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Volumn 125, Issue 11, 2012, Pages 2561-2569

Microtubule-severing enzymes at the cutting edge

Author keywords

AAA atpase; Microtubule severing enzyme; Microtubules

Indexed keywords

ENZYME; FIDGETIN; GAMMA TUBULIN; KATANIN; MICROTUBULE PROTEIN; RAC PROTEIN; SPASTIN; TAU PROTEIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 84865037917     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.101139     Document Type: Article
Times cited : (172)

References (88)
  • 2
    • 0344603646 scopus 로고    scopus 로고
    • An essential role for katanin in severing microtubules in the neuron
    • Ahmad, F. J., Yu, W., McNally, F. J. and Baas, P. W. (1999). An essential role for katanin in severing microtubules in the neuron. J. Cell Biol. 145, 305-315.
    • (1999) J. Cell Biol. , vol.145 , pp. 305-315
    • Ahmad, F.J.1    Yu, W.2    McNally, F.J.3    Baas, P.W.4
  • 3
    • 16844379161 scopus 로고    scopus 로고
    • Neuronal microtubules: when the MAP is the roadblock
    • Baas, P. W. and Qiang, L. (2005). Neuronal microtubules: when the MAP is the roadblock. Trends Cell Biol. 15, 183-187.
    • (2005) Trends Cell Biol , vol.15 , pp. 183-187
    • Baas, P.W.1    Qiang, L.2
  • 5
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., Wendland, B., Estepa, E. J. and Emr, S. D. (1998). The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 6
    • 0030040856 scopus 로고    scopus 로고
    • The Ras-related GTPase Rac1 binds tubulin
    • Best, A., Ahmed, S., Kozma, R. and Lim, L. (1996). The Ras-related GTPase Rac1 binds tubulin. J. Biol. Chem. 271, 3756-3762.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3756-3762
    • Best, A.1    Ahmed, S.2    Kozma, R.3    Lim, L.4
  • 7
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop, N. and Woodman, P. (2000). ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell 11, 227-239.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 8
    • 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. and Ye, Z. H. (2001). A katanin-like protein regulates normal cell wall biosynthesis and cell elongation. Plant Cell 13, 807-827.
    • (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
  • 9
    • 0036500127 scopus 로고    scopus 로고
    • Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis
    • Buster, D., McNally, K. and McNally, F. J. (2002). Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis. J. Cell Sci. 115, 1083-1092.
    • (2002) J. Cell Sci. , vol.115 , pp. 1083-1092
    • Buster, D.1    McNally, K.2    McNally, F.J.3
  • 10
    • 34547748865 scopus 로고    scopus 로고
    • Poleward tubulin flux in spindles: regulation and function in mitotic cells
    • Buster, D. W., Zhang, D. and Sharp, D. J. (2007). Poleward tubulin flux in spindles: regulation and function in mitotic cells. Mol. Biol. Cell 18, 3094-3104.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3094-3104
    • Buster, D.W.1    Zhang, D.2    Sharp, D.J.3
  • 11
    • 78649313012 scopus 로고    scopus 로고
    • Genetic and chemical modulation of spastin-dependent axon outgrowth in zebrafish embryos indicates a role for impaired microtubule dynamics in hereditary spastic paraplegia
    • Butler, R., Wood, J. D., Landers, J. A. and Cunliffe, V. T. (2010). Genetic and chemical modulation of spastin-dependent axon outgrowth in zebrafish embryos indicates a role for impaired microtubule dynamics in hereditary spastic paraplegia. Dis. Model. Mech. 3, 743-751.
