메뉴 건너뛰기




Volumn 16, Issue 6, 2015, Pages 345-359

New roles for mitochondrial proteases in health, ageing and disease

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; MITOCHONDRIAL PROTEIN; PEPTIDE HYDROLASE; TUMOR PROTEIN;

EID: 84930040430     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3984     Document Type: Article
Times cited : (419)

References (182)
  • 1
    • 84859366447 scopus 로고    scopus 로고
    • Protease signalling: The cutting edge
    • Turk, B., Turk, D. & Turk, V. Protease signalling: the cutting edge. EMBO J. 31, 1630-1643 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1630-1643
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 2
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • Lopez-Otin, C. & Bond, J. S. Proteases: multifunctional enzymes in life and disease. J. Biol. Chem. 283, 30433-30437 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 30433-30437
    • Lopez-Otin, C.1    Bond, J.S.2
  • 3
    • 77950012622 scopus 로고    scopus 로고
    • The regulatory crosstalk between kinases and proteases in cancer
    • Lopez-Otin, C. & Hunter, T. The regulatory crosstalk between kinases and proteases in cancer. Nature Rev. Cancer 10, 278-292 (2010).
    • (2010) Nature Rev. Cancer , vol.10 , pp. 278-292
    • Lopez-Otin, C.1    Hunter, T.2
  • 4
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: Versatile activities of AAA proteases and other peptidases
    • Koppen, M. & Langer, T. Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit. Rev. Biochem. Mol. Biol. 42, 221-242 (2007).
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 5
    • 84871821553 scopus 로고    scopus 로고
    • Proteolytic control of mitochondrial function and morphogenesis
    • Anand, R., Langer, T. & Baker, M. J. Proteolytic control of mitochondrial function and morphogenesis. Biochim. Biophys. Acta 1833, 195-204 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 195-204
    • Anand, R.1    Langer, T.2    Baker, M.J.3
  • 6
    • 84858791998 scopus 로고    scopus 로고
    • Mitochondrial quality control: A matter of life and death for neurons
    • Rugarli, E. I. & Langer, T. Mitochondrial quality control: a matter of life and death for neurons. EMBO J. 31, 1336-1349 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1336-1349
    • Rugarli, E.I.1    Langer, T.2
  • 7
    • 84901494659 scopus 로고    scopus 로고
    • Mitochondrial matrix proteases as novel therapeutic targets in malignancy
    • Goard, C. A. & Schimmer, A. D. Mitochondrial matrix proteases as novel therapeutic targets in malignancy. Oncogene 33, 2690-2699 (2014).
    • (2014) Oncogene , vol.33 , pp. 2690-2699
    • Goard, C.A.1    Schimmer, A.D.2
  • 8
    • 79955593116 scopus 로고    scopus 로고
    • Mitochondrial proteases and cancer
    • Bulteau, A. L. & Bayot, A. Mitochondrial proteases and cancer. Biochim. Biophys. Acta 1807, 595-601 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 595-601
    • Bulteau, A.L.1    Bayot, A.2
  • 11
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Waller, M., Barrett, A. J. & Bateman, A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 42, D503-D509 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 12
    • 46349103594 scopus 로고    scopus 로고
    • A mitochondrial protein compendium elucidates complex i disease biology
    • Pagliarini, D. J. et al. A mitochondrial protein compendium elucidates complex I disease biology. Cell 134, 112-123 (2008).
    • (2008) Cell , vol.134 , pp. 112-123
    • Pagliarini, D.J.1
  • 13
    • 0035878402 scopus 로고    scopus 로고
    • Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein
    • Kremmidiotis, G. et al. Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein. Genomics 76, 58-65 (2001).
    • (2001) Genomics , vol.76 , pp. 58-65
    • Kremmidiotis, G.1
  • 14
    • 84871793725 scopus 로고    scopus 로고
    • Chaperone-protease networks in mitochondrial protein homeostasis
    • Voos, W. Chaperone-protease networks in mitochondrial protein homeostasis. Biochim. Biophys. Acta 1833, 388-399 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 388-399
    • Voos, W.1
  • 15
    • 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. Nature Rev. Mol. Cell Biol. 11, 655-667 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 17
    • 84871796609 scopus 로고    scopus 로고
    • Processing peptidases in mitochondria and chloroplasts
    • Teixeira, P. F. & Glaser, E. Processing peptidases in mitochondria and chloroplasts. Biochim. Biophys. Acta 1833, 360-370 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 360-370
    • Teixeira, P.F.1    Glaser, E.2
  • 18
    • 77649269949 scopus 로고    scopus 로고
    • Glycine-rich loop of mitochondrial processing peptidase a-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20
    • Dvorakova-Hola, K. et al. Glycine-rich loop of mitochondrial processing peptidase a-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20. J. Mol. Biol. 396, 1197-1210 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 1197-1210
    • Dvorakova-Hola, K.1
  • 19
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari, J., Fox, T. D. & Walter, P. A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262, 1997-2004 (1993).
    • (1993) Science , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 20
    • 84889592795 scopus 로고    scopus 로고
    • Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-Terminal targeting sequence
    • Ieva, R. et al. Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-Terminal targeting sequence. Nature Commun. 4, 2853 (2013).
    • (2013) Nature Commun. , vol.4 , Issue.2853
    • Ieva, R.1
  • 21
    • 79959871792 scopus 로고    scopus 로고
    • Mitochondrial protein turnover: Role of the precursor intermediate peptidase Oct1 in protein stabilization
    • Vogtle, F. N. et al. Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization. Mol. Biol. Cell 22, 2135-2143 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2135-2143
    • Vogtle, F.N.1
  • 22
    • 70349840621 scopus 로고    scopus 로고
    • Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
    • Vogtle, F. N. et al. Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell 139, 428-439 (2009).
    • (2009) Cell , vol.139 , pp. 428-439
    • Vogtle, F.N.1
  • 23
    • 0347993051 scopus 로고    scopus 로고
    • An unusual peptide deformylase features in the human mitochondrial N-Terminal methionine excision pathway
    • Serero, A., Giglione, C., Sardini, A., Martinez-Sanz, J. & Meinnel, T. An unusual peptide deformylase features in the human mitochondrial N-Terminal methionine excision pathway. J. Biol. Chem. 278, 52953-52963 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 52953-52963
    • Serero, A.1    Giglione, C.2    Sardini, A.3    Martinez-Sanz, J.4    Meinnel, T.5
  • 24
    • 84855240784 scopus 로고    scopus 로고
    • Mitochondrial AAA proteases-Towards a molecular understanding of membrane-bound proteolytic machines
    • Gerdes, F., Tatsuta, T. & Langer, T. Mitochondrial AAA proteases-Towards a molecular understanding of membrane-bound proteolytic machines. Biochim. Biophys. Acta 1823, 49-55 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 49-55
    • Gerdes, F.1    Tatsuta, T.2    Langer, T.3
  • 25
    • 33846127778 scopus 로고    scopus 로고
    • Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia
    • Koppen, M., Metodiev, M. D., Casari, G., Rugarli, E. I. & Langer, T. Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia. Mol. Cell. Biol. 27, 758-767 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 758-767
    • Koppen, M.1    Metodiev, M.D.2    Casari, G.3    Rugarli, E.I.4    Langer, T.5
  • 26
    • 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. et al. 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 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1010-1023
    • Stiburek, L.1
  • 27
    • 84858001999 scopus 로고    scopus 로고
    • Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assembly
    • Hornig-Do, H. T. et al. Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assembly. EMBO J. 31, 1293-1307 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1293-1307
    • Hornig-Do, H.T.1
  • 28
    • 84865073903 scopus 로고    scopus 로고
    • Early complex i assembly defects result in rapid turnover of the ND1 subunit
    • Zurita Rendon, O. & Shoubridge, E. A. Early complex I assembly defects result in rapid turnover of the ND1 subunit. Hum. Mol. Genet. 21, 3815-3824 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3815-3824
    • Zurita Rendon, O.1    Shoubridge, E.A.2
  • 29
    • 0037434941 scopus 로고    scopus 로고
    • The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
    • Lu, B. et al. The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals. Gene 306, 45-55 (2003).
