메뉴 건너뛰기




Volumn 44, Issue 2, 2012, Pages 266-274

Interplay between microtubule dynamics and intracellular organization

Author keywords

Cellular organization; Microtubule dynamics; Organelles; Polarization; Tubulin

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; TUBULIN;

EID: 84855602576     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2011.11.009     Document Type: Review
Times cited : (193)

References (136)
  • 1
    • 0029093287 scopus 로고
    • Microtubules released from the neuronal centrosome are transported into the axon
    • F.J. Ahmad, and P.W. Baas Microtubules released from the neuronal centrosome are transported into the axon J Cell Sci 108 Pt 8 1995 2761 2769
    • (1995) J Cell Sci , vol.108 , Issue.PART 8 , pp. 2761-2769
    • Ahmad, F.J.1    Baas, P.W.2
  • 2
    • 0032567765 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon
    • DOI 10.1083/jcb.140.2.391
    • F.J. Ahmad, C.J. Echeverri, R.B. Vallee, and P.W. Baas Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon J Cell Biol 140 1998 391 401 (Pubitemid 28078402)
    • (1998) Journal of Cell Biology , vol.140 , Issue.2 , pp. 391-401
    • Ahmad, F.J.1    Echeverri, C.J.2    Vallee, R.B.3    Baas, P.W.4
  • 3
    • 0344603646 scopus 로고    scopus 로고
    • An essential role for katanin in severing microtubules in the neuron
    • DOI 10.1083/jcb.145.2.305
    • F.J. Ahmad, W. Yu, F.J. McNally, and P.W. Baas An essential role for katanin in severing microtubules in the neuron J Cell Biol 145 1999 305 315 (Pubitemid 29198303)
    • (1999) Journal of Cell Biology , vol.145 , Issue.2 , pp. 305-315
    • Ahmad, F.J.1    Yu, W.2    McNally, F.J.3    Baas, P.W.4
  • 6
    • 77957881380 scopus 로고    scopus 로고
    • Microtubule +TIPs at a glance
    • A. Akhmanova, and M.O. Steinmetz Microtubule +TIPs at a glance J Cell Sci 123 2010 3415 3419
    • (2010) J Cell Sci , vol.123 , pp. 3415-3419
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 7
    • 77955588492 scopus 로고    scopus 로고
    • CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule
    • J. Al-Bassam, H. Kim, G. Brouhard, A. van Oijen, S.C. Harrison, and F. Chang CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule Dev Cell 19 2010 245 258
    • (2010) Dev Cell , vol.19 , pp. 245-258
    • Al-Bassam, J.1    Kim, H.2    Brouhard, G.3    Van Oijen, A.4    Harrison, S.C.5    Chang, F.6
  • 10
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dendrite
    • P.W. Baas, J.S. Deitch, M.M. Black, and G.A. Banker Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dendrite Proc Natl Acad Sci U S A 85 1988 8335 8339
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8335-8339
    • Baas, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 11
    • 70350490026 scopus 로고    scopus 로고
    • Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases
    • R. Ban, H. Matsuzaki, T. Akashi, G. Sakashita, H. Taniguchi, and S.-Y. Park Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases J Biol Chem 284 2009 28367 28381
    • (2009) J Biol Chem , vol.284 , pp. 28367-28381
    • Ban, R.1    Matsuzaki, H.2    Akashi, T.3    Sakashita, G.4    Taniguchi, H.5    Park, S.-Y.6
  • 12
    • 33751191831 scopus 로고    scopus 로고
    • Generation of noncentrosomal microtubule arrays
    • DOI 10.1242/jcs.03227
    • F. Bartolini, and G.G. Gundersen Generation of noncentrosomal microtubule arrays J Cell Sci 119 2006 4155 4163 (Pubitemid 44774022)
    • (2006) Journal of Cell Science , vol.119 , Issue.20 , pp. 4155-4163
    • Bartolini, F.1    Gundersen, G.G.2
  • 13
    • 0037059611 scopus 로고    scopus 로고
    • Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina
    • DOI 10.1016/S0092-8674(01)00627-4
    • J.L. Beaudouin, D. Gerlich, N. Daigle, R. Eils, and J. Ellenberg Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina Cell 108 2002 83 96 (Pubitemid 34137014)
    • (2002) Cell , vol.108 , Issue.1 , pp. 83-96