    • (2010) Dis. Model. Mech. , vol.3 , pp. 743-751
    • Butler, R.1    Wood, J.D.2    Landers, J.A.3    Cunliffe, V.T.4
  • 12
    • 0242609977 scopus 로고    scopus 로고
    • EB1 reveals mobile microtubule nucleation sites in Arabidopsis
    • Chan, J., Calder, G. M., Doonan, J. H. and Lloyd, C. W. (2003). EB1 reveals mobile microtubule nucleation sites in Arabidopsis. Nat. Cell Biol. 5, 967-971.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 967-971
    • Chan, J.1    Calder, G.M.2    Doonan, J.H.3    Lloyd, C.W.4
  • 13
    • 0027172949 scopus 로고
    • Genetic studies of mei-1 gene activity during the transition from meiosis to mitosis in Caenorhabditis elegans
    • Clandinin, T. R. and Mains, P. E. (1993). Genetic studies of mei-1 gene activity during the transition from meiosis to mitosis in Caenorhabditis elegans. Genetics 134, 199-210.
    • (1993) Genetics , vol.134 , pp. 199-210
    • Clandinin, T.R.1    Mains, P.E.2
  • 14
    • 0028236624 scopus 로고
    • Localization of the mei-1 gene product of Caenorhaditis elegans, a meiotic-specific spindle component
    • Clark-Maguire, S. and Mains, P. E. (1994a). Localization of the mei-1 gene product of Caenorhaditis elegans, a meiotic-specific spindle component. J. Cell Biol. 126, 199-209.
    • (1994) J. Cell Biol. , vol.126 , pp. 199-209
    • Clark-Maguire, S.1    Mains, P.E.2
  • 15
    • 0028147310 scopus 로고
    • mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases
    • Clark-Maguire, S. and Mains, P. E. (1994b). mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases. Genetics 136, 533-546.
    • (1994) Genetics , vol.136 , pp. 533-546
    • Clark-Maguire, S.1    Mains, P.E.2
  • 16
    • 0033775573 scopus 로고    scopus 로고
    • The mouse fidgetin gene defines a new role for AAA family proteins in mammalian development
    • Cox, G. A., Mahaffey, C. L., Nystuen, A., Letts, V. A. and Frankel, W. N. (2000). The mouse fidgetin gene defines a new role for AAA family proteins in mammalian development. Nat. Genet. 26, 198-202.
    • (2000) Nat. Genet. , vol.26 , pp. 198-202
    • Cox, G.A.1    Mahaffey, C.L.2    Nystuen, A.3    Letts, V.A.4    Frankel, W.N.5
  • 17
    • 0036112205 scopus 로고    scopus 로고
    • The importance of lattice defects in katanin-mediated microtubule severing in vitro
    • Davis, L. J., Odde, D. J., Block, S. M. and Gross, S. P. (2002). The importance of lattice defects in katanin-mediated microtubule severing in vitro. Biophys. J. 82, 2916-2927.
    • (2002) Biophys. J. , vol.82 , pp. 2916-2927
    • Davis, L.J.1    Odde, D.J.2    Block, S.M.3    Gross, S.P.4
  • 19
    • 4143093686 scopus 로고    scopus 로고
    • PF15p is the chlamydomonas homologue of the Katanin p80 subunit and is required for assembly of flagellar central microtubules
    • Dymek, E. E., Lefebvre, P. A. and Smith, E. F. (2004). PF15p is the chlamydomonas homologue of the Katanin p80 subunit and is required for assembly of flagellar central microtubules. Eukaryot. Cell 3, 870-879.
    • (2004) Eukaryot. Cell , vol.3 , pp. 870-879
    • Dymek, E.E.1    Lefebvre, P.A.2    Smith, E.F.3
  • 20
    • 5744240094 scopus 로고    scopus 로고
    • Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon
    • Errico, A., Claudiani, P., D'Addio, M. and Rugarli, E. I. (2004). Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon. Hum. Mol. Genet. 13, 2121-2132.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2121-2132
    • Errico, A.1    Claudiani, P.2    D'Addio, M.3    Rugarli, E.I.4
  • 21
    • 1642343784 scopus 로고    scopus 로고
    • Phylogenetic analysis of AAA proteins
    • Frickey, T. and Lupas, A. N. (2004). Phylogenetic analysis of AAA proteins. J. Struct. Biol. 146, 2-10.