    • (2003) Gene , vol.306 , pp. 45-55
    • Lu, B.1
  • 30
    • 84855225838 scopus 로고    scopus 로고
    • Multitasking in the mitochondrion by the ATP-dependent Lon protease
    • Venkatesh, S., Lee, J., Singh, K., Lee, I. & Suzuki, C. K. Multitasking in the mitochondrion by the ATP-dependent Lon protease. Biochim. Biophys. Acta 1823, 56-66 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 56-66
    • Venkatesh, S.1    Lee, J.2    Singh, K.3    Lee, I.4    Suzuki, C.K.5
  • 31
    • 84881101982 scopus 로고    scopus 로고
    • Oxygen-sensitive mitochondrial accumulation of cystathionine b-synthase mediated by Lon protease
    • Teng, H. et al. Oxygen-sensitive mitochondrial accumulation of cystathionine b-synthase mediated by Lon protease. Proc. Natl Acad. Sci. USA 110, 12679-12684 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 12679-12684
    • Teng, H.1
  • 32
    • 84901044652 scopus 로고    scopus 로고
    • Mitochondrial matrix proteostasis is linked to hereditary paraganglioma: LON-mediated turnover of the human flavinylation factor SDH5 is regulated by its interaction with SDHA
    • Bezawork-Geleta, A., Saiyed, T., Dougan, D. A. & Truscott, K. N. Mitochondrial matrix proteostasis is linked to hereditary paraganglioma: LON-mediated turnover of the human flavinylation factor SDH5 is regulated by its interaction with SDHA. FASEB J. 28, 1794-1804 (2014).
    • (2014) FASEB J. , vol.28 , pp. 1794-1804
    • Bezawork-Geleta, A.1    Saiyed, T.2    Dougan, D.A.3    Truscott, K.N.4
  • 33
    • 84861561418 scopus 로고    scopus 로고
    • Diphenylarsinic acid promotes degradation of glutaminase C by mitochondrial Lon protease
    • Kita, K., Suzuki, T. & Ochi, T. Diphenylarsinic acid promotes degradation of glutaminase C by mitochondrial Lon protease. J. Biol. Chem. 287, 18163-18172 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 18163-18172
    • Kita, K.1    Suzuki, T.2    Ochi, T.3
  • 34
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda, R. et al. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell 129, 111-122 (2007).
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1
  • 35
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota, D. A. & Davies, K. J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nature Cell Biol. 4, 674-680 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 36
    • 34548446023 scopus 로고    scopus 로고
    • Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: The unexpected effect of proteasome inhibitors
    • Granot, Z. et al. Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors. Mol. Endocrinol. 21, 2164-2177 (2007).
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2164-2177
    • Granot, Z.1
  • 37
    • 79960659551 scopus 로고    scopus 로고
    • Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-Aminolevulinic acid synthase protein by heme in human liver cells
    • Tian, Q. et al. Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-Aminolevulinic acid synthase protein by heme in human liver cells. J. Biol. Chem. 286, 26424-26430 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 26424-26430
    • Tian, Q.1
  • 38
    • 78649842154 scopus 로고    scopus 로고
    • Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)
    • Matsushima, Y., Goto, Y. & Kaguni, L. S. Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM). Proc. Natl Acad. Sci. USA 107, 18410-18415 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18410-18415
    • Matsushima, Y.1    Goto, Y.2    Kaguni, L.S.3
  • 39
    • 84904795370 scopus 로고    scopus 로고
    • ATP-dependent Lon protease controls tumor bioenergetics by reprogramming mitochondrial activity
    • Quiros, P. M. et al. ATP-dependent Lon protease controls tumor bioenergetics by reprogramming mitochondrial activity. Cell Rep. 8, 542-556 (2014).
    • (2014) Cell Rep. , vol.8 , pp. 542-556
    • Quiros, P.M.1
  • 40
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C elegans
    • Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y. & Ron, D. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 13, 467-480 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 41
    • 84888196854 scopus 로고    scopus 로고
    • Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors
    • Gispert, S. et al. Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors. Hum. Mol. Genet. 22, 4871-4887 (2013).
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4871-4887
    • Gispert, S.1
  • 42
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants
    • Stahl, A. et al. Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. J. Biol. Chem. 277, 41931-41939 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 41931-41939
    • Stahl, A.1
  • 43
    • 21244505013 scopus 로고    scopus 로고
    • Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria
    • Kambacheld, M., Augustin, S., Tatsuta, T., Muller, S. & Langer, T. Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J. Biol. Chem. 280, 20132-20139 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 20132-20139
    • Kambacheld, M.1    Augustin, S.2    Tatsuta, T.3    Muller, S.4    Langer, T.5
  • 44
    • 84907990407 scopus 로고    scopus 로고
    • Amyloid-b peptide induces mitochondrial dysfunction by inhibition of preprotein maturation
    • Mossmann, D. et al. Amyloid-b peptide induces mitochondrial dysfunction by inhibition of preprotein maturation. Cell Metab. 20, 662-669 (2014).
    • (2014) Cell Metab. , vol.20 , pp. 662-669
    • Mossmann, D.1
  • 45
    • 33749391917 scopus 로고    scopus 로고
    • Degradation of the amyloid b-protein by the novel mitochondrial peptidasome, PreP
    • Falkevall, A. et al. Degradation of the amyloid b-protein by the novel mitochondrial peptidasome, PreP. J. Biol. Chem. 281, 29096-29104 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 29096-29104
    • Falkevall, A.1
  • 46
    • 0028897489 scopus 로고
    • Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase
    • Serizawa, A., Dando, P. M. & Barrett, A. J. Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase. J. Biol. Chem. 270, 2092-2098 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2092-2098
    • Serizawa, A.1    Dando, P.M.2    Barrett, A.J.3
  • 47
  • 48
    • 84863455932 scopus 로고    scopus 로고
    • HtrA2 deficiency causes mitochondrial uncoupling through the F1F0-ATP synthase and consequent ATP depletion
    • Plun-Favreau, H. et al. HtrA2 deficiency causes mitochondrial uncoupling through the F1F0-ATP synthase and consequent ATP depletion. Cell Death Dis. 3, e335 (2012).
    • (2012) Cell Death Dis. , vol.3 , pp. e335
    • Plun-Favreau, H.1
  • 49
    • 33846826875 scopus 로고    scopus 로고
    • Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1F0-ATP synthase
    • Osman, C., Wilmes, C., Tatsuta, T. & Langer, T. Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1F0-ATP synthase. Mol. Biol. Cell 18, 627-635 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 627-635
    • Osman, C.1    Wilmes, C.2    Tatsuta, T.3    Langer, T.4
  • 50
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • Potting, C., Wilmes, C., Engmann, T., Osman, C. & Langer, T. Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 29, 2888-2898 (2010).
