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Volumn 212, Issue 2, 2016, Pages 157-166

Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MITOCHONDRIAL DNA; OMA1 PROTEIN; OPA1 PROTEIN; UNCLASSIFIED DRUG; METALLOPROTEINASE; MITOCHONDRIAL PROTEIN; OMA1 PROTEIN, MOUSE; OPA1 PROTEIN (GTPASE), MOUSE; PROHIBITIN; REPRESSOR PROTEIN;

EID: 84959453982     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201507022     Document Type: Article
Times cited : (115)

References (50)
  • 1
    • 45249104409 scopus 로고    scopus 로고
    • Characterization of OPA1 isoforms isolated from mouse tissues
    • Akepati, V.R., E.C. Müller, A. Otto, H.M. Strauss, M. Portwich, and C. Alexander. 2008. Characterization of OPA1 isoforms isolated from mouse tissues. J. Neurochem. 106:372-383. http://dx.doi.org/10.1111/j.1471-4159.2008.05401.x
    • (2008) J. Neurochem. , vol.106 , pp. 372-383
    • Akepati, V.R.1    Müller, E.C.2    Otto, A.3    Strauss, H.M.4    Portwich, M.5    Alexander, C.6
  • 3
    • 84896264348 scopus 로고    scopus 로고
    • The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
    • Anand, R., T. Wai, M.J. Baker, N. Kladt, A.C. Schauss, E. Rugarli, and T. Langer. 2014. The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission. J. Cell Biol. 204:919-929. http://dx.doi.org/10.1083/jcb.201308006
    • (2014) J. Cell Biol. , vol.204 , pp. 919-929
    • Anand, R.1    Wai, T.2    Baker, M.J.3    Kladt, N.4    Schauss, A.C.5    Rugarli, E.6    Langer, T.7
  • 4
    • 84898603457 scopus 로고    scopus 로고
    • Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics
    • Baker, M.J., P.A. Lampe, D. Stojanovski, A. Korwitz, R. Anand, T. Tatsuta, and T. Langer. 2014. Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics. EMBO J. 33:578-593. http://dx.doi.org/10.1002/embj.201386474
    • (2014) EMBO J. , vol.33 , pp. 578-593
    • Baker, M.J.1    Lampe, P.A.2    Stojanovski, D.3    Korwitz, A.4    Anand, R.5    Tatsuta, T.6    Langer, T.7
  • 5
    • 84926258887 scopus 로고    scopus 로고
    • Disturbed mitochondrial dynamics and neurodegenerative disorders
    • Burté, F., V. Carelli, P.F. Chinnery, and P. Yu-Wai-Man. 2015. Disturbed mitochondrial dynamics and neurodegenerative disorders. Nat. Rev. Neurol. 11:11-24. http://dx.doi.org/10.1038/nrneurol.2014.228
    • (2015) Nat. Rev. Neurol. , vol.11 , pp. 11-24
    • Burté, F.1    Carelli, V.2    Chinnery, P.F.3    Yu-Wai-Man, P.4
  • 8
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S., T. Rudka, D. Hartmann, V. Costa, L. Serneels, K. Craessaerts, K. Metzger, C. Frezza, W. Annaert, L. D'Adamio, et al. 2006. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell. 126:163-175. http://dx.doi.org/10.1016/j.cell.2006.06.021
    • (2006) Cell. , vol.126 , pp. 163-175
    • Cipolat, S.1    Rudka, T.2    Hartmann, D.3    Costa, V.4    Serneels, L.5    Craessaerts, K.6    Metzger, K.7    Frezza, C.8    Annaert, W.9    D'Adamio, L.10
  • 10
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs, J.T., and S. Strack. 2007. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8:939-944. http://dx.doi.org/10.1038/sj.embor.7401062
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 11
    • 84924917575 scopus 로고    scopus 로고
    • C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization
    • Desmurs, M., M. Foti, E. Raemy, F.M. Vaz, J.C. Martinou, A. Bairoch, and L. Lane. 2015. C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization. Mol. Cell. Biol. 35:1139-1156. http://dx.doi.org/10.1128/MCB.01047-14
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 1139-1156
    • Desmurs, M.1    Foti, M.2    Raemy, E.3    Vaz, F.M.4    Martinou, J.C.5    Bairoch, A.6    Lane, L.7
  • 14
    • 84892600839 scopus 로고    scopus 로고
    • Mitochondrial form and function