    • (2004) J. Struct. Biol. , vol.146 , pp. 2-10
    • Frickey, T.1    Lupas, A.N.2
  • 22
    • 77957817006 scopus 로고    scopus 로고
    • Patronin regulates the microtubule network by protecting microtubule minus ends
    • Goodwin, S. S. and Vale, R. D. (2010). Patronin regulates the microtubule network by protecting microtubule minus ends. Cell 143, 263-274.
    • (2010) Cell , vol.143 , pp. 263-274
    • Goodwin, S.S.1    Vale, R.D.2
  • 23
    • 77958493799 scopus 로고    scopus 로고
    • Cell and molecular biology of microtubule plus end tracking proteins: end binding proteins and their partners
    • Gouveia, S. M. and Akhmanova, A. (2010). Cell and molecular biology of microtubule plus end tracking proteins: end binding proteins and their partners. Int. Rev. Cell. Mol. Biol. 285, 1-74.
    • (2010) Int. Rev. Cell. Mol. Biol. , vol.285 , pp. 1-74
    • Gouveia, S.M.1    Akhmanova, A.2
  • 24
    • 0002700029 scopus 로고
    • Two new mutant genes in the house mouse
    • Grüneberg, H. (1943). Two new mutant genes in the house mouse. J. Genet. 45, 22-28.
    • (1943) J. Genet. , vol.45 , pp. 22-28
    • Grüneberg, H.1
  • 26
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman, J. J. and Vale, R. D. (1999). Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286, 782-785.
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 27
    • 18344403503 scopus 로고    scopus 로고
    • Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
    • Hartman, J. J., Mahr, J., McNally, K., Okawa, K., Iwamatsu, A., Thomas, S., Cheesman, S., Heuser, J., Vale, R. D. and McNally, F. J. (1998). Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell 93, 277-287.
    • (1998) Cell , vol.93 , pp. 277-287
    • Hartman, J.J.1    Mahr, J.2    McNally, K.3    Okawa, K.4    Iwamatsu, A.5    Thomas, S.6    Cheesman, S.7    Heuser, J.8    Vale, R.D.9    McNally, F.J.10
  • 29
    • 37049025567 scopus 로고    scopus 로고
    • Knot/Collier and cut control different aspects of dendrite cytoskeleton and synergize to define final arbor shape
    • Jinushi-Nakao, S., Arvind, R., Amikura, R., Kinameri, E., Liu, A. W. and Moore, A. W. (2007). Knot/Collier and cut control different aspects of dendrite cytoskeleton and synergize to define final arbor shape. Neuron 56, 963-978.
    • (2007) Neuron , vol.56 , pp. 963-978
    • Jinushi-Nakao, S.1    Arvind, R.2    Amikura, R.3    Kinameri, E.4    Liu, A.W.5    Moore, A.W.6
  • 30
    • 3042853307 scopus 로고    scopus 로고
    • Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules
    • Karabay, A., Yu, W., Solowska, J. M., Baird, D. H. and Baas, P. W. (2004). Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules. J. Neurosci. 24, 5778-5788.
    • (2004) J. Neurosci. , vol.24 , pp. 5778-5788
    • Karabay, A.1    Yu, W.2    Solowska, J.M.3    Baird, D.H.4    Baas, P.W.5
  • 32
    • 65549090937 scopus 로고    scopus 로고
    • Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamor-phosis
    • Lee, H. H., Jan, L. Y. and Jan, Y. N. (2009). Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamor-phosis. Proc. Natl. Acad. Sci. USA 106, 6363-6368.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6363-6368
    • Lee, H.H.1    Jan, L.Y.2    Jan, Y.N.3
  • 33
    • 0031719188 scopus 로고    scopus 로고
    • A role for katanin-mediated axonemal severing during Chlamydomonas deflagellation
    • Lohret, T. A., McNally, F. J. and Quarmby, L. M. (1998). A role for katanin-mediated axonemal severing during Chlamydomonas deflagellation. Mol. Biol. Cell 9, 1195-1207.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1195-1207
    • Lohret, T.A.1    McNally, F.J.2    Quarmby, L.M.3
  • 34
    • 33846799159 scopus 로고    scopus 로고
    • The C. elegans anaphase promoting complex and MBK-2/DYRK kinase act redundantly with CUL-3/MEL-26 ubiquitin ligase to degrade MEI-1 microtubule-severing activity after meiosis
    • Lu, C. and Mains, P. E. (2007). The C. elegans anaphase promoting complex and MBK-2/DYRK kinase act redundantly with CUL-3/MEL-26 ubiquitin ligase to degrade MEI-1 microtubule-severing activity after meiosis. Dev. Biol. 302, 438-447.