    • (2010) EMBO J. , vol.29 , pp. 2888-2898
    • Potting, C.1    Wilmes, C.2    Engmann, T.3    Osman, C.4    Langer, T.5
  • 51
    • 84868628376 scopus 로고    scopus 로고
    • AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival
    • Almajan, E. R. et al. AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival. J. Clin. Invest. 122, 4048-4058 (2012).
    • (2012) J. Clin. Invest. , vol.122 , pp. 4048-4058
    • Almajan, E.R.1
  • 52
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden, M. et al. The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123, 277-289 (2005).
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1
  • 53
    • 84920438196 scopus 로고    scopus 로고
    • Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model
    • Maltecca, F. et al. Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model. J. Clin. Invest. 125, 263-274 (2015).
    • (2015) J. Clin. Invest. , vol.125 , pp. 263-274
    • Maltecca, F.1
  • 54
    • 84889652177 scopus 로고    scopus 로고
    • Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation
    • Rainbolt, T. K., Atanassova, N., Genereux, J. C. & Wiseman, R. L. Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation. Cell Metab. 18, 908-919 (2013).
    • (2013) Cell Metab. , vol.18 , pp. 908-919
    • Rainbolt, T.K.1    Atanassova, N.2    Genereux, J.C.3    Wiseman, R.L.4
  • 55
    • 84881326056 scopus 로고    scopus 로고
    • TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid
    • Potting, C. et al. TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid. Cell Metab. 18, 287-295 (2013).
    • (2013) Cell Metab. , vol.18 , pp. 287-295
    • Potting, C.1
  • 56
    • 84872271398 scopus 로고    scopus 로고
    • Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
    • Lu, B. et al. Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease. Mol. Cell 49, 121-132 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 121-132
    • Lu, B.1
  • 57
    • 1842690145 scopus 로고    scopus 로고
    • DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrate
    • Liu, T. et al. DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrate. J. Biol. Chem. 279, 13902-13910 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 13902-13910
    • Liu, T.1
  • 58
    • 84877796195 scopus 로고    scopus 로고
    • HtrA2/Omi deficiency causes damage and mutation of mitochondrial DNA
    • Goo, H. G., Jung, M. K., Han, S. S., Rhim, H. & Kang, S. HtrA2/Omi deficiency causes damage and mutation of mitochondrial DNA. Biochim. Biophys. Acta 1833, 1866-1875 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1866-1875
    • Goo, H.G.1    Jung, M.K.2    Han, S.S.3    Rhim, H.4    Kang, S.5
  • 59
    • 70350132871 scopus 로고    scopus 로고
    • Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein, is essential for mitochondrial genome maintenance
    • Oberto, J. et al. Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein, is essential for mitochondrial genome maintenance. Nucleic Acids Res. 37, 5343-5352 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5343-5352
    • Oberto, J.1
  • 60
    • 73149117556 scopus 로고    scopus 로고
    • LACTB is a filament-forming protein localized in mitochondria
    • Polianskyte, Z. et al. LACTB is a filament-forming protein localized in mitochondria. Proc. Natl Acad. Sci. USA 106, 18960-18965 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18960-18965
    • Polianskyte, Z.1
  • 61
    • 84878138385 scopus 로고    scopus 로고
    • Mitonuclear protein imbalance as a conserved longevity mechanism
    • Houtkooper, R. H. et al. Mitonuclear protein imbalance as a conserved longevity mechanism. Nature 497, 451-457 (2013).
    • (2013) Nature , vol.497 , pp. 451-457
    • Houtkooper, R.H.1
  • 62
    • 84875968253 scopus 로고    scopus 로고
    • Surveillance-Activated defenses block the ROS-induced mitochondrial unfolded protein response
    • Runkel, E. D., Liu, S., Baumeister, R. & Schulze, E. Surveillance-Activated defenses block the ROS-induced mitochondrial unfolded protein response. PLoS Genet. 9, e1003346 (2013).
    • (2013) PLoS Genet. , vol.9 , pp. e1003346
    • Runkel, E.D.1    Liu, S.2    Baumeister, R.3    Schulze, E.4
  • 63
    • 0037009521 scopus 로고    scopus 로고
    • A mitochondrial specific stress response in mammalian cells
    • Zhao, Q. et al. A mitochondrial specific stress response in mammalian cells. EMBO J. 21, 4411-4419 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4411-4419
    • Zhao, Q.1
  • 64
    • 84896499806 scopus 로고    scopus 로고
    • The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease
    • Jovaisaite, V., Mouchiroud, L. & Auwerx, J. The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease. J. Exp. Biol. 217, 137-143 (2014).
    • (2014) J. Exp. Biol. , vol.217 , pp. 137-143
    • Jovaisaite, V.1    Mouchiroud, L.2    Auwerx, J.3
  • 65
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M. & Haynes, C. M. 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
  • 66
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements
    • Aldridge, J. E., Horibe, T. & Hoogenraad, N. J. Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS ONE 2, e874 (2007).
    • (2007) PLoS ONE , vol.2 , pp. e874
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 67
    • 84908077262 scopus 로고    scopus 로고
    • Multilayered genetic and omics dissection of mitochondrial activity in a mouse reference population
    • Wu, Y. et al. Multilayered genetic and omics dissection of mitochondrial activity in a mouse reference population. Cell 158, 1415-1430 (2014).
    • (2014) Cell , vol.158 , pp. 1415-1430
    • Wu, Y.1
  • 68
    • 84892500395 scopus 로고    scopus 로고
    • StAR enhances transcription of genes encoding the mitochondrial proteases involved in its own degradation
    • Bahat, A. et al. StAR enhances transcription of genes encoding the mitochondrial proteases involved in its own degradation. Mol. Endocrinol. 28, 208-224 (2014).
    • (2014) Mol. Endocrinol. , vol.28 , pp. 208-224
    • Bahat, A.1
  • 69
    • 60849097548 scopus 로고    scopus 로고
    • Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
    • Moisoi, N. et al. Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death Differ. 16, 449-464 (2009).
    • (2009) Cell Death Differ. , vol.16 , pp. 449-464
    • Moisoi, N.1
  • 70
    • 84892600839 scopus 로고    scopus 로고
    • Mitochondrial form and function
    • Friedman, J. R. & Nunnari, J. Mitochondrial form and function. Nature 505, 335-343 (2014).
    • (2014) Nature , vol.505 , pp. 335-343
    • Friedman, J.R.1    Nunnari, J.2
  • 71
    • 84910141948 scopus 로고    scopus 로고
    • Mitochondrial dynamics and inheritance during cell division, development and disease
    • Mishra, P. & Chan, D. C. Mitochondrial dynamics and inheritance during cell division, development and disease. Nature Rev. Mol. Cell Biol. 15, 634-646 (2014).
    • (2014) Nature Rev. Mol. Cell Biol. , vol.15 , pp. 634-646
    • Mishra, P.1    Chan, D.C.2
  • 72
    • 84896264348 scopus 로고    scopus 로고
    • The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
    • Anand, R. et al. The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission. J. Cell Biol. 204, 919-929 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 919-929
    • Anand, R.1
  • 73
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara, N., Fujita, Y., Oka, T. & Mihara, K. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25, 2966-2977 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 74
    • 84909595098 scopus 로고    scopus 로고
    • A Mitofusin-2-dependent inactivating cleavage of Opa1 links changes in mitochondria cristae and ER contacts in the postprandial liver
    • Sood, A. et al. A Mitofusin-2-dependent inactivating cleavage of Opa1 links changes in mitochondria cristae and ER contacts in the postprandial liver. Proc. Natl Acad. Sci. USA 111, 16017-16022 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 16017-16022
    • Sood, A.1
  • 75
    • 84897538678 scopus 로고    scopus 로고
    • Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation
    • Mishra, P., Carelli, V., Manfredi, G. & Chan, D. C. Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation. Cell Metab. 19, 630-641 (2014).