    • Friedman, J.R., and J. Nunnari. 2014. Mitochondrial form and function. Nature. 505:335-343. http://dx.doi.org/10.1038/nature12985
    • (2014) Nature. , vol.505 , pp. 335-343
    • Friedman, J.R.1    Nunnari, J.2
  • 15
    • 34548313686 scopus 로고    scopus 로고
    • Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
    • Griparic, L., T. Kanazawa, and A.M. van der Bliek. 2007. Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. J. Cell Biol. 178:757-764. http://dx.doi.org/10.1083/jcb.200704112
    • (2007) J. Cell Biol. , vol.178 , pp. 757-764
    • Griparic, L.1    Kanazawa, T.2    van der Bliek, A.M.3
  • 17
    • 76149093590 scopus 로고    scopus 로고
    • Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
    • Head, B., L. Griparic, M. Amiri, S. Gandre-Babbe, and A.M. van der Bliek. 2009. Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J. Cell Biol. 187:959-966. http://dx.doi.org/10.1083/jcb.200906083
    • (2009) J. Cell Biol. , vol.187 , pp. 959-966
    • Head, B.1    Griparic, L.2    Amiri, M.3    Gandre-Babbe, S.4    van der Bliek, A.M.5
  • 18
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara, N., Y. Fujita, T. Oka, and K. Mihara. 2006. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25:2966-2977. http://dx.doi.org/10.1038/sj.emboj.7601184
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 19
    • 84907919478 scopus 로고    scopus 로고
    • Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis
    • Jiang, X., H. Jiang, Z. Shen, and X. Wang. 2014. Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis. Proc. Natl. Acad. Sci. USA. 111:14782-14787. http://dx.doi.org/10.1073/pnas.1417253111
    • (2014) Proc. Natl. Acad. Sci. USA. , vol.111 , pp. 14782-14787
    • Jiang, X.1    Jiang, H.2    Shen, Z.3    Wang, X.4
  • 20
    • 39549085742 scopus 로고    scopus 로고
    • Human prohibitin 1 maintains the organization and stability of the mitochondrial nucleoids
    • Kasashima, K., M. Sumitani, M. Satoh, and H. Endo. 2008. Human prohibitin 1 maintains the organization and stability of the mitochondrial nucleoids. Exp. Cell Res. 314:988-996. http://dx.doi.org/10.1016/j.yexcr.2008.01.005
    • (2008) Exp. Cell Res. , vol.314 , pp. 988-996
    • Kasashima, K.1    Sumitani, M.2    Satoh, M.3    Endo, H.4
  • 21
    • 80052827401 scopus 로고    scopus 로고
    • Inflammation in the early stages of neurodegenerative pathology
    • Khandelwal, P.J., A.M. Herman, and C.E. Moussa. 2011. Inflammation in the early stages of neurodegenerative pathology. J. Neuroimmunol. 238:1-11. http://dx.doi.org/10.1016/j.jneuroim.2011.07.002
    • (2011) J. Neuroimmunol. , vol.238 , pp. 1-11
    • Khandelwal, P.J.1    Herman, A.M.2    Moussa, C.E.3
  • 22
    • 33749991592 scopus 로고    scopus 로고
    • Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1
    • Meeusen, S., R. DeVay, J. Block, A. Cassidy-Stone, S. Wayson, J.M. McCaffery, and J. Nunnari. 2006. Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1. Cell. 127:383-395. http://dx.doi.org/10.1016/j.cell.2006.09.021
    • (2006) Cell. , vol.127 , pp. 383-395
    • Meeusen, S.1    DeVay, R.2    Block, J.3    Cassidy-Stone, A.4    Wayson, S.5    McCaffery, J.M.6    Nunnari, J.7
  • 24
    • 84870679012 scopus 로고    scopus 로고
    • Loss of prohibitin membrane scaffolds impairs mitochondrial architecture and leads to tau hyperphosphorylation and neurodegeneration
    • Merkwirth, C., P. Martinelli, A. Korwitz, M. Morbin, H.S. Brönneke, S.D. Jordan, E.I. Rugarli, and T. Langer. 2012. Loss of prohibitin membrane scaffolds impairs mitochondrial architecture and leads to tau hyperphosphorylation and neurodegeneration. PLoS Genet. 8:e1003021. http://dx.doi.org/10.1371/journal.pgen.1003021
    • (2012) PLoS Genet. , vol.8 , pp. e1003021
    • Merkwirth, C.1    Martinelli, P.2    Korwitz, A.3    Morbin, M.4    Brönneke, H.S.5    Jordan, S.D.6    Rugarli, E.I.7    Langer, T.8
