메뉴 건너뛰기




Volumn 27, Issue 2, 2007, Pages 758-767

Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia

Author keywords

[No Author keywords available]

Indexed keywords

AAA PROTEINASE; ADENOSINE TRIPHOSPHATASE; MITOCHONDRIAL ENZYME; PARAPLEGIN; UNCLASSIFIED DRUG;

EID: 33846127778     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01470-06     Document Type: Article
Times cited : (161)

References (36)
  • 2
    • 33744752749 scopus 로고    scopus 로고
    • The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1
    • Antonicka, H., F. Sasarman, N. G. Kennaway, and E. A. Shoubridge. 2006. The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1. Hum. Mol. Genet. 15:1835-1846.
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1835-1846
    • Antonicka, H.1    Sasarman, F.2    Kennaway, N.G.3    Shoubridge, E.A.4
  • 3
    • 0032541406 scopus 로고    scopus 로고
    • The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease
    • Arlt, H., G. Steglich, R. Perryman, B. Guiard, W. Neupert, and T. Langer. 1998. The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease. EMBO J. 17:4837-4847.
    • (1998) EMBO J , vol.17 , pp. 4837-4847
    • Arlt, H.1    Steglich, G.2    Perryman, R.3    Guiard, B.4    Neupert, W.5    Langer, T.6
  • 4
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12-complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • Arlt, H., R. Tauer, H. Feldmann, W. Neupert, and T. Langer. 1996. The YTA10-12-complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85:875-885.
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 5
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino, L., L. Silvestri, M. Koppen, L. Cassina, A. Ballabio, R. Marconi, T. Langer, and G. Casari. 2003. Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J. Cell Biol. 163:777-787.
    • (2003) J. Cell Biol , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3    Cassina, L.4    Ballabio, A.5    Marconi, R.6    Langer, T.7    Casari, G.8
  • 6
    • 13244298414 scopus 로고    scopus 로고
    • Characterization of peptides released from mitochondria: Evidence for constant proteolysis and peptide efflux
    • Augustin, S., M. Nolden, S. Müller, O. Hardt, I. Arnold, and T. Langer. 2005. Characterization of peptides released from mitochondria: evidence for constant proteolysis and peptide efflux. J. Biol. Chem. 280:2691-2699.
    • (2005) J. Biol. Chem , vol.280 , pp. 2691-2699
    • Augustin, S.1    Nolden, M.2    Müller, S.3    Hardt, O.4    Arnold, I.5    Langer, T.6
  • 9
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic organelles in disease, aging, and development
    • Chan, D. C. 2006. Mitochondria: dynamic organelles in disease, aging, and development. Cell 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 10
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • Chan, D. C. 2006. Mitochondrial fusion and fission in mammals. Annu. Rev. Cell Dev. Biol. 22:79-99.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 12
    • 0036424840 scopus 로고    scopus 로고
    • A novel two-step mechanism for removal of a mitochondrial signal sequence involves the m-AAA complex and the putative rhomboid protease Pcp1
    • Esser, K., B. Tursun, M. Ingenhoven, G. Michaelis, and E. Pratje. 2002. A novel two-step mechanism for removal of a mitochondrial signal sequence involves the m-AAA complex and the putative rhomboid protease Pcp1. J. Mol. Biol. 323:835-843.
    • (2002) J. Mol. Biol , vol.323 , pp. 835-843
    • Esser, K.1    Tursun, B.2    Ingenhoven, M.3    Michaelis, G.4    Pratje, E.5
  • 14
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner, F., L. J. Foster, S. Campanaro, G. Valle, and M. Mann. 2006. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell Proteomics 5:608-619.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 16
    • 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.
    • (2006) EMBO J , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 17
    • 0034666092 scopus 로고    scopus 로고
    • The mitochondrial inner membrane AAA metalloprotease family in metazoans
    • Juhola, M. K., Z. H. Shah, L. A. Grivell, and H. T. Jacobs. 2000. The mitochondrial inner membrane AAA metalloprotease family in metazoans. FEBS Lett. 481:91-95.
    • (2000) FEBS Lett , vol.481 , pp. 91-95
    • Juhola, M.K.1    Shah, Z.H.2    Grivell, L.A.3    Jacobs, H.T.4
  • 18
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., T. Inagawa, A. J. Wilkinson, T. Tatsuta, and T. Ogura. 1999. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274:26225-26232.
    • (1999) J. Biol. Chem , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 19
    • 4444332721 scopus 로고    scopus 로고
    • Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits
    • Korbel, D., S. Wurth, M. Kaser, and T. Langer. 2004. Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits. EMBO Rep. 5:698-703.
    • (2004) EMBO Rep , vol.5 , pp. 698-703
    • Korbel, D.1    Wurth, S.2    Kaser, M.3    Langer, T.4
  • 20
    • 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., A. E. Gardner, C. Settasatian, A. Savoia, G. R. Sutherland, and D. F. Callen. 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.
    • (2001) Genomics , vol.76 , pp. 58-65
    • Kremmidiotis, G.1    Gardner, A.E.2    Settasatian, C.3    Savoia, A.4    Sutherland, G.R.5    Callen, D.F.6
  • 21
    • 33745028132 scopus 로고    scopus 로고
    • The role of mitochondria in inherited neurodegenerative diseases
    • Kwong, J. Q., M. F. Beal, and G. Manfredi. 2006. The role of mitochondria in inherited neurodegenerative diseases. J. Neurochem. 97:1659-1675.
    • (2006) J. Neurochem , vol.97 , pp. 1659-1675
    • Kwong, J.Q.1    Beal, M.F.2    Manfredi, G.3
  • 22
    • 0033639076 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria: Extraction of substrates from either membrane surface
    • Leonhard, K., B. Guiard, G. Pellechia, A. Tzagoloff, W. Neupert, and T. Langer. 2000. Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol. Cell 5:629-638.
    • (2000) Mol. Cell , vol.5 , pp. 629-638
    • Leonhard, K.1    Guiard, B.2    Pellechia, G.3    Tzagoloff, A.4    Neupert, W.5    Langer, T.6
  • 23
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., A. McKenzie III, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 24
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi, M., M. D'Aurelio, C. D. Gajewski, K. Martushova, M. Kiaei, M. F. Beal, and G. Manfredi. 2002. Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem. 277:29626-29633.
    • (2002) J. Biol. Chem , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3    Martushova, K.4    Kiaei, M.5    Beal, M.F.6    Manfredi, G.7
  • 26
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden, M., S. Ehses, M. Koppen, A. Bernacchia, E. I. Rugarli, and T. Langer. 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
  • 28
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura, T., S. W. Whiteheart, and A. J. Wilkinson. 2004. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol. 146:106-112.
    • (2004) J. Struct. Biol , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 29
    • 33744970020 scopus 로고    scopus 로고
    • Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia
    • Rugarli, E. I., and T. Langer. 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
  • 30
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolated protein complexes from mitochondria
    • Schägger, H. 2001. Blue-native gels to isolated protein complexes from mitochondria. Methods Cell Biol. 65:231-244.
    • (2001) Methods Cell Biol , vol.65 , pp. 231-244
    • Schägger, H.1
  • 31
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich, G., W. Neupert, and T. Langer. 1999. Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol. Cell. Biol. 19:3435-3442.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 32
    • 33744552902 scopus 로고    scopus 로고
    • Structure of the whole cytosolic region of ATP-dependent protease FtsH
    • Suno, R., H. Niwa, D. Tsuchiya, X. Zhang, M. Yoshida, and K. Morikawa. 2006. Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol. Cell 22:575-585.
    • (2006) Mol. Cell , vol.22 , pp. 575-585
    • Suno, R.1    Niwa, H.2    Tsuchiya, D.3    Zhang, X.4    Yoshida, M.5    Morikawa, K.6
  • 33
    • 33846153029 scopus 로고    scopus 로고
    • Studying proteolysis within mitochondria
    • in press
    • Tatsuta, T., and T. Langer. Studying proteolysis within mitochondria. Curr. Top. Gen., in press.
    • Curr. Top. Gen
    • Tatsuta, T.1    Langer, T.2
  • 34
    • 33846490396 scopus 로고    scopus 로고
    • m-AAA protease-driven membrane dislocation allows intermembrane cleavage by rhomboid in mitochondria
    • in press
    • Tatsuta, T., S. Augustin, M. Nolden, B. Friedrich, and T. Langer. m-AAA protease-driven membrane dislocation allows intermembrane cleavage by rhomboid in mitochondria. EMBOJ. in press.
    • EMBOJ
    • Tatsuta, T.1    Augustin, S.2    Nolden, M.3    Friedrich, B.4    Langer, T.5
  • 35
    • 17744393686 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in human disease
    • Taylor, R. W., and D. M. Turnbull. 2005. Mitochondrial DNA mutations in human disease. Nat. Rev. Genet. 6:389-402.
    • (2005) Nat. Rev. Genet , vol.6 , pp. 389-402
    • Taylor, R.W.1    Turnbull, D.M.2
  • 36
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D. C. 1999. Mitochondrial diseases in man and mouse. Science 283:1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.