메뉴 건너뛰기




Volumn 451, Issue 7176, 2008, Pages 363-367

Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin

Author keywords

[No Author keywords available]

Indexed keywords

SPASTIN;

EID: 38349097870     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06482     Document Type: Article
Times cited : (266)

References (34)
  • 1
    • 0032721512 scopus 로고    scopus 로고
    • Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia
    • Hazan, J. et al. Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia. Nature Genet. 23, 296-303 (1999).
    • (1999) Nature Genet , vol.23 , pp. 296-303
    • Hazan, J.1
  • 2
    • 1642343784 scopus 로고    scopus 로고
    • Phylogenetic analysis of AAA proteins
    • Frickey, T. & Lupas, A. N. Phylogenetic analysis of AAA proteins. J. Struct. Biol. 146, 2-10 (2004).
    • (2004) J. Struct. Biol , vol.146 , pp. 2-10
    • Frickey, T.1    Lupas, A.N.2
  • 3
    • 17144424690 scopus 로고    scopus 로고
    • The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules
    • Roll-Mecak, A. & Vale, R. D. The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules. Curr. Biol. 15, 650-655 (2005).
    • (2005) Curr. Biol , vol.15 , pp. 650-655
    • Roll-Mecak, A.1    Vale, R.D.2
  • 4
    • 13944283245 scopus 로고    scopus 로고
    • Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing
    • Evans, K. J., Gomes, E. R., Reisenweber, S. M., Gundersen, G. G. & Lauring, B. P. Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing. J. Cell Biol. 168, 599-606 (2005).
    • (2005) J. Cell Biol , vol.168 , pp. 599-606
    • Evans, K.J.1    Gomes, E.R.2    Reisenweber, S.M.3    Gundersen, G.G.4    Lauring, B.P.5
  • 5
    • 28844436513 scopus 로고    scopus 로고
    • Human spastin has multiple microtubule-related functions
    • Salinas, S. et al. Human spastin has multiple microtubule-related functions. J. Neurochem. 95, 1411-1420 (2005).
    • (2005) J. Neurochem , vol.95 , pp. 1411-1420
    • Salinas, S.1
  • 6
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F. J. & Vale, R. D. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75, 419-429 (1993).
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 7
    • 33845686334 scopus 로고    scopus 로고
    • Making more microtubules by severing: A common theme of noncentrosomal microtubule arrays?
    • Roll-Mecak, A. & Vale, R. D. Making more microtubules by severing: a common theme of noncentrosomal microtubule arrays? J. Cell Biol. 175, 849-851 (2006).
    • (2006) J. Cell Biol , vol.175 , pp. 849-851
    • Roll-Mecak, A.1    Vale, R.D.2
  • 8
    • 3142647116 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia gene, spastin, regulates microtubule stability to modulate synaptic structure and function
    • Trotta, N., Orso, G., Rossetto, M. G., Daga, A. & Broadie, K. The hereditary spastic paraplegia gene, spastin, regulates microtubule stability to modulate synaptic structure and function. Curr. Biol. 14, 1135-1147 (2004).
    • (2004) Curr. Biol , vol.14 , pp. 1135-1147
    • Trotta, N.1    Orso, G.2    Rossetto, M.G.3    Daga, A.4    Broadie, K.5
  • 9
    • 13944280702 scopus 로고    scopus 로고
    • Drosophila Spastin regulates synaptic microtubule networks and is required for normal motor function
    • Sherwood, N. T., Sun, Q., Xue, M., Zhang, B. & Zinn, K. Drosophila Spastin regulates synaptic microtubule networks and is required for normal motor function. PLoS Biol. 2, e429 (2004).
    • (2004) PLoS Biol , vol.2
    • Sherwood, N.T.1    Sun, Q.2    Xue, M.3    Zhang, B.4    Zinn, K.5
  • 10
    • 33748747401 scopus 로고    scopus 로고
    • The microtubule-severing protein Spastin is essential for axon outgrowth in the zebrafish embryo
    • Wood, J. D. et al. The microtubule-severing protein Spastin is essential for axon outgrowth in the zebrafish embryo. Hum. Mol. Genet. 15, 2763-2771 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2763-2771
    • Wood, J.D.1
  • 11
    • 0035032507 scopus 로고    scopus 로고
    • A katanin-like protein regulates normal cell wall biosynthesis and cell elongation
    • Burk, D. H., Liu, B., Zhong, R., Morrison, W. H. & Ye, Z. H. A katanin-like protein regulates normal cell wall biosynthesis and cell elongation. Plant Cell 13, 807-827 (2001).
    • (2001) Plant Cell , vol.13 , pp. 807-827
    • Burk, D.H.1    Liu, B.2    Zhong, R.3    Morrison, W.H.4    Ye, Z.H.5
  • 12
    • 0034192639 scopus 로고    scopus 로고
    • MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis
    • Srayko, M., Buster, D. W., Bazirgan, O. A., McNally, F. J. & Mains, P. E. MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis. Genes Dev. 14, 1072-1084 (2000).
    • (2000) Genes Dev , vol.14 , pp. 1072-1084
    • Srayko, M.1    Buster, D.W.2    Bazirgan, O.A.3    McNally, F.J.4    Mains, P.E.5
  • 13
    • 34247526438 scopus 로고    scopus 로고
    • Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromosomes
    • Zhang, D., Rogers, G. C., Buster, D. W. & Sharp, D. J. Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromosomes. J. Cell Biol. 177, 231-242 (2007).
    • (2007) J. Cell Biol , vol.177 , pp. 231-242
    • Zhang, D.1    Rogers, G.C.2    Buster, D.W.3    Sharp, D.J.4
  • 14
    • 33947713961 scopus 로고    scopus 로고
    • Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing
    • White, S. R., Evans, K. J., Lary, J., Cole, J. L. & Lauring, B. Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing. J. Cell Biol. 176, 995-1005 (2007).
    • (2007) J. Cell Biol , vol.176 , pp. 995-1005
    • White, S.R.1    Evans, K.J.2    Lary, J.3    Cole, J.L.4    Lauring, B.5
  • 15