    • (2014) Cell Metab. , vol.19 , pp. 630-641
    • Mishra, P.1    Carelli, V.2    Manfredi, G.3    Chan, D.C.4
  • 76
    • 76149140917 scopus 로고    scopus 로고
    • Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
    • Ehses, S. et al. Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1. J. Cell Biol. 187, 1023-1036 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 1023-1036
    • Ehses, S.1
  • 77
    • 84860505850 scopus 로고    scopus 로고
    • Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice
    • Quiros, P. M. et al. Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice. EMBO J. 31, 2117-2133 (2012).
    • (2012) EMBO J. , vol.31 , pp. 2117-2133
    • Quiros, P.M.1
  • 78
    • 76149093590 scopus 로고    scopus 로고
    • Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
    • Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S. & van der Bliek, A. M. Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J. Cell Biol. 187, 959-966 (2009).
    • (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
  • 79
    • 84930039695 scopus 로고    scopus 로고
    • New roles for OMA1 metalloprotease: From mitochondrial proteostasis to metabolic homeostasis
    • Quiros, P. M., Ramsay, A. J. & Lopez-Otin, C. New roles for OMA1 metalloprotease: from mitochondrial proteostasis to metabolic homeostasis. Adipocyte 2, 7-11 (2013).
    • (2013) Adipocyte , vol.2 , pp. 7-11
    • Quiros, P.M.1    Ramsay, A.J.2    Lopez-Otin, C.3
  • 80
    • 84898612040 scopus 로고    scopus 로고
    • Dynamic survey of mitochondria by ubiquitin
    • Escobar-Henriques, M. & Langer, T. Dynamic survey of mitochondria by ubiquitin. EMBO Rep. 15, 231-243 (2014).
    • (2014) EMBO Rep. , vol.15 , pp. 231-243
    • Escobar-Henriques, M.1    Langer, T.2
  • 81
    • 84898025574 scopus 로고    scopus 로고
    • A small natural molecule promotes mitochondrial fusion through inhibition of the deubiquitinase USP30
    • Yue, W. et al. A small natural molecule promotes mitochondrial fusion through inhibition of the deubiquitinase USP30. Cell Res. 24, 482-496 (2014).
    • (2014) Cell Res. , vol.24 , pp. 482-496
    • Yue, W.1
  • 82
    • 48249124967 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane
    • Nakamura, N. & Hirose, S. Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane. Mol. Biol. Cell 19, 1903-1911 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1903-1911
    • Nakamura, N.1    Hirose, S.2
  • 84
    • 84887486172 scopus 로고    scopus 로고
    • The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
    • Jin, S. M. & Youle, R. J. The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria. Autophagy 9, 1750-1757 (2013).
    • (2013) Autophagy , vol.9 , pp. 1750-1757
    • Jin, S.M.1    Youle, R.J.2
  • 85
    • 84859428688 scopus 로고    scopus 로고
    • Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
    • Greene, A. W. et al. Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. EMBO Rep. 13, 378-385 (2012).
    • (2012) EMBO Rep. , vol.13 , pp. 378-385
    • Greene, A.W.1
  • 86
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin, S. M. et al. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191, 933-942 (2010).
    • (2010) J. Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1
  • 87
    • 84901615924 scopus 로고    scopus 로고
    • PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix
    • Thomas, R. E., Andrews, L. A., Burman, J. L., Lin, W. Y. & Pallanck, L. J. PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix. PLoS Genet. 10, e1004279 (2014).
    • (2014) PLoS Genet. , vol.10 , pp. e1004279
    • Thomas, R.E.1    Andrews, L.A.2    Burman, J.L.3    Lin, W.Y.4    Pallanck, L.J.5
  • 88
    • 84905696703 scopus 로고    scopus 로고
    • Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy
    • Cilenti, L. et al. Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy. Biochim. Biophys. Acta 1843, 1295-1307 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1295-1307
    • Cilenti, L.1
  • 89
    • 68249124331 scopus 로고    scopus 로고
    • The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity
    • Park, H. M. et al. The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity. Biochem. Biophys. Res. Commun. 387, 537-542 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 537-542
    • Park, H.M.1
  • 90
    • 65649118917 scopus 로고    scopus 로고
    • Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation
    • Xiong, H. et al. Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. J. Clin. Invest. 119, 650-660 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 650-660
    • Xiong, H.1
  • 91
    • 84867257217 scopus 로고    scopus 로고
    • Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5
    • Sekine, S. et al. Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5. J. Biol. Chem. 287, 34635-34645 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 34635-34645
    • Sekine, S.1
  • 92
    • 84899912073 scopus 로고    scopus 로고
    • A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy
    • Chen, G. et al. A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy. Mol. Cell 54, 362-377 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 362-377
    • Chen, G.1
  • 93
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang, Z., Jiang, H., Chen, S., Du, F. & Wang, X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 148, 228-243 (2012).
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 94
    • 84900801787 scopus 로고    scopus 로고
    • Impaired OMA1-dependent cleavage of OPA1 and reduced DRP1 fission activity combine to prevent mitophagy in cells that are dependent on oxidative phosphorylation
    • MacVicar, T. D. & Lane, J. D. Impaired OMA1-dependent cleavage of OPA1 and reduced DRP1 fission activity combine to prevent mitophagy in cells that are dependent on oxidative phosphorylation. J. Cell Sci. 127, 2313-2325 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 2313-2325
    • MacVicar, T.D.1    Lane, J.D.2
  • 95
    • 84887472941 scopus 로고    scopus 로고
    • Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy
    • Wang, K., Jin, M., Liu, X. & Klionsky, D. J. Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy. Autophagy 9, 1828-1836 (2013).
    • (2013) Autophagy , vol.9 , pp. 1828-1836
    • Wang, K.1    Jin, M.2    Liu, X.3    Klionsky, D.J.4
  • 96
    • 84903179483 scopus 로고    scopus 로고
    • The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
    • Bingol, B. et al. The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510, 370-375 (2014).
    • (2014) Nature , vol.510 , pp. 370-375
    • Bingol, B.1
  • 98
    • 84907919478 scopus 로고    scopus 로고
    • Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis
    • Jiang, X., Jiang, H., Shen, Z. & Wang, X. Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis. Proc. Natl Acad. Sci. USA 111, 14782-14787 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 14782-14787
    • Jiang, X.1    Jiang, H.2    Shen, Z.3    Wang, X.4
  • 99
    • 84898603457 scopus 로고    scopus 로고
    • Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics
    • Baker, M. J. et al. Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics. EMBO J. 33, 578-593 (2014).
    • (2014) EMBO J. , vol.33 , pp. 578-593
    • Baker, M.J.1
  • 100
    • 84901712100 scopus 로고    scopus 로고
    • OMA1 mediates OPA1 proteolysis and mitochondrial fragmentation in experimental models of ischemic kidney injury
    • Xiao, X. et al. OMA1 mediates OPA1 proteolysis and mitochondrial fragmentation in experimental models of ischemic kidney injury. Am. J. Physiol. Renal Physiol. 306, F1318-F1326 (2014).
    • (2014) Am. J. Physiol. Renal Physiol. , vol.306 , pp. F1318-F1326
    • Xiao, X.1
  • 101
    • 40449124712 scopus 로고    scopus 로고
    • Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons
    • Chao, J. R. et al. Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons. Nature 452, 98-102 (2008).
