메뉴 건너뛰기




Volumn 20, Issue 19, 2009, Pages 4216-4224

Autocatalytic processing of m-AAA protease subunits in mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

M AAA PROTEASE; PARAPLEGIN; PEPTIDASE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 70350230142     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-03-0218     Document Type: Article
Times cited : (44)

References (30)
  • 1
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • DOI 10.1016/S0092-8674(00)81271-4
    • Arlt, H., Tauer, R., Feldmann, H., Neupert, W., and Langer, T. (1996). The YTA10-12-complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85, 875-885. (Pubitemid 26192138)
    • (1996) Cell , vol.85 , Issue.6 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 4
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic Organelles in Disease, Aging, and Development
    • DOI 10.1016/j.cell.2006.06.010, PII S0092867406007689
    • Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252. (Pubitemid 43929096)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1241-1252
    • Chan, D.C.1
  • 5
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S., et al. (2006). Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126, 163-175.
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 6
    • 65549158993 scopus 로고    scopus 로고
    • AFG3L2 mutations cause autosomal dominant ataxia SCA28 and reveal an essential role of the m-AAA AFG3L2 homocomplex in the cerebellum
    • DiBella, D., et al. (2008). AFG3L2 mutations cause autosomal dominant ataxia SCA28 and reveal an essential role of the m-AAA AFG3L2 homocomplex in the cerebellum. In: Annual meeting of the American Society of Human Genetics, Philadelphia, PA.
    • (2008) Annual Meeting of the American Society of Human Genetics, Philadelphia, PA
    • DiBella, D.1
  • 7
    • 34548349869 scopus 로고    scopus 로고
    • OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria
    • Duvezin-Caubet, S., et al. (2007). OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria. Mol. Biol. Cell 18, 3582-3590.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3582-3590
    • Duvezin-Caubet, S.1
  • 8
    • 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. (2004). Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J. Clin. Invest. 113, 231-242.
    • (2004) J. Clin. Invest. , vol.113 , pp. 231-242
    • Ferreirinha, F.1
  • 10
    • 34548313686 scopus 로고    scopus 로고
    • Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
    • DOI 10.1083/jcb.200704112
    • Griparic, L., Kanazawa, T., and van der Bliek, A. M. (2007). Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. J. Cell Biol. 178, 757-764. (Pubitemid 47347361)
    • (2007) Journal of Cell Biology , vol.178 , Issue.5 , pp. 757-764
    • Griparic, L.1    Kanazawa, T.2    Van Der Bliek, A.M.3
  • 11
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • DOI 10.1038/sj.emboj.7601184, PII 7601184
    • Ishihara, N., Fujita, Y., Oka, T., and Mihara, K. (2006). Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25, 2966-2977. (Pubitemid 44106750)
    • (2006) EMBO Journal , vol.25 , Issue.13 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 12
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: Versatile activities of AAA proteases and other peptidases
    • Koppen, M., and Langer, T. (2007). Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit. Rev. Biochem. Mol. Biol. 42, 221-242.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 13
    • 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., and Langer, T. (2007). Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia. Mol. Cell. Biol. 27, 758-767.
    • (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
  • 14
    • 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
    • DOI 10.1006/geno.2001.6560
    • Kremmidiotis, G., Gardner, A. E., Settasatian, C., Savoia, A., Sutherland, G. R., and Callen, D. F. (2001). 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. (Pubitemid 32744624)
    • (2001) Genomics , vol.76 , Issue.1-3 , pp. 58-65
    • Kremmidiotis, G.1    Gardner, A.E.2    Settasatian, C.3    Savoia, A.4    Sutherland, G.R.5    Callen, D.F.6
  • 15
    • 0030453927 scopus 로고    scopus 로고
    • The mitochondrial processing peptidase: Function and specificity
    • DOI 10.1007/BF01952105
    • Luciano, P., and Geli, V. (1996). The mitochondrial processing peptidase: function and specificity. Experientia 52, 1077-1082. (Pubitemid 27022817)
    • (1996) Experientia , vol.52 , Issue.12 , pp. 1077-1082
    • Luciano, P.1    Geli, V.2
  • 16
    • 40849142484 scopus 로고    scopus 로고