    • Beaudouin, J.1    Gerlich, D.2    Daigle, N.3    Eils, R.4    Ellenberg, J.5
  • 14
    • 70349417837 scopus 로고    scopus 로고
    • Microtubule plus-end and minus-end capture at adherens junctions is involved in the assembly of apico-basal arrays in polarised epithelial cells
    • G. Bellett, J.M. Carter, J. Keynton, D. Goldspink, C. James, and D.K. Moss Microtubule plus-end and minus-end capture at adherens junctions is involved in the assembly of apico-basal arrays in polarised epithelial cells Cell Motil Cytoskeleton 66 2009 893 908
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 893-908
    • Bellett, G.1    Carter, J.M.2    Keynton, J.3    Goldspink, D.4    James, C.5    Moss, D.K.6
  • 15
    • 0029998419 scopus 로고    scopus 로고
    • Catastrophic revelations about Op18/stathmin
    • DOI 10.1016/0968-0004(96)30021-2
    • L. Belmont, T. Mitchison, and H.W. Deacon Catastrophic revelations about Op18/stathmin Trends Biochem Sci 21 1996 197 198 (Pubitemid 26191221)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.6 , pp. 197-198
    • Belmont, L.1    Mitchison, T.2    Deacon, H.W.3
  • 16
    • 0035918287 scopus 로고    scopus 로고
    • Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation
    • C. Bonnet, D. Boucher, S. Lazereg, B. Pedrotti, K. Islam, and P. Denoulet Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation J Biol Chem 276 2001 12839 12848
    • (2001) J Biol Chem , vol.276 , pp. 12839-12848
    • Bonnet, C.1    Boucher, D.2    Lazereg, S.3    Pedrotti, B.4    Islam, K.5    Denoulet, P.6
  • 18
    • 79961115058 scopus 로고    scopus 로고
    • Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia
    • J.R. Bowen, D. Hwang, X. Bai, D. Roy, and E.T. Spiliotis Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia J Cell Biol 194 2011 187 197
    • (2011) J Cell Biol , vol.194 , pp. 187-197
    • Bowen, J.R.1    Hwang, D.2    Bai, X.3    Roy, D.4    Spiliotis, E.T.5
  • 20
    • 11244278743 scopus 로고    scopus 로고
    • Reorganization of microtubule nucleation during muscle differentiation
    • DOI 10.1002/cm.20042
    • E. Bugnard, K.J. Zaal, and E. Ralston Reorganization of microtubule nucleation during muscle differentiation Cell Motil Cytoskeleton 60 2005 1 13 (Pubitemid 40066222)
    • (2005) Cell Motility and the Cytoskeleton , vol.60 , Issue.1 , pp. 1-13
    • Bugnard, E.1    Zaal, K.J.M.2    Ralston, E.3
  • 21
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • DOI 10.1083/jcb.139.2.469
    • J.K. Burkhardt, C.J. Echeverri, T. Nilsson, and R.B. Vallee Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution J Cell Biol 139 1997 469 484 (Pubitemid 27459318)
    • (1997) Journal of Cell Biology , vol.139 , Issue.2 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 22
    • 0035166773 scopus 로고    scopus 로고
    • Single site α-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: Possible role for palmitoylation of α-tubulin
    • J.M. Caron, L.R. Vega, J. Fleming, R. Bishop, and F. Solomon Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: possible role for palmitoylation of alpha-tubulin Mol Biol Cell 12 2001 2672 2687 (Pubitemid 33051933)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.9 , pp. 2672-2687
    • Caron, J.M.1    Vega, L.R.2    Fleming, J.3    Bishop, R.4    Solomon, F.5
  • 24
    • 47549090803 scopus 로고    scopus 로고
    • CLASP regulates mitochondrial distribution in Schizosaccharomyces pombe
    • DOI 10.1083/jcb.200712147
    • S. Chiron, A. Bobkova, H. Zhou, and M. Yaffe CLASP regulates mitochondrial distribution in Schizosaccharomyces pombe J Cell Biol 182 1 2008 41 49 (Pubitemid 352008620)
    • (2008) Journal of Cell Biology , vol.182 , Issue.1 , pp. 41-49
    • Chiron, S.1    Bobkova, A.2    Zhou, H.3    Yaffe, M.P.4
  • 25
    • 0036774805 scopus 로고    scopus 로고
    • The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase
    • DOI 10.1093/embo-reports/kvf197
    • J.H. Choi, P.G. Bertram, R. Drenan, J. Carvalho, H.H. Zhou, and X.F.S. Zheng The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase EMBO Rep 3 2002 988 994 (Pubitemid 35256474)
    • (2002) EMBO Reports , vol.3 , Issue.10 , pp. 988-994
    • Choi, J.H.1    Bertram, P.G.2    Drenan, R.3    Carvalho, J.4    Zhou, H.H.5    Zheng, X.F.S.6
  • 26
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • N.B. Cole, N. Sciaky, A. Marotta, J. Song, and J. Lippincott-Schwartz Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites Mol Biol Cell 7 1996 631 650 (Pubitemid 26112568)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.4 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 28
    • 77955330151 scopus 로고    scopus 로고
    • Myc-nick: A cytoplasmic cleavage product of Myc that promotes alpha-tubulin acetylation and cell differentiation
    • M. Conacci-Sorrell, C. Ngouenet, and R.N. Eisenman Myc-nick: a cytoplasmic cleavage product of Myc that promotes alpha-tubulin acetylation and cell differentiation Cell 142 2010 480 493
    • (2010) Cell , vol.142 , pp. 480-493
    • Conacci-Sorrell, M.1    Ngouenet, C.2    Eisenman, R.N.3
  • 29
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons thrhough acetylation of alpha-tubulin
    • C. Creppe, L. Malinouskaya, M.L. Volvert, M. Gillard, P. Close, and O. Malaise Elongator controls the migration and differentiation of cortical neurons thrhough acetylation of alpha-tubulin Cell 136 3 2009 551 564
    • (2009) Cell , vol.136 , Issue.3 , pp. 551-564
    • Creppe, C.1    Malinouskaya, L.2    Volvert, M.L.3    Gillard, M.4    Close, P.5    Malaise, O.6
  • 30
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • DOI 10.1074/jbc.C000635200
    • H. Daub, K. Gevaert, J. Vandekerckhove, A. Sobel, and A. Hall Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16 J Biol Chem 276 2001 1677 1680 (Pubitemid 32109635)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 31
    • 77955408770 scopus 로고    scopus 로고
    • Centrosome motility is essential for initial axon formation in the neocortex
    • F.C. de Anda, K. Meletis, X. Ge, D. Rei, and L.-H. Tsai Centrosome motility is essential for initial axon formation in the neocortex J Neurosci 30 2010 10391 10406
    • (2010) J Neurosci , vol.30 , pp. 10391-10406
    • De Anda, F.C.1    Meletis, K.2    Ge, X.3    Rei, D.4    Tsai, L.-H.5
  • 33
    • 57149102485 scopus 로고    scopus 로고
    • Detection of GTP-tubulin conformation in vivo reveals a role for GTP remnants in microtubule rescues
    • DOI 10.1126/science.1165401
    • A. Dimitrov, M.l. Quesnoit, S. Moutel, I. Cantaloube, C. Poüs, and F. Perez Detection of GTP-tubulin conformation in vivo reveals a role for GTP remnants in microtubule rescues Science 322 2008 1353 1356 (Pubitemid 352775242)
    • (2008) Science , vol.322 , Issue.5906 , pp. 1353-1356
    • Dimitrov, A.1    Quesnoit, M.2    Moutel, S.3    Cantaloube, I.4    Pous, C.5    Perez, F.6
  • 34
    • 0035951060 scopus 로고    scopus 로고
    • Mutation in the β-tubulin signature motif suppresses microtubule GTPase activity and dynamics, and slows mitosis
    • DOI 10.1021/bi010070y
    • C.A. Dougherty, C.R. Sage, A. Davis, and K.W. Farrell Mutation in the beta-tubulin signature motif suppresses microtubule GTPase activity and dynamics, and slows mitosis Biochemistry 40 2001 15725 15732 (Pubitemid 34015201)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15725-15732
    • Dougherty, C.A.1    Sage, C.R.2    Davis, A.3    Farrell, K.W.4
  • 36
    • 43249126878 scopus 로고    scopus 로고
    • Asymmetric tethering of flat and curved lipid membranes by a golgin
    • DOI 10.1126/science.1155821
    • G. Drin, V. Morello, J.F. Casella, P. Gounon, and B. Antonny Asymetric tethering of flat and curved lipid membranes by a golgin Science 320 5876 2008 670 673 (Pubitemid 351928350)
    • (2008) Science , vol.320 , Issue.5876 , pp. 670-673