    • (2008) Nature , vol.452 , pp. 98-102
    • Chao, J.R.1
  • 102
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y. et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell 8, 613-621 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1
  • 103
    • 74749104596 scopus 로고    scopus 로고
    • The Wilms' tumor suppressor protein WT1 is processed by the serine protease HtrA2/Omi
    • Hartkamp, J., Carpenter, B. & Roberts, S. G. The Wilms' tumor suppressor protein WT1 is processed by the serine protease HtrA2/Omi. Mol. Cell 37, 159-171 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 159-171
    • Hartkamp, J.1    Carpenter, B.2    Roberts, S.G.3
  • 104
    • 84884824441 scopus 로고    scopus 로고
    • The proteases HtrA2/Omi and UCH-L1 regulate TNF-induced necroptosis
    • Sosna, J. et al. The proteases HtrA2/Omi and UCH-L1 regulate TNF-induced necroptosis. Cell Commun. Signal. 11, 76 (2013).
    • (2013) Cell Commun. Signal. , vol.11 , Issue.76
    • Sosna, J.1
  • 105
    • 84876414704 scopus 로고    scopus 로고
    • Alternative germ cell death pathway in Drosophila involves HtrA2/Omi, lysosomes, and a caspase-9 counterpart
    • Yacobi-Sharon, K., Namdar, Y. & Arama, E. Alternative germ cell death pathway in Drosophila involves HtrA2/Omi, lysosomes, and a caspase-9 counterpart. Dev. Cell 25, 29-42 (2013).
    • (2013) Dev. Cell , vol.25 , pp. 29-42
    • Yacobi-Sharon, K.1    Namdar, Y.2    Arama, E.3
  • 106
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S. et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126, 163-175 (2006).
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 107
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza, C. et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126, 177-189 (2006).
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 108
    • 84874591240 scopus 로고    scopus 로고
    • The role of mitochondria in aging
    • Bratic, A. & Larsson, N. G. The role of mitochondria in aging. J. Clin. Invest. 123, 951-957 (2013).
    • (2013) J. Clin. Invest. , vol.123 , pp. 951-957
    • Bratic, A.1    Larsson, N.G.2
  • 109
    • 79955664111 scopus 로고    scopus 로고
    • Mitochondrial protein quality control during biogenesis and aging
    • Baker, B. M. & Haynes, C. M. Mitochondrial protein quality control during biogenesis and aging. Trends Biochem. Sci. 36, 254-261 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 254-261
    • Baker, B.M.1    Haynes, C.M.2
  • 110
    • 84887022165 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial protein quality control in aging
    • Lionaki, E. & Tavernarakis, N. Oxidative stress and mitochondrial protein quality control in aging. J. Proteomics 92, 181-194 (2013).
    • (2013) J. Proteomics , vol.92 , pp. 181-194
    • Lionaki, E.1    Tavernarakis, N.2
  • 111
    • 36549006049 scopus 로고    scopus 로고
    • Importance of the Lon protease in mitochondrial maintenance and the significance of declining Lon in aging
    • Ngo, J. K. & Davies, K. J. Importance of the Lon protease in mitochondrial maintenance and the significance of declining Lon in aging. Ann. N.Y. Acad. Sci. 1119, 78-87 (2007).
    • (2007) Ann. N.Y. Acad. Sci. , vol.1119 , pp. 78-87
    • Ngo, J.K.1    Davies, K.J.2
  • 112
    • 84878771657 scopus 로고    scopus 로고
    • Upregulation of the mitochondrial Lon protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging
    • Ngo, J. K., Pomatto, L. C. & Davies, K. J. Upregulation of the mitochondrial Lon protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging. Redox Biol. 1, 258-264 (2013).
    • (2013) Redox Biol. , vol.1 , pp. 258-264
    • Ngo, J.K.1    Pomatto, L.C.2    Davies, K.J.3
  • 113
    • 84871962586 scopus 로고    scopus 로고
    • Deletion of the mitochondrial Pim1/Lon protease in yeast results in accelerated aging and impairment of the proteasome
    • Erjavec, N. et al. Deletion of the mitochondrial Pim1/Lon protease in yeast results in accelerated aging and impairment of the proteasome. Free Radic. Biol. Med. 56, 9-16 (2013).
    • (2013) Free Radic. Biol. Med. , vol.56 , pp. 9-16
    • Erjavec, N.1
  • 114
    • 67650091290 scopus 로고    scopus 로고
    • Increasing organismal healthspan by enhancing mitochondrial protein quality control
    • Luce, K. & Osiewacz, H. D. Increasing organismal healthspan by enhancing mitochondrial protein quality control. Nature Cell Biol. 11, 852-858 (2009).
    • (2009) Nature Cell Biol. , vol.11 , pp. 852-858
    • Luce, K.1    Osiewacz, H.D.2
  • 115
    • 84879151902 scopus 로고    scopus 로고
    • Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain
    • Fischer, F., Weil, A., Hamann, A. & Osiewacz, H. D. Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain. Nature Commun. 4, 1397 (2013).
    • (2013) Nature Commun. , vol.4 , Issue.1397
    • Fischer, F.1    Weil, A.2    Hamann, A.3    Osiewacz, H.D.4
  • 116
    • 84872355087 scopus 로고    scopus 로고
    • Loss of HtrA2/Omi activity in non-neuronal tissues of adult mice causes premature aging
    • Kang, S. et al. Loss of HtrA2/Omi activity in non-neuronal tissues of adult mice causes premature aging. Cell Death Differ. 20, 259-269 (2013).
    • (2013) Cell Death Differ. , vol.20 , pp. 259-269
    • Kang, S.1
  • 117
    • 40849142484 scopus 로고    scopus 로고
    • The mitochondrial protease AFG3L2 is essential for axonal development
    • Maltecca, F. et al. The mitochondrial protease AFG3L2 is essential for axonal development. J. Neurosci. 28, 2827-2836 (2008).
    • (2008) J. Neurosci. , vol.28 , pp. 2827-2836
    • Maltecca, F.1
  • 118
    • 84857194709 scopus 로고    scopus 로고
    • Evolutionary conserved longevity genes and human cognitive abilities in elderly cohorts
    • Lopez, L. M. et al. Evolutionary conserved longevity genes and human cognitive abilities in elderly cohorts. Eur. J. Hum. Genet. 20, 341-347 (2012).
    • (2012) Eur. J. Hum. Genet. , vol.20 , pp. 341-347
    • Lopez, L.M.1
  • 119
    • 41549167023 scopus 로고    scopus 로고
    • A mutation in the inner mitochondrial membrane peptidase 2-like gene (Immp2l) affects mitochondrial function and impairs fertility in mice
    • Lu, B. et al. A mutation in the inner mitochondrial membrane peptidase 2-like gene (Immp2l) affects mitochondrial function and impairs fertility in mice. Biol. Reprod. 78, 601-610 (2008).
    • (2008) Biol. Reprod. , vol.78 , pp. 601-610
    • Lu, B.1
  • 120
    • 79960327664 scopus 로고    scopus 로고
    • Mitochondrial peptidase IMMP2L mutation causes early onset of age-Associated disorders and impairs adult stem cell self-renewal
    • George, S. K., Jiao, Y., Bishop, C. E. & Lu, B. Mitochondrial peptidase IMMP2L mutation causes early onset of age-Associated disorders and impairs adult stem cell self-renewal. Aging Cell 10, 584-594 (2011).