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R. C., Hanson, P. I., Jahn, R. & Brunger, A. T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nature Struct. Biol. 5, 803-811 (1998).
    • (1998) Nature Struct. Biol , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 16
    • 0034163576 scopus 로고    scopus 로고
    • Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia
    • Fonknechten, N. et al. Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia. Hum. Mol. Genet. 9, 637-644 (2000).
    • (2000) Hum. Mol. Genet , vol.9 , pp. 637-644
    • Fonknechten, N.1
  • 17
    • 27144444327 scopus 로고    scopus 로고
    • Structural and mechanistic studies of VPS4 proteins
    • Scott, A. et al. Structural and mechanistic studies of VPS4 proteins. EMBO J. 24, 3658-3669 (2005).
    • (2005) EMBO J , vol.24 , pp. 3658-3669
    • Scott, A.1
  • 18
    • 34249723183 scopus 로고    scopus 로고
    • Matsushita-Ishiodori, Y., Yamanaka, K. & Ogura, T. The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules. Biochem. Biophys. Res. Commun. 359, 157-162 (2007).
    • Matsushita-Ishiodori, Y., Yamanaka, K. & Ogura, T. The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules. Biochem. Biophys. Res. Commun. 359, 157-162 (2007).
  • 19
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA(+) proteases and disassembly machines
    • Sauer, R. T. et al. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119, 9-18 (2004).
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1
  • 20
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman, J. J. & Vale, R. D. Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286, 782-785 (1999).
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 21
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V. & Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-2953 (2001).
    • (2001) Biophys. J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 22
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., Fenton, W. A., Furtak, K. J., Farr, G. W. & Horwich, A. L. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041 (2005).
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 23
    • 3042642040 scopus 로고    scopus 로고
    • Substrate recognition by the AAA+ chaperone ClpB
    • Schlieker, C. et al. Substrate recognition by the AAA+ chaperone ClpB. Nature Struct. Mol. Biol. 11, 607-615 (2004).
    • (2004) Nature Struct. Mol. Biol , vol.11 , pp. 607-615
    • Schlieker, C.1
  • 24
    • 0347990575 scopus 로고    scopus 로고
    • The Caenorhabditis elegans microtubule-severing complex MEI-1/MEI-2 katanin interacts differently with two superficially redundant beta-tubulin isotypes
    • Lu, C., Srayko, M. & Mains, P. E. The Caenorhabditis elegans microtubule-severing complex MEI-1/MEI-2 katanin interacts differently with two superficially redundant beta-tubulin isotypes. Mol. Biol. Cell 15, 142-150 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 142-150
    • Lu, C.1    Srayko, M.2    Mains, P.E.3
  • 25
    • 0021074286 scopus 로고
    • A rat monoclonal antibody reacting specifically with the tyrosylated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo
    • Wehland, J., Willingham, M. C. & Sandoval, I. V. A rat monoclonal antibody reacting specifically with the tyrosylated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo. J. Cell Biol. 97, 1467-1475 (1983).
    • (1983) J. Cell Biol , vol.97 , pp. 1467-1475
    • Wehland, J.1    Willingham, M.C.2    Sandoval, I.V.3
  • 26
    • 0018776206 scopus 로고
    • Tyrosination state of free tubulin subunits and tubulin disassembled from microtubules of rat brain tissue
    • Rodriguez, J. A. & Borisy, G. G. Tyrosination state of free tubulin subunits and tubulin disassembled from microtubules of rat brain tissue. Biochem. Biophys. Res. Commun. 89, 893-899 (1979).
    • (1979) Biochem. Biophys. Res. Commun , vol.89 , pp. 893-899
    • Rodriguez, J.A.1    Borisy, G.G.2
  • 27
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo
    • Gundersen, G. G., Kalnoski, M. H. & Bulinski, J. C. Distinct populations of microtubules: tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo. Cell 38, 779-789 (1984).
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 28
    • 1542283751 scopus 로고    scopus 로고
    • Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
    • Siddiqui, S. M., Sauer, R. T. & Baker, T. A. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes Dev. 18, 369-374 (2004).
    • (2004) Genes Dev , vol.18 , pp. 369-374
    • Siddiqui, S.M.1    Sauer, R.T.2    Baker, T.A.3
  • 29
    • 33846188909 scopus 로고    scopus 로고
    • Visualizing the ATPase cycle in a protein disaggregating machine: Structural basis for substrate binding by ClpB
    • Lee, S., Choi, J. M. & Tsai, F. T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol. Cell 25, 261-271 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 261-271
    • Lee, S.1    Choi, J.M.2    Tsai, F.T.3
  • 30
    • 33845353014 scopus 로고    scopus 로고
    • A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition
    • Tarrade, A. et al. A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition. Hum. Mol. Genet. 15, 3544-3558 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 3544-3558
    • Tarrade, A.1
  • 32
    • 0026910457 scopus 로고
    • Determination of the regulatization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. Determination of the regulatization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 (1992).
    • (1992) J. Appl. Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 33
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V. & Svergun, D. I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.