  • 25
    • 84893127504 scopus 로고    scopus 로고
    • Mitochondria: a kinase anchoring protein 1, a signaling platform for mitochondrial form and function
    • Merrill, R.A., and S. Strack. 2014. Mitochondria: a kinase anchoring protein 1, a signaling platform for mitochondrial form and function. Int. J. Biochem. Cell Biol. 48:92-96. http://dx.doi.org/10.1016/j.biocel.2013.12.012
    • (2014) Int. J. Biochem. Cell Biol. , vol.48 , pp. 92-96
    • Merrill, R.A.1    Strack, S.2
  • 26
    • 84910141948 scopus 로고    scopus 로고
    • Mitochondrial dynamics and inheritance during cell division, development and disease
    • Mishra, P., and D.C. Chan. 2014. Mitochondrial dynamics and inheritance during cell division, development and disease. Nat. Rev. Mol. Cell Biol. 15:634-646. http://dx.doi.org/10.1038/nrm3877
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 634-646
    • Mishra, P.1    Chan, D.C.2
  • 27
    • 84897538678 scopus 로고    scopus 로고
    • Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation
    • Mishra, P., V. Carelli, G. Manfredi, and D.C. Chan. 2014. Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation. Cell Metab. 19:630-641. http://dx.doi.org/10.1016/j.cmet.2014.03.011
    • (2014) Cell Metab. , vol.19 , pp. 630-641
    • Mishra, P.1    Carelli, V.2    Manfredi, G.3    Chan, D.C.4
  • 29
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon, A., L. Baricault, N. Gas, E. Guillou, A. Valette, P. Belenguer, and G. Lenaers. 2003. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278:7743-7746. http://dx.doi.org/10.1074/jbc.C200677200
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 30
    • 84879858842 scopus 로고    scopus 로고
    • Mitochondrial dynamics in cardiovascular health and disease
    • Ong, S.B., A.R. Hall, and D.J. Hausenloy. 2013. Mitochondrial dynamics in cardiovascular health and disease. Antioxid. Redox Signal. 19:400-414. http://dx.doi.org/10.1089/ars.2012.4777
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 400-414
    • Ong, S.B.1    Hall, A.R.2    Hausenloy, D.J.3
  • 31
    • 70450265196 scopus 로고    scopus 로고
    • Prohibitins and the functional compartmentalization of mitochondrial membranes
    • Osman, C., C. Merkwirth, and T. Langer. 2009. Prohibitins and the functional compartmentalization of mitochondrial membranes. J. Cell Sci. 122:3823-3830. http://dx.doi.org/10.1242/jcs.037655
    • (2009) J. Cell Sci. , vol.122 , pp. 3823-3830
    • Osman, C.1    Merkwirth, C.2    Langer, T.3
  • 32
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman, C., D.R. Voelker, and T. Langer. 2011. Making heads or tails of phospholipids in mitochondria. J. Cell Biol. 192:7-16. http://dx.doi.org/10.1083/jcb.201006159
    • (2011) J. Cell Biol. , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 37
    • 84930040430 scopus 로고    scopus 로고
    • New roles for mitochondrial proteases in health, ageing and disease
    • Quirós, P.M., T. Langer, and C. López-Otín. 2015. New roles for mitochondrial proteases in health, ageing and disease. Nat. Rev. Mol. Cell Biol. 16:345-359. http://dx.doi.org/10.1038/nrm3984
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 345-359
    • Quirós, P.M.1    Langer, T.2    López-Otín, C.3
  • 38
    • 84904037057 scopus 로고    scopus 로고
    • DNA JC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling
    • Richter-Dennerlein, R., A. Korwitz, M. Haag, T. Tatsuta, S. Dargazanli, M. Baker, T. Decker, T. Lamkemeyer, E.I. Rugarli, and T. Langer. 2014. DNA JC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling. Cell Metab. 20:158-171. http://dx.doi.org/10.1016/j.cmet.2014.04.016
    • (2014) Cell Metab. , vol.20 , pp. 158-171
    • Richter-Dennerlein, R.1    Korwitz, A.2    Haag, M.3    Tatsuta, T.4    Dargazanli, S.5    Baker, M.6    Decker, T.7    Lamkemeyer, T.8    Rugarli, E.I.9    Langer, T.10