    • (2011) Aging Cell , vol.10 , pp. 584-594
    • George, S.K.1    Jiao, Y.2    Bishop, C.E.3    Lu, B.4
  • 121
    • 84861594496 scopus 로고    scopus 로고
    • Oxidative stress is involved in age-dependent spermatogenic damage of Immp2l mutant mice
    • George, S. K., Jiao, Y., Bishop, C. E. & Lu, B. Oxidative stress is involved in age-dependent spermatogenic damage of Immp2l mutant mice. Free Radic. Biol. Med. 52, 2223-2233 (2012).
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 2223-2233
    • George, S.K.1    Jiao, Y.2    Bishop, C.E.3    Lu, B.4
  • 122
    • 84885139764 scopus 로고    scopus 로고
    • Mitochondrial aminopeptidase deletion increases chronological lifespan and oxidative stress resistance while decreasing respiratory metabolism in S. Cerevisiae
    • Stames, E. M. & O'Toole, J. F. Mitochondrial aminopeptidase deletion increases chronological lifespan and oxidative stress resistance while decreasing respiratory metabolism in S. cerevisiae. PLoS ONE 8, e77234 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e77234
    • Stames, E.M.1    O'toole, J.F.2
  • 124
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati, V. et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299, 256-259 (2003).
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1
  • 125
    • 25444498785 scopus 로고    scopus 로고
    • Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
    • Strauss, K. M. et al. Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum. Mol. Genet. 14, 2099-2111 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2099-2111
    • Strauss, K.M.1
  • 126
    • 84919898161 scopus 로고    scopus 로고
    • Mitochondrial serine protease HTRA2 p.G399S in a kindred with essential tremor and Parkinson disease
    • Unal Gulsuner, H. et al. Mitochondrial serine protease HTRA2 p.G399S in a kindred with essential tremor and Parkinson disease. Proc. Natl Acad. Sci. USA 111, 18285-18290 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 18285-18290
    • Unal Gulsuner, H.1
  • 127
    • 0142246441 scopus 로고    scopus 로고
    • Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of Mnd2 mutant mice
    • Jones, J. M. et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of Mnd2 mutant mice. Nature 425, 721-727 (2003).
    • (2003) Nature , vol.425 , pp. 721-727
    • Jones, J.M.1
  • 128
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • Martins, L. M. et al. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol. Cell. Biol. 24, 9848-9862 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9848-9862
    • Martins, L.M.1
  • 129
    • 79955410000 scopus 로고    scopus 로고
    • Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease
    • Shi, G. et al. Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease. Hum. Mol. Genet. 20, 1966-1974 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1966-1974
    • Shi, G.1
  • 130
    • 84887084958 scopus 로고    scopus 로고
    • The role of PARL and HtrA2 in striatal neuronal injury after transient global cerebral ischemia
    • Yoshioka, H. et al. The role of PARL and HtrA2 in striatal neuronal injury after transient global cerebral ischemia. J. Cereb. Blood Flow Metab. 33, 1658-1665 (2013).
    • (2013) J. Cereb. Blood Flow Metab. , vol.33 , pp. 1658-1665
    • Yoshioka, H.1
  • 131
    • 84908513899 scopus 로고    scopus 로고
    • Intragenic deletions affecting two alternative transcripts of the IMMP2L gene in patients with Tourette syndrome
    • Bertelsen, B. et al. Intragenic deletions affecting two alternative transcripts of the IMMP2L gene in patients with Tourette syndrome. Eur. J. Hum. Genet. 22, 1283-1289 (2014).
    • (2014) Eur. J. Hum. Genet. , vol.22 , pp. 1283-1289
    • Bertelsen, B.1
  • 132
    • 84860879137 scopus 로고    scopus 로고
    • A novel approach of homozygous haplotype sharing identifies candidate genes in autism spectrum disorder
    • Casey, J. P. et al. A novel approach of homozygous haplotype sharing identifies candidate genes in autism spectrum disorder. Hum. Genet. 131, 565-579 (2012).
    • (2012) Hum. Genet. , vol.131 , pp. 565-579
    • Casey, J.P.1
  • 133
    • 84906932969 scopus 로고    scopus 로고
    • Interstitial 7q31.1 copy number variations disrupting IMMP2L gene are associated with a wide spectrum of neurodevelopmental disorders
    • Gimelli, S. et al. Interstitial 7q31.1 copy number variations disrupting IMMP2L gene are associated with a wide spectrum of neurodevelopmental disorders. Mol. Cytogenet. 7, 54 (2014).
    • (2014) Mol. Cytogenet. , vol.7 , Issue.54
    • Gimelli, S.1
  • 134
    • 77950298030 scopus 로고    scopus 로고
    • Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28
    • Di Bella, D. et al. Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nature Genet. 42, 313-321 (2010).
    • (2010) Nature Genet. , vol.42 , pp. 313-321
    • Di Bella, D.1
  • 135
    • 80055087830 scopus 로고    scopus 로고
    • Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases
    • Pierson, T. M. et al. Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases. PLoS Genet. 7, e1002325 (2011).
    • (2011) PLoS Genet. , vol.7 , pp. e1002325
    • Pierson, T.M.1
  • 136
    • 0032511186 scopus 로고    scopus 로고
    • Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease
    • Casari, G. et al. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93, 973-983 (1998).
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1
  • 137
    • 84899863857 scopus 로고    scopus 로고
    • Mutations in the SPG7 gene cause chronic progressive external ophthalmoplegia through disordered mitochondrial DNA maintenance
    • Pfeffer, G. et al. Mutations in the SPG7 gene cause chronic progressive external ophthalmoplegia through disordered mitochondrial DNA maintenance. Brain 137, 1323-1336 (2014).
    • (2014) Brain , vol.137 , pp. 1323-1336
    • Pfeffer, G.1
  • 138
    • 84899688615 scopus 로고    scopus 로고
    • Spastic paraplegia type 7 is associated with multiple mitochondrial DNA deletions
    • Wedding, I. M. et al. Spastic paraplegia type 7 is associated with multiple mitochondrial DNA deletions. PLoS ONE 9, e86340 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e86340
    • Wedding, I.M.1
  • 139
    • 1342310772 scopus 로고    scopus 로고
    • Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport
    • Ferreirinha, F. et al. Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J. Clin. Invest. 113, 231-242 (2004).
    • (2004) J. Clin. Invest. , vol.113 , pp. 231-242
    • Ferreirinha, F.1
  • 140
    • 65549147202 scopus 로고    scopus 로고
    • Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration
    • Martinelli, P. et al. Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration. Hum. Mol. Genet. 18, 2001-2013 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2001-2013
    • Martinelli, P.1
  • 141
    • 84899885579 scopus 로고    scopus 로고
    • Loss of the m-AAA protease subunit AFG3L2 causes mitochondrial transport defects and tau hyperphosphorylation
    • Kondadi, A. K. et al. Loss of the m-AAA protease subunit AFG3L2 causes mitochondrial transport defects and tau hyperphosphorylation. EMBO J. 33, 1011-1026 (2014).
    • (2014) EMBO J. , vol.33 , pp. 1011-1026
    • Kondadi, A.K.1
  • 142
    • 67651154308 scopus 로고    scopus 로고
    • Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration
    • Maltecca, F. et al. Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration. J. Neurosci. 29, 9244-9254 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 9244-9254
    • Maltecca, F.1
  • 143
    • 84899987055 scopus 로고    scopus 로고
    • SPG7 variant escapes phosphorylation-regulated processing by AFG3L2, elevates mitochondrial ROS, and is associated with multiple clinical phenotypes
    • Almontashiri, N. A. et al. SPG7 variant escapes phosphorylation-regulated processing by AFG3L2, elevates mitochondrial ROS, and is associated with multiple clinical phenotypes. Cell Rep. 7, 834-847 (2014).