    • Drin, G.1    Morello, V.2    Casella, J.-F.3    Gounon, P.4    Antonny, B.5
  • 39
    • 77949489741 scopus 로고    scopus 로고
    • Kinesin-13s in mitosis: Key players in the spatial and temporal organization of spindle microtubules
    • S.C. Ems-McClung, and C.E. Walczak Kinesin-13s in mitosis: key players in the spatial and temporal organization of spindle microtubules Semin Cell Dev Biol 21 2010 276 282
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 276-282
    • Ems-Mcclung, S.C.1    Walczak, C.E.2
  • 40
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42 - The centre of polarity
    • DOI 10.1242/jcs.01115
    • S. Etienne-Manneville Cdc42 - the centre of polarity J Cell Sci 117 2004 1291 1300 (Pubitemid 38559807)
    • (2004) Journal of Cell Science , vol.117 , Issue.8 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 41
    • 75749146306 scopus 로고    scopus 로고
    • Plasticity of cell migration: A multiscale tuning model
    • P. Friedl, and K. Wolf Plasticity of cell migration: a multiscale tuning model J Cell Biol 188 1 2010 11 19
    • (2010) J Cell Biol , vol.188 , Issue.1 , pp. 11-19
    • Friedl, P.1    Wolf, K.2
  • 42
    • 77955459468 scopus 로고    scopus 로고
    • ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
    • J.R. Friedman, B. Webster, D. Mastronarde, K. Verhey, and G. Voeltz ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules J Cell Biol 190 3 2010 363 375
    • (2010) J Cell Biol , vol.190 , Issue.3 , pp. 363-375
    • Friedman, J.R.1    Webster, B.2    Mastronarde, D.3    Verhey, K.4    Voeltz, G.5
  • 43
    • 80052814012 scopus 로고    scopus 로고
    • Tran PT. mmb1p binds mitochondria to dynamic microtubules
    • C. Fu, D. Jain, J. Costa, and G. Velve-Casquillas Tran PT. mmb1p binds mitochondria to dynamic microtubules Curr Biol 21 17 2011 143 149
    • (2011) Curr Biol , vol.21 , Issue.17 , pp. 143-149
    • Fu, C.1    Jain, D.2    Costa, J.3    Velve-Casquillas, G.4
  • 45
    • 0031745447 scopus 로고    scopus 로고
    • The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
    • O. Gavet, S. Ozon, V. Manceau, S. Lawler, P. Curmi, and A. Sobel The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network J Cell Sci 111 Pt 22 1998 3333 3346 (Pubitemid 28563036)
    • (1998) Journal of Cell Science , vol.111 , Issue.22 , pp. 3333-3346
    • Gavet, O.1    Ozon, S.2    Manceau, V.3    Lawler, S.4    Curmi, P.5    Sobel, A.6
  • 46
    • 77957817006 scopus 로고    scopus 로고
    • Patronin regulates the microtubule network by protecting minus-ends
    • S.S. Goodwin, and R.D. Vale Patronin regulates the microtubule network by protecting minus-ends Cell 143 2 2010 263 274
    • (2010) Cell , vol.143 , Issue.2 , pp. 263-274
    • Goodwin, S.S.1    Vale, R.D.2
  • 47
    • 17844379382 scopus 로고    scopus 로고
    • Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells
    • DOI 10.1016/j.cell.2005.02.022, PII S0092867405001881
    • E.R. Gomes, S. Jani, and G.G. Gundersen Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells Cell 121 2005 451 463 (Pubitemid 40692304)
    • (2005) Cell , vol.121 , Issue.3 , pp. 451-463
    • Gomes, E.R.1    Jani, S.2    Gundersen, G.G.3
  • 49
    • 0023794840 scopus 로고
    • Selective stabilization of microtubules oriented toward the direction of cell migration
    • G.G. Gundersen, and J.C. Bulinski Selective stabilization of microtubules oriented toward the direction of cell migration Proc Natl Acad Sci U S A 85 1988 5946 5950
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 5946-5950
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 50
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • DOI 10.1083/jcb.141.1.51
    • A. Harada, Y. Takei, Y. Kanai, Y. Tanaka, S. Nonaka, and N. Hirokawa Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein J Cell Biol 141 1998 51 59 (Pubitemid 28182640)