    • (2007) Dev. Biol. , vol.302 , pp. 438-447
    • Lu, C.1    Mains, P.E.2
  • 36
    • 0025119673 scopus 로고
    • Mutations affecting the meiotic and mitotic divisions of the early Caenorhabditis elegans embryo
    • Mains, P. E., Kemphues, K. J., Sprunger, S. A., Sulston, I. A. and Wood, W. B. (1990). Mutations affecting the meiotic and mitotic divisions of the early Caenorhabditis elegans embryo. Genetics 126, 593-605.
    • (1990) Genetics , vol.126 , pp. 593-605
    • Mains, P.E.1    Kemphues, K.J.2    Sprunger, S.A.3    Sulston, I.A.4    Wood, W.B.5
  • 37
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F. J. and Vale, R. D. (1993). Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75, 419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 38
    • 79955487783 scopus 로고    scopus 로고
    • The spindle assembly function of Caenorhabditis elegans katanin does not require microtubule-severing activity
    • McNally, K. P. and McNally, F. J. (2011). The spindle assembly function of Caenorhabditis elegans katanin does not require microtubule-severing activity. Mol. Biol. Cell 22, 1550-1560.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1550-1560
    • McNally, K.P.1    McNally, F.J.2
  • 39
    • 33845713718 scopus 로고    scopus 로고
    • Katanin controls mitotic and meiotic spindle length
    • McNally, K., Audhya, A., Oegema, K. and McNally, F. J. (2006). Katanin controls mitotic and meiotic spindle length. J. Cell Biol. 175, 881-891.
    • (2006) J. Cell Biol. , vol.175 , pp. 881-891
    • McNally, K.1    Audhya, A.2    Oegema, K.3    McNally, F.J.4
  • 40
    • 0036890208 scopus 로고    scopus 로고
    • Katanin-mediated microtubule severing can be regulated by multiple mechanisms
    • McNally, K. P., Buster, D. and McNally, F. J. (2002). Katanin-mediated microtubule severing can be regulated by multiple mechanisms. Cell Motil. Cytoskeleton 53, 337-349.
    • (2002) Cell Motil. Cytoskeleton , vol.53 , pp. 337-349
    • McNally, K.P.1    Buster, D.2    McNally, F.J.3
  • 41
    • 14744287039 scopus 로고    scopus 로고
    • Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase
    • Mennella, V., Rogers, G. C., Rogers, S. L., Buster, D. W., Vale, R. D. and Sharp, D. J. (2005). Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase. Nat. Cell Biol. 7, 235-245.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 235-245
    • Mennella, V.1    Rogers, G.C.2    Rogers, S.L.3    Buster, D.W.4    Vale, R.D.5    Sharp, D.J.6
  • 43
    • 27144543017 scopus 로고    scopus 로고
    • Microtubule-dependent microtubule nucleation based on recruitment of gamma-tubulin in higher plants
    • Murata, T., Sonobe, S., Baskin, T. I., Hyodo, S., Hasezawa, S., Nagata, T., Horio, T. and Hasebe, M. (2005). Microtubule-dependent microtubule nucleation based on recruitment of gamma-tubulin in higher plants. Nat. Cell Biol. 7, 961-968.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 961-968
    • Murata, T.1    Sonobe, S.2    Baskin, T.I.3    Hyodo, S.4    Hasezawa, S.5    Nagata, T.6    Horio, T.7    Hasebe, M.8
  • 44
    • 78149281358 scopus 로고    scopus 로고
    • Microtubule and katanin-dependent dynamics of microtubule nucleation complexes in the acentrosomal Arabidopsis cortical array
    • Nakamura, M., Ehrhardt, D. W. and Hashimoto, T. (2010). Microtubule and katanin-dependent dynamics of microtubule nucleation complexes in the acentrosomal Arabidopsis cortical array. Nat. Cell Biol. 12, 1064-1070.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1064-1070
    • Nakamura, M.1    Ehrhardt, D.W.2    Hashimoto, T.3
  • 45
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. and Koonin, E. V. (1999). AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 46
    • 33645221487 scopus 로고    scopus 로고
    • Tau protects microtubules in the axon from severing by katanin
    • Qiang, L., Yu, W., Andreadis, A., Luo, M. and Baas, P. W. (2006). Tau protects microtubules in the axon from severing by katanin. J. Neurosci. 26, 3120-3129.
