메뉴 건너뛰기




Volumn 4 AUG, Issue , 2014, Pages

The c ring of the F1Fo ATP synthase forms the mitochondrial permeability transition pore: A critical appraisal

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; ADENINE NUCLEOTIDE TRANSLOCASE; BONGKREKIC ACID; CARBOXYATRACTYLOSIDE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PHOSPHATE TRANSPORTER; PROTEOLIPOSOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84906268632     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2014.00234     Document Type: Note
Times cited : (60)

References (22)
  • 1
    • 84904646147 scopus 로고    scopus 로고
    • An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore
    • Alavian, K.N., Beutner, G., Lazrove, E., Sacchetti, S., Park, H.A., Licznerski, P., et al (2014). An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore. Proc. Natl. Acad. Sci. USA 111, 10580-10585.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 10580-10585
    • Alavian, K.N.1    Beutner, G.2    Lazrove, E.3    Sacchetti, S.4    Park, H.A.5    Licznerski, P.6
  • 2
    • 84883776628 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: a mystery solved?
    • doi: 10.3389
    • Bernardi, P. (2013). The mitochondrial permeability transition pore: a mystery solved? Front. Physiol. 4, 95. doi: 10.3389.
    • (2013) Front. Physiol. , vol.4 , pp. 95
    • Bernardi, P.1
  • 3
    • 84874640414 scopus 로고    scopus 로고
    • Role of the c subunit of the Fo ATP synthase in mitochondrial permeability transition
    • Bonora, M.; Bononi, A.; De Marchi, E.; Giorgi, C.; Lebiedzinska, M.; Marchi, S. et al (2013) Role of the c subunit of the Fo ATP synthase in mitochondrial permeability transition. Cell Cycle 12, 674-683
    • (2013) Cell Cycle , vol.12 , pp. 674-683
    • Bonora, M.1    Bononi, A.2    De Marchi, E.3    Giorgi, C.4    Lebiedzinska, M.5    Marchi, S.6
  • 4
    • 84897967621 scopus 로고    scopus 로고
    • Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition
    • Oncogene Epub ahead of print doi: 10.1038.
    • Bonora, M., Wieckowski, M.R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., and Pinton, P. (2014). Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition. Oncogene Epub ahead of print doi: 10.1038.
    • (2014)
    • Bonora, M.1    Wieckowski, M.R.2    Chinopoulos, C.3    Kepp, O.4    Kroemer, G.5    Galluzzi, L.6    Pinton, P.7
  • 5
    • 0030068505 scopus 로고    scopus 로고
    • Electrical currents associated with nucleotide transport by the reconstituted mitochondrial ADP/ATP carrier
    • Brustovetsky, N., Becker, A., Klingenberg, M., and Bamberg, E. (1996). Electrical currents associated with nucleotide transport by the reconstituted mitochondrial ADP/ATP carrier. Proc. Natl. Acad. Sci. USA 93, 664-668.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 664-668
    • Brustovetsky, N.1    Becker, A.2    Klingenberg, M.3    Bamberg, E.4
  • 6
    • 0036771787 scopus 로고    scopus 로고
    • A large Ca2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore
    • Brustovetsky, N., Tropschug, M., Heimpel, S., Heidkamper, D., and Klingenberg, M. (2002). A large Ca2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore. Biochemistry 41, 11804-11811.
    • (2002) Biochemistry , vol.41 , pp. 11804-11811
    • Brustovetsky, N.1    Tropschug, M.2    Heimpel, S.3    Heidkamper, D.4    Klingenberg, M.5
  • 7
    • 45549108453 scopus 로고    scopus 로고
    • Regulation of mitochondrial structure and function by the F1Fo-ATPase inhibitor protein, IF1
    • Campanella, M., Casswell, E., Chong, S., Farah, Z., Wieckowski, M.R., Abramov, A.Y. et al (2008). Regulation of mitochondrial structure and function by the F1Fo-ATPase inhibitor protein, IF1. Cell. Metab. 8, 13-25.
    • (2008) Cell. Metab. , vol.8 , pp. 13-25
    • Campanella, M.1    Casswell, E.2    Chong, S.3    Farah, Z.4    Wieckowski, M.R.5    Abramov, A.Y.6
  • 8
    • 85047687351 scopus 로고    scopus 로고
    • Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.
    • Carraro, M., Giorgio, V., Sileikyte, J., Sartori, G., Forte, M., Lippe, G., Zoratti, M. et al (2014). Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition. J. Biol. Chem. 289:15980-15985.
    • (2014) J. Biol. Chem. , vol.289 , pp. 15980-15985
    • Carraro, M.1    Giorgio, V.2    Sileikyte, J.3    Sartori, G.4    Forte, M.5    Lippe, G.6    Zoratti, M.7
  • 9