    • (2014) Cell Rep. , vol.7 , pp. 834-847
    • Almontashiri, N.A.1
  • 144
    • 77955284487 scopus 로고    scopus 로고
    • Regulation of skeletal muscle oxidative capacity and insulin signaling by the mitochondrial rhomboid protease PARL
    • Civitarese, A. E. et al. Regulation of skeletal muscle oxidative capacity and insulin signaling by the mitochondrial rhomboid protease PARL. Cell Metab. 11, 412-426 (2010).
    • (2010) Cell Metab. , vol.11 , pp. 412-426
    • Civitarese, A.E.1
  • 145
    • 84901713796 scopus 로고    scopus 로고
    • Neurolysin knockout mice generation and initial phenotype characterization
    • Cavalcanti, D. M. et al. Neurolysin knockout mice generation and initial phenotype characterization. J. Biol. Chem. 289, 15426-15440 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 15426-15440
    • Cavalcanti, D.M.1
  • 146
    • 40749105508 scopus 로고    scopus 로고
    • Variations in DNA elucidate molecular networks that cause disease
    • Chen, Y. et al. Variations in DNA elucidate molecular networks that cause disease. Nature 452, 429-435 (2008).
    • (2008) Nature , vol.452 , pp. 429-435
    • Chen, Y.1
  • 147
    • 84920722450 scopus 로고    scopus 로고
    • CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease
    • Strauss, K. A. et al. CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease. Am. J. Hum. Genet. 96, 121-135 (2015).
    • (2015) Am. J. Hum. Genet. , vol.96 , pp. 121-135
    • Strauss, K.A.1
  • 148
    • 84875944287 scopus 로고    scopus 로고
    • Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease
    • Jenkinson, E. M. et al. Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease. Am. J. Hum. Genet. 92, 605-613 (2013).
    • (2013) Am. J. Hum. Genet. , vol.92 , pp. 605-613
    • Jenkinson, E.M.1
  • 149
    • 84873995203 scopus 로고    scopus 로고
    • Mitochondrial complex III deficiency caused by a homozygous UQCRC2 mutation presenting with neonatal-onset recurrent metabolic decompensation
    • Miyake, N. et al. Mitochondrial complex III deficiency caused by a homozygous UQCRC2 mutation presenting with neonatal-onset recurrent metabolic decompensation. Hum. Mutat. 34, 446-452 (2013).
    • (2013) Hum. Mutat. , vol.34 , pp. 446-452
    • Miyake, N.1
  • 150
    • 77949865316 scopus 로고    scopus 로고
    • Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
    • O'Toole, J. F. et al. Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy. J. Clin. Invest. 120, 791-802 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 791-802
    • O'toole, J.F.1
  • 151
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D. & Weinberg, R. A. Hallmarks of cancer: the next generation. Cell 144, 646-674 (2011).
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 152
    • 84866665390 scopus 로고    scopus 로고
    • Mitochondria and cancer
    • Wallace, D. C. Mitochondria and cancer. Nature Rev. Cancer 12, 685-698 (2012).
    • (2012) Nature Rev. Cancer , vol.12 , pp. 685-698
    • Wallace, D.C.1
  • 153
    • 84894201019 scopus 로고    scopus 로고
    • Down-regulating overexpressed human Lon in cervical cancer suppresses cell proliferation and bioenergetics
    • Nie, X. et al. Down-regulating overexpressed human Lon in cervical cancer suppresses cell proliferation and bioenergetics. PLoS ONE 8, e81084 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e81084
    • Nie, X.1
  • 154
    • 84879678155 scopus 로고    scopus 로고
    • Overexpression of Lon contributes to survival and aggressive phenotype of cancer cells through mitochondrial complex I-mediated generation of reactive oxygen species
    • Cheng, C. W. et al. Overexpression of Lon contributes to survival and aggressive phenotype of cancer cells through mitochondrial complex I-mediated generation of reactive oxygen species. Cell Death Dis. 4, e681 (2013).
    • (2013) Cell Death Dis. , vol.4 , pp. e681
    • Cheng, C.W.1
  • 155
    • 84919715326 scopus 로고    scopus 로고
    • Silencing of mitochondrial Lon protease deeply impairs mitochondrial proteome and function in colon cancer cells
    • Gibellini, L. et al. Silencing of mitochondrial Lon protease deeply impairs mitochondrial proteome and function in colon cancer cells. FASEB J. 28, 5122-5135 (2014).
    • (2014) FASEB J. , vol.28 , pp. 5122-5135
    • Gibellini, L.1
  • 156
    • 84897098198 scopus 로고    scopus 로고
    • Effect of Lon protease knockdown on mitochondrial function in HeLa cells
    • Bayot, A. et al. Effect of Lon protease knockdown on mitochondrial function in HeLa cells. Biochimie 100, 38-47 (2014).
    • (2014) Biochimie , vol.100 , pp. 38-47
    • Bayot, A.1
  • 157
    • 84859585597 scopus 로고    scopus 로고
    • The mitochondrial ATP-dependent Lon protease: A novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives
    • Bernstein, S. H. et al. The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives. Blood 119, 3321-3329 (2012).
    • (2012) Blood , vol.119 , pp. 3321-3329
    • Bernstein, S.H.1
  • 158
    • 85019028850 scopus 로고    scopus 로고
    • Lon protease: A key enzyme controlling mitochondrial bioenergetics in cancer
    • Quir, P. M., Bocena, C. & Laez-Ota, C. Lon protease: a key enzyme controlling mitochondrial bioenergetics in cancer. Mol. Cell. Oncol. 1, e968505 (2014).
    • (2014) Mol. Cell. Oncol. , vol.1 , pp. e968505
    • Quir, P.M.1    Bocena, C.2    Laez-Ota, C.3
  • 159
    • 84897553749 scopus 로고    scopus 로고
    • P53-mediated activation of the mitochondrial protease HtrA2/Omi prevents cell invasion
    • Yamauchi, S. et al. p53-mediated activation of the mitochondrial protease HtrA2/Omi prevents cell invasion. J. Cell Biol. 204, 1191-1207 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 1191-1207
    • Yamauchi, S.1
  • 160
    • 84907584469 scopus 로고    scopus 로고
    • P53 is required for cisplatin-induced processing of the mitochondrial fusion protein L-Opa1 that is mediated by the mitochondrial metallopeptidase Oma1 in gynecologic cancers
    • Kong, B., Wang, Q., Fung, E., Xue, K. & Tsang, B. K. p53 is required for cisplatin-induced processing of the mitochondrial fusion protein L-Opa1 that is mediated by the mitochondrial metallopeptidase Oma1 in gynecologic cancers. J. Biol. Chem. 289, 27134-27145 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 27134-27145
    • Kong, B.1    Wang, Q.2    Fung, E.3    Xue, K.4    Tsang, B.K.5
  • 161
    • 33745056525 scopus 로고    scopus 로고
    • MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer
    • Leszczyniecka, M. et al. MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer. Oncogene 25, 3471-3478 (2006).
    • (2006) Oncogene , vol.25 , pp. 3471-3478
    • Leszczyniecka, M.1
  • 162
    • 84885235141 scopus 로고    scopus 로고
    • Genome-wide association study on differentiated thyroid cancer
    • Kohler, A. et al. Genome-wide association study on differentiated thyroid cancer. J. Clin. Endocrinol. Metab. 98, E1674-E1681 (2013).