  • 39
    • 84922988247 scopus 로고    scopus 로고
    • Mitochondrial division and fusion in metabolism
    • Roy, M., P.H. Reddy, M. Iijima, and H. Sesaki. 2015. Mitochondrial division and fusion in metabolism. Curr. Opin. Cell Biol. 33:111-118. http://dx.doi.org/10.1016/j.ceb.2015.02.001
    • (2015) Curr. Opin. Cell Biol. , vol.33 , pp. 111-118
    • Roy, M.1    Reddy, P.H.2    Iijima, M.3    Sesaki, H.4
  • 40
    • 84873167935 scopus 로고    scopus 로고
    • Cardiolipin remodeling and the function of tafazzin
    • Schlame, M. 2013. Cardiolipin remodeling and the function of tafazzin. Biochim. Biophys. Acta. 1831:582-588. http://dx.doi.org/10.1016/j.bbalip.2012.11.007
    • (2013) Biochim. Biophys. Acta. , vol.1831 , pp. 582-588
    • Schlame, M.1
  • 42
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • Song, Z., H. Chen, M. Fiket, C. Alexander, and D.C. Chan. 2007. OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 178:749-755. http://dx.doi.org/10.1083/jcb.200704110
    • (2007) J. Cell Biol. , vol.178 , pp. 749-755
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4    Chan, D.C.5
  • 43
    • 84858411560 scopus 로고    scopus 로고
    • YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation
    • Stiburek, L., J. Cesnekova, O. Kostkova, D. Fornuskova, K. Vinsova, L. Wenchich, J. Houstek, and J. Zeman. 2012. YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation. Mol. Biol. Cell. 23:1010-1023. http://dx.doi.org/10.1091/mbc. E11-08-0674
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 1010-1023
    • Stiburek, L.1    Cesnekova, J.2    Kostkova, O.3    Fornuskova, D.4    Vinsova, K.5    Wenchich, L.6    Houstek, J.7    Zeman, J.8
  • 44
    • 11144336620 scopus 로고    scopus 로고
    • Formation of membrane-bound ring complexes by prohibitins in mitochondria
    • Tatsuta, T., K. Model, and T. Langer. 2005. Formation of membrane-bound ring complexes by prohibitins in mitochondria. Mol. Biol. Cell. 16:248-259. http://dx.doi.org/10.1091/mbc. E04-09-0807
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 248-259
    • Tatsuta, T.1    Model, K.2    Langer, T.3
  • 47
    • 84901712100 scopus 로고    scopus 로고
    • OMA1 mediates OPA1 proteolysis and mitochondrial fragmentation in experimental models of ischemic kidney injury
    • Xiao, X., Y. Hu, P.M. Quirós, Q. Wei, C. López-Otín, and Z. Dong. 2014. OMA1 mediates OPA1 proteolysis and mitochondrial fragmentation in experimental models of ischemic kidney injury. Am. J. Physiol. Renal Physiol. 306:F1318-F1326. http://dx.doi.org/10.1152/ajprenal.00036.2014
    • (2014) Am. J. Physiol. Renal Physiol. , vol.306 , pp. F1318-F1326
    • Xiao, X.1    Hu, Y.2    Quirós, P.M.3    Wei, Q.4    López-Otín, C.5    Dong, Z.6
  • 48
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle, R.J., and A.M. van der Bliek. 2012. Mitochondrial fission, fusion, and stress. Science. 337:1062-1065. http://dx.doi.org/10.1126/science.1219855
    • (2012) Science. , vol.337 , pp. 1062-1065
    • Youle, R.J.1    van der Bliek, A.M.2
  • 49
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto, E., L. Vergani, and F. Dabbeni-Sala. 1997. Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis. 18:2059-2064. http://dx.doi.org/10.1002/elps.1150181131
    • (1997) Electrophoresis. , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Vergani, L.2    Dabbeni-Sala, F.3
  • 50
    • 84899844027 scopus 로고    scopus 로고
    • Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self-cleavage
    • Zhang, K., H. Li, and Z. Song. 2014. Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self-cleavage. EMBO Rep. 15:576-585. http://dx.doi.org/10.1002/embr.201338240
    • (2014) EMBO Rep. , vol.15 , pp. 576-585
    • Zhang, K.1    Li, H.2    Song, Z.3


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