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen, C., Ko, Y., Delannoy, M., Ludtke, S.J., Chiu, W., and Pedersen, P.L. (2004). Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J. Biol. Chem. 279, 31761-31768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 10
    • 79952837890 scopus 로고    scopus 로고
    • Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels
    • Chinopoulos, C., Konrad, C., Kiss, G., Metelkin, E., Torocsik, B., Zhang, S.F. et al (2011). Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels. FEBS J. 278, 1112-1125.
    • (2011) FEBS J. , vol.278 , pp. 1112-1125
    • Chinopoulos, C.1    Konrad, C.2    Kiss, G.3    Metelkin, E.4    Torocsik, B.5    Zhang, S.F.6
  • 11
    • 71749098386 scopus 로고    scopus 로고
    • Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex
    • Giorgio, V., Bisetto, E., Soriano, M.E., Dabbeni-Sala, F., Basso, E., Petronilli, V. et al (2009). Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex. J. Biol. Chem. 284, 33982-33988.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33982-33988
    • Giorgio, V.1    Bisetto, E.2    Soriano, M.E.3    Dabbeni-Sala, F.4    Basso, E.5    Petronilli, V.6
  • 14
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • Halestrap, A.P. (2009). What is the mitochondrial permeability transition pore? J. Mol. Cell. Cardiol. 46, 821-831.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 15
    • 77955955395 scopus 로고    scopus 로고
    • A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection
    • Halestrap, A.P. (2010). A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection. Biochem. Soc. Trans. 38, 841-860.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 841-860
    • Halestrap, A.P.1
  • 16
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap, A.P., and Brenner, C. (2003). The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death. Curr. Med. Chem. 10, 1507-1525.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1507-1525
    • Halestrap, A.P.1    Brenner, C.2
  • 17
    • 84904608695 scopus 로고    scopus 로고
    • Identifying the components of the elusive mitochondrial permeability transition pore
    • Karch, J., and Molkentin, J.D. (2014). Identifying the components of the elusive mitochondrial permeability transition pore. Proc. Natl. Acad. Sci. USA 111, 10396-10397.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 10396-10397
    • Karch, J.1    Molkentin, J.D.2
  • 18
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka, J.E., Waymire, K.G., Levy, S.E., Sligh, J.E., Cal, J.Y., Jones, D.P. et al. (2004). The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427, 461-465.
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3    Sligh, J.E.4    Cal, J.Y.5    Jones, D.P.6
  • 19
    • 84905042938 scopus 로고    scopus 로고
    • Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy
    • Kwong, J.Q., Davis, J., Baines, C.P., Sargent, M.A., Karch, J., Wang, X. et al (2014). Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy. Cell. Death. Differ. 21:1209-1217.
    • (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
  • 20
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • Leung, A.W.C., Varanyuwatana, P., and Halestrap, A.P. (2008). The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition. J. Biol. Chem. 283, 26312-26323. Varanyuwatana, P., and Halestrap, A.P. (2012). The roles of phosphate and the mitochondrial phosphate carrier in the mechanism of the permeability transition. Mitochondrion 12, 120-125.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26312-26323
    • Leung, A.W.C.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 21
    • 84856526180 scopus 로고    scopus 로고
    • The roles of phosphate and the mitochondrial phosphate carrier in the mechanism of the permeability transition
    • Varanyuwatana, P., and Halestrap, A.P. (2012). The roles of phosphate and the mitochondrial phosphate carrier in the mechanism of the permeability transition. Mitochondrion 12, 120-125
    • (2012) Mitochondrion , vol.12 , pp. 120-125
    • Varanyuwatana, P.1    Halestrap, A.P.2
  • 22
    • 77952675154 scopus 로고    scopus 로고
    • Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore
    • Zoratti, M., De Marchi, U., Biasutto, L., and Szabo, I. (2010). Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore. FEBS Lett. 584, 1997-2004.
    • (2010) FEBS Lett. , vol.584 , pp. 1997-2004
    • Zoratti, M.1    De Marchi, U.2    Biasutto, L.3    Szabo, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.