    • (2006) J. Neurosci. , vol.26 , pp. 3120-3129
    • Qiang, L.1    Yu, W.2    Andreadis, A.3    Luo, M.4    Baas, P.W.5
  • 47
    • 75649119687 scopus 로고    scopus 로고
    • Basic fibroblast growth factor elicits formation of interstitial axonal branches via enhanced severing of microtubules
    • Qiang, L., Yu, W., Liu, M., Solowska, J. M. and Baas, P. W. (2010). Basic fibroblast growth factor elicits formation of interstitial axonal branches via enhanced severing of microtubules. Mol. Biol. Cell 21, 334-344.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 334-344
    • Qiang, L.1    Yu, W.2    Liu, M.3    Solowska, J.M.4    Baas, P.W.5
  • 48
    • 63049095708 scopus 로고    scopus 로고
    • Katanin knockdown supports a role for microtubule severing in release of basal bodies before mitosis in Chlamydomonas
    • Rasi, M. Q., Parker, J. D., Feldman, J. L., Marshall, W. F. and Quarmby, L. M. (2009). Katanin knockdown supports a role for microtubule severing in release of basal bodies before mitosis in Chlamydomonas. Mol. Biol. Cell 20, 379-388.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 379-388
    • Rasi, M.Q.1    Parker, J.D.2    Feldman, J.L.3    Marshall, W.F.4    Quarmby, L.M.5
  • 49
    • 79958723408 scopus 로고    scopus 로고
    • The molecular basis of anaphase A in animal cells
    • Rath, U. and Sharp, D. J. (2011). The molecular basis of anaphase A in animal cells. Chromosome Res. 19, 423-432.
    • (2011) Chromosome Res , vol.19 , pp. 423-432
    • Rath, U.1    Sharp, D.J.2
  • 51
  • 52
    • 17144424690 scopus 로고    scopus 로고
    • The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules
    • Roll-Mecak, A. and Vale, R. D. (2005). The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules. Curr. Biol. 15, 650-655.
    • (2005) Curr. Biol. , vol.15 , pp. 650-655
    • Roll-Mecak, A.1    Vale, R.D.2
  • 53
    • 33845686334 scopus 로고    scopus 로고
    • Making more microtubules by severing: a common theme of noncentrosomal microtubule arrays? J
    • Roll-Mecak, A. and Vale, R. D. (2006). Making more microtubules by severing: a common theme of noncentrosomal microtubule arrays? J. Cell Biol. 175, 849-851.
    • (2006) Cell Biol , vol.175 , pp. 849-851
    • Roll-Mecak, A.1    Vale, R.D.2
  • 54
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak, A. and Vale, R. D. (2008). Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451, 363-367.