    • (1998) Journal of Cell Biology , vol.141 , Issue.1 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 51
    • 33646800165 scopus 로고    scopus 로고
    • ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
    • M.V. Hernandez, M.G. Sala, J. Balsamo, J. Lilien, and C.O. Arregui ER-bound PTP1B is targeted to newly forming cell-matrix adhesions J Cell Sci 119 2006 1233 1243
    • (2006) J Cell Sci , vol.119 , pp. 1233-1243
    • Hernandez, M.V.1    Sala, M.G.2    Balsamo, J.3    Lilien, J.4    Arregui, C.O.5
  • 56
    • 0032741169 scopus 로고    scopus 로고
    • Decreasing oncoprotein 18/stathmin levels reduces microtubule catastrophes and increases microtubule polymer in vivo
    • B. Howell, H. Deacon, and L. Cassimeris Decreasing oncoprotein 18/stathmin levels reduces microtubule catastrophes and increases microtubule polymer in vivo J Cell Sci 112 Pt 21 1999 3713 3722
    • (1999) J Cell Sci , vol.112 , Issue.PART 21 , pp. 3713-3722
    • Howell, B.1    Deacon, H.2    Cassimeris, L.3
  • 57
    • 79959480895 scopus 로고    scopus 로고
    • Disconnecting the Golgi ribbon from the centrosome prevents directional cell migration and ciliogenesis
    • L. Hurtado, C. Caballero, M.P. Gavilan, J. Cardenas, M. Bornens, and R.M. Rios Disconnecting the Golgi ribbon from the centrosome prevents directional cell migration and ciliogenesis J Cell Biol 193 2011 917 933
    • (2011) J Cell Biol , vol.193 , pp. 917-933
    • Hurtado, L.1    Caballero, C.2    Gavilan, M.P.3    Cardenas, J.4    Bornens, M.5    Rios, R.M.6
  • 58
    • 77955272733 scopus 로고    scopus 로고
    • Tubulin post-translational modifications: Encoding functions on the neuronal microtubule cytoskeleton
    • C. Janke, and M. Kneussel Tubulin post-translational modifications: encoding functions on the neuronal microtubule cytoskeleton Trends Neurosci 33 2010 362 372
    • (2010) Trends Neurosci , vol.33 , pp. 362-372
    • Janke, C.1    Kneussel, M.2
  • 60
    • 33745737636 scopus 로고    scopus 로고
    • Adenomatous polyposis coli on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1
    • DOI 10.1091/mbc.E05-06-0498
    • K. Kita, T. Wittmann, I.S. Näthke, and C.M. Waterman-Storer Adenomatous polyposis coli on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1 Mol Biol Cell 17 2006 2331 2345 (Pubitemid 44011748)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2331-2345
    • Kita, K.1    Wittmann, T.2    Nathke, I.S.3    Waterman-Storer, C.M.4
  • 61
    • 64149084265 scopus 로고    scopus 로고
    • GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization
    • A. Kodani, I. Kristensen, L. Huang, and C. Sütterlin GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization Mol Biol Cell 20 2009 1192 1200
    • (2009) Mol Biol Cell , vol.20 , pp. 1192-1200
    • Kodani, A.1    Kristensen, I.2    Huang, L.3    Sütterlin, C.4
  • 62
    • 39449124362 scopus 로고    scopus 로고
    • The Golgi protein GM130 regulates centrosome morphology and function
    • DOI 10.1091/mbc.E07-08-0847
    • A. Kodani, and C. Sütterlin The Golgi protein GM130 regulates centrosome morphology and function Mol Biol Cell 19 2008 745 753 (Pubitemid 351272161)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 745-753
    • Kodani, A.1    Sutterlin, C.2
  • 66
    • 64049115132 scopus 로고    scopus 로고
    • GSK3beta phosphorylation modulates CLASP-microtubule association and lamella microtubule attachment
    • P. Kumar, K.S. Lyle, S. Gierke, A. Matov, G. Danuser, and T. Wittmann GSK3beta phosphorylation modulates CLASP-microtubule association and lamella microtubule attachment J Cell Biol 184 2009 895 908
    • (2009) J Cell Biol , vol.184 , pp. 895-908
    • Kumar, P.1    Lyle, K.S.2    Gierke, S.3    Matov, A.4    Danuser, G.5    Wittmann, T.6
  • 68
    • 4644364674 scopus 로고    scopus 로고
    • CLIPR-59 is a lipid raft-associated protein containing a cytoskeleton-associated protein glycine-rich domain (CAP-Gly) that perturbs microtubule dynamics