    • The mitochondrial protease AFG3L2 is essential for axonal development
    • Maltecca, F., et al. (2008). The mitochondrial protease AFG3L2 is essential for axonal development. J. Neurosci. 28, 2827-2836.
    • (2008) J. Neurosci. , vol.28 , pp. 2827-2836
    • Maltecca, F.1
  • 18
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W., and Herrmann, J. M. (2007). Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 19
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., and Langer, T. (2005). The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123, 277-289.
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1    Ehses, S.2    Koppen, M.3    Bernacchia, A.4    Rugarli, E.I.5    Langer, T.6
  • 20
    • 34250768073 scopus 로고    scopus 로고
    • A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • DOI 10.1038/sj.cdd.4402145, PII 4402145
    • Pellegrini, L., and Scorrano, L. (2007). A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ. 14, 1275-1284. (Pubitemid 46969865)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.7 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2
  • 21
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • Piwko, W., and Jentsch, S. (2006). Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site. Nat. Struct. Mol. Biol. 13, 691-697.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 22
    • 33744970020 scopus 로고    scopus 로고
    • Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia
    • Rugarli, E. I., and Langer, T. (2006). Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia. Trends Mol. Med. 12, 262-269.
    • (2006) Trends Mol. Med. , vol.12 , pp. 262-269
    • Rugarli, E.I.1    Langer, T.2
  • 23
    • 55549094109 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia: Clinical features and pathogenetic mechanisms
    • Salinas, S., Proukakis, C., Crosby, A., and Warner, T. T. (2008). Hereditary spastic paraplegia: clinical features and pathogenetic mechanisms. Lancet Neurol. 7, 1127-1138.
    • (2008) Lancet Neurol. , vol.7 , pp. 1127-1138
    • Salinas, S.1    Proukakis, C.2    Crosby, A.3    Warner, T.T.4
  • 24
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • DOI 10.1083/jcb.200704110
    • Song, Z., Chen, H., Fiket, M., Alexander, C., and Chan, D. C. (2007). OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 178, 749-755. (Pubitemid 47347360)
    • (2007) Journal of Cell Biology , vol.178 , Issue.5 , pp. 749-755
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4    Chan, D.C.5
  • 25
    • 33846526268 scopus 로고    scopus 로고
    • Studying proteolysis within mitochondria
    • Tatsuta, T., and Langer, T. (2007). Studying proteolysis within mitochondria. Methods Mol. Biol. 372, 343-360.
    • (2007) Methods Mol. Biol. , vol.372 , pp. 343-360
    • Tatsuta, T.1    Langer, T.2
  • 26
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • DOI 10.1038/sj.emboj.7601972, PII 7601972
    • Tatsuta, T., and Langer, T. (2008). Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 27, 306-314. (Pubitemid 351161660)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 27
    • 28544434064 scopus 로고    scopus 로고
    • A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-kappaB
    • Tian, L., Holmgren, R. A., and Matouschek, A. (2005). A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-kappaB. Nat. Struct. Mol. Biol. 12, 1045-1053.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1045-1053
    • Tian, L.1    Holmgren, R.A.2    Matouschek, A.3
  • 28
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann, C., Neupert, W., and Cyr, D. M. (1994). The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266, 1250-1253. (Pubitemid 24371284)
    • (1994) Science , vol.266 , Issue.5188 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 29
    • 0031463338 scopus 로고    scopus 로고
    • Autocatalytic processing of the ATP-dependent PIM1 protease: Crucial function of a pro-region for sorting to mitochondria
    • Wagner, I., Van Dyck, L., Savel'ev, A., Neupert, W., and Langer, T. (1997). Autocatalytic processing of the ATP-dependent PIM1 protease: Crucial function of a pro-region for sorting to mitochondria. EMBO J. 16, 7317-7325.
    • (1997) EMBO J. , vol.16 , pp. 7317-7325
    • Wagner, I.1    Van Dyck, L.2    Savel'ev, A.3    Neupert, W.4    Langer, T.5
  • 30
    • 55749085411 scopus 로고    scopus 로고
    • Features and applications of blue-native and clear-native electrophoresis
    • Wittig, I., and Schägger, H. (2008). Features and applications of blue-native and clear-native electrophoresis. Proteomics 8, 3974-3990.
    • (2008) Proteomics , vol.8 , pp. 3974-3990
    • Wittig, I.1    Schägger, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.