, C.1    Zhang, J.2    Huang, X.3    Sun, J.4    Xu, Y.5    Tang, Y.6    Wu, J.7    Shi, Y.8    Huang, Q.9    Zhang, Q.10
  • 32
    • 0029982651 scopus 로고    scopus 로고
    • Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization
    • Y. Zhao, and H. Ke Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization Biochemistry 35 1996 7356 7361
    • (1996) Biochemistry , vol.35 , pp. 7356-7361
    • Zhao, Y.1    Ke, H.2
  • 33
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • D.T. Lin, and J.D. Lechleiter Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization J. Biol. Chem. 277 2002 31134 31141
    • (2002) J. Biol. Chem. , vol.277 , pp. 31134-31141
    • Lin, D.T.1    Lechleiter, J.D.2
  • 34
    • 39749107259 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 096-A resolution
    • K. Kajitani, M. Fujihashi, Y. Kobayashi, S. Shimizu, Y. Tsujimoto, and K. Miki Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 096-A resolution Proteins 70 2008 1635 1639
    • (2008) Proteins , vol.70 , pp. 1635-1639
    • Kajitani, K.1    Fujihashi, M.2    Kobayashi, Y.3    Shimizu, S.4    Tsujimoto, Y.5    Miki, K.6
  • 35
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • E.J. Griffiths, and A.P. Halestrap Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion Biochem. J. 307 Pt 1 1995 93 98
    • (1995) Biochem. J. , vol.307 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 36
    • 0032860116 scopus 로고    scopus 로고
    • Cyclosporin A and its nonimmunosuppressive analogue N-Me-Val-4-cyclosporin A mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons
    • L. Khaspekov, H. Friberg, A. Halestrap, I. Viktorov, and T. Wieloch Cyclosporin A and its nonimmunosuppressive analogue N-Me-Val-4-cyclosporin A mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons Eur. J. Neurosci. 11 1999 3194 3198
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 3194-3198
    • Khaspekov, L.1    Friberg, H.2    Halestrap, A.3    Viktorov, I.4    Wieloch, T.5
  • 37
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel
    • A. Nicolli, E. Basso, V. Petronilli, R.M. Wenger, and P. Bernardi Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel J. Biol. Chem. 271 1996 2185 2192
    • (1996) J. Biol. Chem. , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 38
    • 0037144409 scopus 로고    scopus 로고
    • Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A
    • S.J. Clarke, G.P. McStay, and A.P. Halestrap Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A J. Biol. Chem. 277 2002 34793 34799
    • (2002) J. Biol. Chem. , vol.277 , pp. 34793-34799
    • Clarke, S.J.1    McStay, G.P.2    Halestrap, A.P.3
  • 39
    • 70350553816 scopus 로고    scopus 로고
    • Redox characterization of human cyclophilin D: Identification of a new mammalian mitochondrial redox sensor?
    • D. Linard, A. Kandlbinder, H. Degand, P. Morsomme, K.J. Dietz, and B. Knoops Redox characterization of human cyclophilin D: identification of a new mammalian mitochondrial redox sensor? Arch. Biochem. Biophys. 491 2009 39 45
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 39-45
    • Linard, D.1    Kandlbinder, A.2    Degand, H.3    Morsomme, P.4    Dietz, K.J.5    Knoops, B.6
  • 41
    • 81155123702 scopus 로고    scopus 로고
    • Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore
    • T.T. Nguyen, M.V. Stevens, M. Kohr, C. Steenbergen, M.N. Sack, and E. Murphy Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore J. Biol. Chem. 286 2011 40184 40192
    • (2011) J. Biol. Chem. , vol.286 , pp. 40184-40192
    • Nguyen, T.T.1    Stevens, M.V.2    Kohr, M.3    Steenbergen, C.4    Sack, M.N.5    Murphy, E.6
  • 43
  • 44
    • 84862675016 scopus 로고    scopus 로고
    • P53 Opens the mitochondrial permeability transition pore to trigger necrosis
    • A.V. Vaseva, N.D. Marchenko, K. Ji, S.E. Tsirka, S. Holzmann, and U.M. Moll p53 Opens the mitochondrial permeability transition pore to trigger necrosis Cell 149 2012 1536 1548
    • (2012) Cell , vol.149 , pp. 1536-1548
    • Vaseva, A.V.1    Marchenko, N.D.2    Ji, K.3    Tsirka, S.E.4    Holzmann, S.5    Moll, U.M.6
  • 45
    • 84868686651 scopus 로고    scopus 로고
    • Is p53 the long-sought molecular trigger for cyclophilin D-regulated mitochondrial permeability transition pore formation and necrosis?