    • (2013) J. Clin. Endocrinol. Metab. , vol.98 , pp. E1674-E1681
    • Kohler, A.1
  • 163
    • 79959493954 scopus 로고    scopus 로고
    • Targeting capacity and conservation of PreP homologues localization in mitochondria of different species
    • Alikhani, N. et al. Targeting capacity and conservation of PreP homologues localization in mitochondria of different species. J. Mol. Biol. 410, 400-410 (2011).
    • (2011) J. Mol. Biol. , vol.410 , pp. 400-410
    • Alikhani, N.1
  • 164
    • 2942684871 scopus 로고    scopus 로고
    • The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization
    • Canet-Aviles, R. M. et al. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc. Natl Acad. Sci. USA 101, 9103-9108 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9103-9108
    • Canet-Aviles, R.M.1
  • 165
    • 84655167921 scopus 로고    scopus 로고
    • Biogenesis of the cytochrome bc1 complex and role of assembly factors
    • Smith, P. M., Fox, J. L. & Winge, D. R. Biogenesis of the cytochrome bc1 complex and role of assembly factors. Biochim. Biophys. Acta 1817, 276-286 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 276-286
    • Smith, P.M.1    Fox, J.L.2    Winge, D.R.3
  • 166
    • 33751555610 scopus 로고    scopus 로고
    • The identification of novel ovarian proteases through the use of genomic and bioinformatic methodologies
    • Miyakoshi, K. et al. The identification of novel ovarian proteases through the use of genomic and bioinformatic methodologies. Biol. Reprod. 75, 823-835 (2006).
    • (2006) Biol. Reprod. , vol.75 , pp. 823-835
    • Miyakoshi, K.1
  • 167
    • 84866685475 scopus 로고    scopus 로고
    • Calpains mitochondria, and apoptosis
    • Smith, M. A. & Schnellmann, R. G. Calpains, mitochondria, and apoptosis. Cardiovasc. Res. 96, 32-37 (2012).
    • (2012) Cardiovasc. Res. , vol.96 , pp. 32-37
    • Smith, M.A.1    Schnellmann, R.G.2
  • 168
    • 33845337981 scopus 로고    scopus 로고
    • Calpain 10: A mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction
    • Arrington, D. D., Van Vleet, T. R. & Schnellmann, R. G. Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction. Am. J. Physiol. Cell Physiol. 291, C1159-C1171 (2006).
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291 , pp. C1159-C1171
    • Arrington, D.D.1    Van Vleet, T.R.2    Schnellmann, R.G.3
  • 170
    • 32444434664 scopus 로고    scopus 로고
    • Caspases 3 and 7: Key mediators of mitochondrial events of apoptosis
    • Lakhani, S. A. et al. Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 311, 847-851 (2006).
    • (2006) Science , vol.311 , pp. 847-851
    • Lakhani, S.A.1
  • 171
    • 79952708318 scopus 로고    scopus 로고
    • Caspase-8 and bid: Caught in the act between death receptors and mitochondria
    • Kantari, C. & Walczak, H. Caspase-8 and bid: caught in the act between death receptors and mitochondria. Biochim. Biophys. Acta 1813, 558-563 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 558-563
    • Kantari, C.1    Walczak, H.2
  • 172
    • 18244387009 scopus 로고    scopus 로고
    • Pre-processed caspase-9 contained in mitochondria participates in apoptosis
    • Costantini, P. et al. Pre-processed caspase-9 contained in mitochondria participates in apoptosis. Cell Death Differ. 9, 82-88 (2002).
    • (2002) Cell Death Differ. , vol.9 , pp. 82-88
    • Costantini, P.1
  • 173
    • 84920892842 scopus 로고    scopus 로고
    • USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin
    • Durcan, T. M. et al. USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin. EMBO J. 33, 2473-2491 (2014).
    • (2014) EMBO J. , vol.33 , pp. 2473-2491
    • Durcan, T.M.1
  • 174
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart, M. et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463, 103-107 (2010).
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1
  • 175
    • 84920095272 scopus 로고    scopus 로고
    • The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy
    • Cornelissen, T. et al. The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy. Hum. Mol. Genet. 23, 5227-5242 (2014).
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 5227-5242
    • Cornelissen, T.1
  • 176
    • 84908343054 scopus 로고    scopus 로고
    • Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration
    • Fu, J. et al. Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration. PLoS Genet. 10, e1004579 (2014).
    • (2014) PLoS Genet. , vol.10 , pp. e1004579
    • Fu, J.1
  • 177
    • 34248225298 scopus 로고    scopus 로고
    • The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
    • Zunino, R., Schauss, A., Rippstein, P., Andrade-Navarro, M. & McBride, H. M. The SUMO protease SENP5 is required to maintain mitochondrial morphology and function. J. Cell Sci. 120, 1178-1188 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 1178-1188
    • Zunino, R.1    Schauss, A.2    Rippstein, P.3    Andrade-Navarro, M.4    McBride, H.M.5
  • 178
    • 84862280415 scopus 로고    scopus 로고
    • A cryptic mitochondrial targeting motif in Atg4D links caspase cleavage with mitochondrial import and oxidative stress
    • Betin, V. M., MacVicar, T. D., Parsons, S. F., Anstee, D. J. & Lane, J. D. A cryptic mitochondrial targeting motif in Atg4D links caspase cleavage with mitochondrial import and oxidative stress. Autophagy 8, 664-676 (2012).
    • (2012) Autophagy , vol.8 , pp. 664-676
    • Betin, V.M.1    MacVicar, T.D.2    Parsons, S.F.3    Anstee, D.J.4    Lane, J.D.5
  • 179
    • 9144260111 scopus 로고    scopus 로고
    • Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
    • Leissring, M. A. et al. Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem. J. 383, 439-446 (2004).
    • (2004) Biochem. J. , vol.383 , pp. 439-446
    • Leissring, M.A.1
  • 180
    • 19744366732 scopus 로고    scopus 로고
    • Nardilysin facilitates complex formation between mitochondrial malate dehydrogenase and citrate synthase
    • Chow, K. M., Ma, Z., Cai, J., Pierce, W. M. & Hersh, L. B. Nardilysin facilitates complex formation between mitochondrial malate dehydrogenase and citrate synthase. Biochim. Biophys. Acta 1723, 292-301 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 292-301
    • Chow, K.M.1    Ma, Z.2    Cai, J.3    Pierce, W.M.4    Hersh, L.B.5
  • 181
    • 43049160756 scopus 로고    scopus 로고
    • Granzyme A cleaves a mitochondrial complex i protein to initiate caspase-independent cell death
    • Martinvalet, D., Dykxhoorn, D. M., Ferrini, R. & Lieberman, J. Granzyme A cleaves a mitochondrial complex I protein to initiate caspase-independent cell death. Cell 133, 681-692 (2008).
    • (2008) Cell , vol.133 , pp. 681-692
    • Martinvalet, D.1    Dykxhoorn, D.M.2    Ferrini, R.3    Lieberman, J.4
  • 182
    • 77954595054 scopus 로고    scopus 로고
    • Deregulation of mitochondrial membrane potential by mitochondrial insertion of granzyme B and direct Hax-1 cleavage
    • Han, J. et al. Deregulation of mitochondrial membrane potential by mitochondrial insertion of granzyme B and direct Hax-1 cleavage. J. Biol. Chem. 285, 22461-22472 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 22461-22472
    • Han, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.