    • DOI 10.1074/jbc.M406482200
    • V.r. Lallemand-Breitenbach, M.l. Quesnoit, V. Braun, A. El Marjou, C. Poüs, and B. Goud CLIPR-59 is a lipid raft-associated protein containing a cytoskeleton-associated protein glycine-rich domain (CAP-Gly) that perturbs microtubule dynamics J Biol Chem 279 2004 41168 41178 (Pubitemid 39287719)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 41168-41178
    • Lallemand-Breitenbach, V.1    Quesnoit, M.2    Braun, V.3    El Marjou, A.4    Pous, C.5    Goud, B.6    Perez, F.7
  • 70
    • 0033052099 scopus 로고    scopus 로고
    • Microtubule-based endoplasmic reticulum motility in Xenopus laevis: Activation of membrane-associated kinesin during development
    • J.D. Lane, and V.J. Allan Microtubule-based endoplasmic reticulum motility in Xenopus laevis: activation of membrane-associated kinesin during development Mol Biol Cell 10 1999 1909 1922
    • (1999) Mol Biol Cell , vol.10 , pp. 1909-1922
    • Lane, J.D.1    Allan, V.J.2
  • 72
    • 79959415087 scopus 로고    scopus 로고
    • EB1 promotes microtubule dynamics by recruiting Sentin in Drosophila cells
    • W. Li, T. Miki, T. Watanabe, M. Kakeno, I. Sugiyama, and K. Kaibuchi EB1 promotes microtubule dynamics by recruiting Sentin in Drosophila cells J Cell Biol 193 2011 973 983
    • (2011) J Cell Biol , vol.193 , pp. 973-983
    • Li, W.1    Miki, T.2    Watanabe, T.3    Kakeno, M.4    Sugiyama, I.5    Kaibuchi, K.6
  • 73
    • 34250888843 scopus 로고    scopus 로고
    • Microtubules tethered at eepithelial cell junctions by dynein facilitate efficient junction assembly
    • DOI 10.1111/j.1600-0854.2007.00574.x
    • L.A. Ligon, and E.L.F. Holzbaur Microtubules tethered at epithelial cell junctions by dynein facilitate efficient junction assembly Traffic 8 2007 808 819 (Pubitemid 46971629)
    • (2007) Traffic , vol.8 , Issue.7 , pp. 808-819
    • Ligon, L.A.1    Holzbaur, E.L.F.2
  • 74
    • 12344300350 scopus 로고    scopus 로고
    • Drosophila CLASP is required for the incorporation of microtubule subunits into fluxing kinetochore fibres
    • DOI 10.1038/ncb1207
    • H. Maiato, A. Khodjakov, and C.L. Rieder Drosophila CLASP is required for the incorporation of microtubule subunits into fluxing kinetochore fibres Nat Cell Biol 7 2005 42 47 (Pubitemid 40123381)
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 42-47
    • Maiato, H.1    Khodjakov, A.2    Rieder, C.L.3
  • 75
    • 78049499222 scopus 로고    scopus 로고
    • Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity
    • J.-B. Manneville, M. Jehanno, and S. Etienne-Manneville Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity J Cell Biol 191 2010 585 598
    • (2010) J Cell Biol , vol.191 , pp. 585-598
    • Manneville, J.-B.1    Jehanno, M.2    Etienne-Manneville, S.3
  • 78
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • W. Meng, Y. Mushika, T. Ichii, and M. Takeichi Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts Cell 135 2008 948 959
    • (2008) Cell , vol.135 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 79
    • 69949178740 scopus 로고    scopus 로고
    • Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells
    • P.M. Miller, A.W. Folkmann, A.R.R. Maia, N. Efimova, A. Efimov, and I. Kaverina Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells Nat Cell Biol 11 2009 1069 1080
    • (2009) Nat Cell Biol , vol.11 , pp. 1069-1080
    • Miller, P.M.1    Folkmann, A.W.2    Maia, A.R.R.3    Efimova, N.4    Efimov, A.5    Kaverina, I.6
  • 81
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • DOI 10.1038/312237a0
    • T. Mitchison, and M. Kirschner Dynamic instability of microtubule growth Nature 312 1984 237 242 (Pubitemid 15201998)
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchinson, T.1    Kirschner, M.2
  • 82
    • 0037054547 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells
    • DOI 10.1083/jcb.200203001