    • J. Karch, and J.D. Molkentin Is p53 the long-sought molecular trigger for cyclophilin D-regulated mitochondrial permeability transition pore formation and necrosis? Circ. Res. 111 2012 1258 1260
    • (2012) Circ. Res. , vol.111 , pp. 1258-1260
    • Karch, J.1    Molkentin, J.D.2
  • 46
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • A.V. Hafner, J. Dai, A.P. Gomes, C.Y. Xiao, C.M. Palmeira, A. Rosenzweig, and D.A. Sinclair Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy Aging (Albany NY) 2 2010 914 923
    • (2010) Aging (Albany NY) , vol.2 , pp. 914-923
    • Hafner, A.V.1    Dai, J.2    Gomes, A.P.3    Xiao, C.Y.4    Palmeira, C.M.5    Rosenzweig, A.6    Sinclair, D.A.7
  • 47
    • 84890381258 scopus 로고    scopus 로고
    • Cyclophilin D and acetylation: A new link in cardiac signaling
    • M.P. Lam, E. Lau, D.A. Liem, and P. Ping Cyclophilin D and acetylation: a new link in cardiac signaling Circ. Res. 113 2013 1268 1269
    • (2013) Circ. Res. , vol.113 , pp. 1268-1269
    • Lam, M.P.1    Lau, E.2    Liem, D.A.3    Ping, P.4
  • 48
    • 77951176793 scopus 로고    scopus 로고
    • Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria
    • N. Shulga, R. Wilson-Smith, and J.G. Pastorino Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria J. Cell Sci. 123 2010 894 902
    • (2010) J. Cell Sci. , vol.123 , pp. 894-902
    • Shulga, N.1    Wilson-Smith, R.2    Pastorino, J.G.3
  • 50
    • 78649743734 scopus 로고    scopus 로고
    • Ethanol sensitizes mitochondria to the permeability transition by inhibiting deacetylation of cyclophilin-D mediated by sirtuin-3
    • N. Shulga, and J.G. Pastorino Ethanol sensitizes mitochondria to the permeability transition by inhibiting deacetylation of cyclophilin-D mediated by sirtuin-3 J. Cell Sci. 123 2010 4117 4127
    • (2010) J. Cell Sci. , vol.123 , pp. 4117-4127
    • Shulga, N.1    Pastorino, J.G.2
  • 51
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • K. Woodfield, A. Ruck, D. Brdiczka, and A.P. Halestrap Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition Biochem. J. 336 Pt 2 1998 287 290
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 53
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • A.P. Halestrap, K.Y. Woodfield, and C.P. Connern Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase J. Biol. Chem. 272 1997 3346 3354
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 55
    • 84916620324 scopus 로고    scopus 로고
    • The mitochondrial permeability transition: A current perspective on its identity and role in ischaemia/reperfusion injury
    • A.P. Halestrap, and A.P. Richardson The mitochondrial permeability transition: a current perspective on its identity and role in ischaemia/reperfusion injury J. Mol. Cell. Cardiol. 2014 10.1016/j.yjmcc.2014.08.018
    • (2014) J. Mol. Cell. Cardiol.
    • Halestrap, A.P.1    Richardson, A.P.2
  • 57
    • 84873120174 scopus 로고    scopus 로고
    • The ATP synthase: The understood, the uncertain and the unknown
    • J.E. Walker The ATP synthase: the understood, the uncertain and the unknown Biochem. Soc. Trans. 41 2013 1 16
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1-16
    • Walker, J.E.1
  • 58
    • 0028905958 scopus 로고
    • The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition
    • D.R. Pfeiffer, T.I. Gudz, S.A. Novgorodov, and W.L. Erdahl The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition J. Biol. Chem. 270 1995 4923 4932
    • (1995) J. Biol. Chem. , vol.270 , pp. 4923-4932
    • Pfeiffer, D.R.1    Gudz, T.I.2    Novgorodov, S.A.3    Erdahl, W.L.4
  • 59
    • 0036044373 scopus 로고    scopus 로고
    • Mitochondrial energy dissipation by fatty acids: Mechanisms and implications for cell death
    • P. Bernardi, D. Penzo, and L. Wojtczak Mitochondrial energy dissipation by fatty acids: mechanisms and implications for cell death Vitam. Horm. 65 2002 97 126
    • (2002) Vitam. Horm. , vol.65 , pp. 97-126
    • Bernardi, P.1    Penzo, D.2    Wojtczak, L.3
  • 63
    • 85047264961 scopus 로고    scopus 로고
    • Mitochondrial ATP synthase: Is the molecular engine of life also an efficient death machine?
    • M. Gutierrez-Aguilar, and C.P. Baines Mitochondrial ATP synthase: is the molecular engine of life also an efficient death machine? Bioenergetics 3 2014 e119
    • (2014) Bioenergetics , vol.3 , pp. e119
    • Gutierrez-Aguilar, M.1    Baines, C.P.2
  • 64
    • 84906268632 scopus 로고    scopus 로고
    • 0 ATP synthase forms the mitochondrial permeability transition pore: A critical appraisal
    • 0 ATP synthase forms the mitochondrial permeability transition pore: a critical appraisal Front. Oncol. 4 2014 234
    • (2014) Front. Oncol. , vol.4 , pp. 234
    • Halestrap, A.P.1
  • 66
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • W.C. Hallows, S. Lee, and J.M. Denu Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases Proc. Natl. Acad. Sci. U.S.A. 103 2006 10230 10235
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3


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