    • (2008) Nature , vol.451 , pp. 363-367
    • Roll-Mecak, A.1    Vale, R.D.2
  • 56
    • 31144453436 scopus 로고    scopus 로고
    • Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners
    • Sanderson, C. M., Connell, J. W., Edwards, T. L., Bright, N. A., Duley, S., Thompson, A., Luzio, J. P. and Reid, E. (2006). Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners. Hum. Mol. Genet. 15, 307-318.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 307-318
    • Sanderson, C.M.1    Connell, J.W.2    Edwards, T.L.3    Bright, N.A.4    Duley, S.5    Thompson, A.6    Luzio, J.P.7    Reid, E.8
  • 57
    • 77957969314 scopus 로고    scopus 로고
    • Making the final cut -mechanisms mediating the abscission step of cytokinesis
    • Schiel, J. A. and Prekeris, R. (2010). Making the final cut -mechanisms mediating the abscission step of cytokinesis. Scientific World Journal 10, 1424-1434.
    • (2010) Scientific World Journal , vol.10 , pp. 1424-1434
    • Schiel, J.A.1    Prekeris, R.2
  • 59
    • 0038518182 scopus 로고    scopus 로고
    • Sustained microtubule treadmilling in Arabidopsis cortical arrays
    • Shaw, S. L., Kamyar, R. and Ehrhardt, D. W. (2003). Sustained microtubule treadmilling in Arabidopsis cortical arrays. Science 300, 1715-1718.
    • (2003) Science , vol.300 , pp. 1715-1718
    • Shaw, S.L.1    Kamyar, R.2    Ehrhardt, D.W.3
  • 60
    • 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. and Zinn, K. (2004). Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function. PLoS Biol. 2, e429.
    • (2004) PLoS Biol , vol.2
    • Sherwood, N.T.1    Sun, Q.2    Xue, M.3    Zhang, B.4    Zinn, K.5
  • 61
    • 39849101639 scopus 로고    scopus 로고
    • Quantitative and functional analyses of spastin in the nervous system: implications for hereditary spastic paraplegia
    • Solowska, J. M., Morfini, G., Falnikar, A., Himes, B. T., Brady, S. T., Huang, D. and Baas, P. W. (2008). Quantitative and functional analyses of spastin in the nervous system: implications for hereditary spastic paraplegia. J. Neurosci. 28, 2147-2157.
    • (2008) J. Neurosci. , vol.28 , pp. 2147-2157
    • Solowska, J.M.1    Morfini, G.2    Falnikar, A.3    Himes, B.T.4    Brady, S.T.5    Huang, D.6    Baas, P.W.7
  • 62
    • 77954168257 scopus 로고    scopus 로고
    • KL1 is a novel microtubule severing enzyme that regulates mitotic spindle architecture
    • Sonbuchner, T. M., Rath, U. and Sharp, D. J. (2010). KL1 is a novel microtubule severing enzyme that regulates mitotic spindle architecture. Cell Cycle 9, 2403-2411.
    • (2010) Cell Cycle , vol.9 , pp. 2403-2411
    • Sonbuchner, T.M.1    Rath, U.2    Sharp, D.J.3
  • 63
    • 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. and Mains, P. E. (2000). MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis. Genes Dev. 14, 1072-1084.
    • (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
  • 64
    • 33749239641 scopus 로고    scopus 로고
    • Katanin disrupts the microtubule lattice and increases polymer number in C. elegans meiosis
    • Srayko, M., O'Toole, E. T., Hypman, A. A. and Muller-Reichert, T. (2006). Katanin disrupts the microtubule lattice and increases polymer number in C. elegans meiosis. Curr. Biol. 16, 1944-1949.
    • (2006) Curr. Biol. , vol.16 , pp. 1944-1949
    • Srayko, M.1    O'Toole, E.T.2    Hypman, A.A.3    Muller-Reichert, T.4
  • 65
    • 33745209613 scopus 로고    scopus 로고
    • Katanin's severing activity favors bundling of cortical microtubules in plants
    • Stoppin-Mellet, V., Gaillard, J. and Vantard, M. (2006). Katanin's severing activity favors bundling of cortical microtubules in plants. Plant J. 46, 1009-1017.
    • (2006) Plant J , vol.46 , pp. 1009-1017
    • Stoppin-Mellet, V.1    Gaillard, J.2    Vantard, M.3
  • 66
    • 34347403453 scopus 로고    scopus 로고
    • LAPSER1 is a putative cytokinetic tumor suppressor that shows the same centrosome and midbody subcellular localization pattern as p80 katanin
    • Sudo, H. and Maru, Y. (2007). LAPSER1 is a putative cytokinetic tumor suppressor that shows the same centrosome and midbody subcellular localization pattern as p80 katanin. FASEB J. 21, 2086-2100.
    • (2007) FASEB J , vol.21 , pp. 2086-2100
    • Sudo, H.1    Maru, Y.2
  • 67
    • 48249139375 scopus 로고    scopus 로고
    • LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the inhibition of katanin-mediated microtubule severing
    • Sudo, H. and Maru, Y. (2008). LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the inhibition of katanin-mediated microtubule severing. Hum. Mol. Genet. 17, 2524-2540.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2524-2540
    • Sudo, H.1    Maru, Y.2
  • 68
    • 77953046399 scopus 로고    scopus 로고
    • Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts
    • Sudo, H. and Baas, P. W. (2010). Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts. J. Neurosci. 30, 7215-7226.
    • (2010) J. Neurosci. , vol.30 , pp. 7215-7226
    • Sudo, H.1    Baas, P.W.2
  • 69
    • 78751685767 scopus 로고    scopus 로고
    • Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases
    • Sudo, H. and Baas, P. W. (2011). Strategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases. Hum. Mol. Genet. 20, 763-778.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 763-778
    • Sudo, H.1    Baas, P.W.2
  • 70
    • 27744560966 scopus 로고    scopus 로고
    • Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration
    • Toyo-Oka, K., Sasaki, S., Yano, Y., Mori, D., Kobayashi, T., Toyoshima, Y. Y., Tokuoka, S. M., Ishii, S., Shimizu, T., Muramatsu, M. et al. (2005). Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration. Hum. Mol. Genet. 14, 3113-3128.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3113-3128
    • Toyo-Oka, K.1    Sasaki, S.2    Yano, Y.3    Mori, D.4    Kobayashi, T.5    Toyoshima, Y.Y.6    Tokuoka, S.M.7    Ishii, S.8    Shimizu, T.9    Muramatsu, M.10
  • 71
    • 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. and Broadie, K. (2004). The hereditary spastic paraplegia gene, spastin, regulates microtubule stability to modulate synaptic structure and function. Curr. Biol. 14, 1135-1147.
    • (2004) Curr. Biol. , vol.14 , pp. 1135-1147
    • Trotta, N.1    Orso, G.2    Rossetto, M.G.3    Daga, A.4    Broadie, K.5
  • 72
    • 77951513241 scopus 로고
    • The anatomy and development of the fidget mouse
    • Truslove, G. M. (1956). The anatomy and development of the fidget mouse. J. Genet. 54, 64-86.
    • (1956) J. Genet. , vol.54 , pp. 64-86
    • Truslove, G.M.1
  • 73
    • 0026016405 scopus 로고
    • Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts
    • Vale, R. D. (1991). Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts. Cell 64, 827-839.
    • (1991) Cell , vol.64 , pp. 827-839
    • Vale, R.D.1
  • 74
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins Lords of the ring
    • Vale, R. D. (2000). AAA proteins. Lords of the ring. J. Cell Biol. 150, F13-F19.
    • (2000) J. Cell Biol. , vol.150
    • Vale, R.D.1
  • 75
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • Verhey, K. J. and Gaertig, J. (2007). The tubulin code. Cell Cycle 6, 2152-2160.
    • (2007) Cell Cycle , vol.6 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 76
    • 13244269913 scopus 로고    scopus 로고
    • Regulation of microtubules in cell migration
    • Watanabe, T., Noritake, J. and Kaibuchi, K. (2005). Regulation of microtubules in cell migration. Trends Cell Biol. 15, 76-83.
    • (2005) Trends Cell Biol , vol.15 , pp. 76-83
    • Watanabe, T.1    Noritake, J.2    Kaibuchi, K.3
  • 78
    • 0242693281 scopus 로고    scopus 로고
    • The cellular and molecular pathology of the motor system in hereditary spastic paraparesis due to mutation of the spastin gene
    • Wharton, S. B., McDermott, C. J., Grierson, A. J., Wood, J. D., Gelsthorpe, C., Ince, P. G. and Shaw, P. J. (2003). The cellular and molecular pathology of the motor system in hereditary spastic paraparesis due to mutation of the spastin gene. J. Neuropathol. Exp. Neurol. 62, 1166-1177.
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 1166-1177
    • Wharton, S.B.1    McDermott, C.J.2    Grierson, A.J.3    Wood, J.D.4    Gelsthorpe, C.5    Ince, P.G.6    Shaw, P.J.7
  • 79
    • 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. and Lauring, B. (2007). 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) 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
  • 80
    • 13544259741 scopus 로고    scopus 로고
    • Functional characterization of fidgetin, an AAA-family protein mutated in fidget mice
    • Yang, Y., Mahaffey, C. L., Bérubé, N., Nystuen, A. and Frankel, W. N. (2005). Functional characterization of fidgetin, an AAA-family protein mutated in fidget mice. Exp. Cell Res. 304, 50-58.
    • (2005) Exp. Cell Res. , vol.304 , pp. 50-58
    • Yang, Y.1    Mahaffey, C.L.2    Bérubé, N.3    Nystuen, A.4    Frankel, W.N.5
  • 81
    • 33746790622 scopus 로고    scopus 로고
    • Interaction between fidgetin and protein kinase A-anchoring protein AKAP95 is critical for palatogenesis in the mouse
    • Yang, Y., Mahaffey, C. L., Bérubé, N. and Frankel, W. N. (2006). Interaction between fidgetin and protein kinase A-anchoring protein AKAP95 is critical for palatogenesis in the mouse. J. Biol. Chem. 281, 22352-22359.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22352-22359
    • Yang, Y.1    Mahaffey, C.L.2    Bérubé, N.3    Frankel, W.N.4
  • 84
    • 0027990996 scopus 로고
    • Microtubule fragmentation and partitioning in the axon during collateral branch formation
    • Yu, W., Ahmad, F. J. and Baas, P. W. (1994). Microtubule fragmentation and partitioning in the axon during collateral branch formation. J. Neurosci. 14, 5872-5884.
    • (1994) J. Neurosci. , vol.14 , pp. 5872-5884
    • Yu, W.1    Ahmad, F.J.2    Baas, P.W.3
  • 85
    • 20444363058 scopus 로고    scopus 로고
    • Regulation of microtubule severing by katanin subunits during neuronal development
    • Yu, W., Solowska, J. M., Qiang, L., Karabay, A., Baird, D. and Baas, P. W. (2005). Regulation of microtubule severing by katanin subunits during neuronal development. J. Neurosci. 25, 5573-5583.
    • (2005) J. Neurosci. , vol.25 , pp. 5573-5583
    • Yu, W.1    Solowska, J.M.2    Qiang, L.3    Karabay, A.4    Baird, D.5    Baas, P.W.6
  • 86
    • 44949204601 scopus 로고    scopus 로고
    • The microtubule-severing proteins spastin and katanin participate differently in the formation of axonal branches
    • Yu, W., Qiang, L., Solowska, J. M., Karabay, A., Korulu, S. and Baas, P. W. (2008). The microtubule-severing proteins spastin and katanin participate differently in the formation of axonal branches. Mol. Biol. Cell 19, 1485-1498.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1485-1498
    • Yu, W.1    Qiang, L.2    Solowska, J.M.3    Karabay, A.4    Korulu, S.5    Baas, P.W.6
  • 87
    • 34247526438 scopus 로고    scopus 로고
    • Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromo-somes
    • Zhang, D., Rogers, G. C., Buster, D. W. and Sharp, D. J. (2007). Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromo-somes. J. Cell Biol. 177, 231-242.
    • (2007) J. Cell Biol. , vol.177 , pp. 231-242
    • Zhang, D.1    Rogers, G.C.2    Buster, D.W.3    Sharp, D.J.4


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