    • M.M. Mogensen, J.B. Tucker, J.B. Mackie, A.R. Prescott, and I.S. Näthke The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells J Cell Biol 157 2002 1041 1048 (Pubitemid 34839778)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 1041-1048
    • Mogensen, M.M.1    Tucker, J.B.2    Mackie, J.B.3    Prescott, A.R.4    Nathke, I.S.5
  • 83
    • 0036140710 scopus 로고    scopus 로고
    • Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport
    • K. Nakajima, Y. Takei, Y. Tanaka, T. Nakagawa, T. Nakata, and Y. Noda Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport Mol Cell Biol 22 2002 866 873 (Pubitemid 34053064)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.3 , pp. 866-873
    • Nakajima, K.1    Takei, Y.2    Tanaka, Y.3    Nakagawa, T.4    Nakata, T.5    Noda, Y.6    Setou, M.7    Hirokawa, N.8
  • 84
    • 77953121697 scopus 로고    scopus 로고
    • AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP170 phosphorylation
    • A. Nakano, H. Kato, T. Watanabe, K.D. Min, S. Yamazaki, and Y. Asano AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP170 phosphorylation Nat Cell Biol 12 2010 583 590
    • (2010) Nat Cell Biol , vol.12 , pp. 583-590
    • Nakano, A.1    Kato, H.2    Watanabe, T.3    Min, K.D.4    Yamazaki, S.5    Asano, Y.6
  • 85
    • 0141656303 scopus 로고    scopus 로고
    • Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head
    • DOI 10.1083/jcb.200302175
    • T. Nakata, and N. Hirokawa Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head J Cell Biol 162 2003 1045 1055 (Pubitemid 37174187)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1045-1055
    • Nakata, T.1    Hirokawa, N.2
  • 86
    • 79961105234 scopus 로고    scopus 로고
    • Preferential binding of a kinesin-1 motor to GTP-tubulin-rich microtubules underlies polarized vesicle transport
    • T. Nakata, S. Niwa, Y. Okada, F. Perez, and N. Hirokawa Preferential binding of a kinesin-1 motor to GTP-tubulin-rich microtubules underlies polarized vesicle transport J Cell Biol 194 2011 245 255
    • (2011) J Cell Biol , vol.194 , pp. 245-255
    • Nakata, T.1    Niwa, S.2    Okada, Y.3    Perez, F.4    Hirokawa, N.5
  • 87
    • 0028641560 scopus 로고
    • KIF1B: A novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • M. Nangaku, R. Sato-Yoshitake, Y. Okada, Y. Noda, R. Takemura, and H. Yamazaki KIF1B: a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria Cell 79 7 1994 1209 1220
    • (1994) Cell , vol.79 , Issue.7 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6
  • 88
    • 4143095005 scopus 로고    scopus 로고
    • MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro
    • DOI 10.1016/j.febslet.2004.06.093, PII S0014579304008695
    • C.N. Newton, M. Wagenbach, Y. Ovechkina, L. Wordeman, and L. Wilson MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro FEBS Lett 572 2004 80 84 (Pubitemid 39092517)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 80-84
    • Newton, C.N.1    Wagenbach, M.2    Ovechkina, Y.3    Wordeman, L.4    Wilson, L.5
  • 89
    • 1642322097 scopus 로고    scopus 로고
    • Stathmin-Tubutin Interaction Gradients in Motile and Mitotic Cells
    • DOI 10.1126/science.1094108
    • P. Niethammer, P. Bastiaens, and E. Karsenti Stathmin-tubulin interaction gradients in motile and mitotic cells Science 303 2004 1862 1866 (Pubitemid 38374877)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1862-1866
    • Niethammer, P.1    Bastiaens, P.2    Karsenti, E.3
  • 90
    • 0037350970 scopus 로고    scopus 로고
    • Microtubule-disruption-induced and chemotactic-peptide-induced migration of human neutrophils: Implications for differential sets of signalling pathways
    • DOI 10.1242/jcs.00306
    • V. Niggli Microtubule-disruption-induces and chemotactic-peptide-induced migration of human neutrophils: implications for differential sets of signalling pathways J Cell Sci 166 Pt5 2003 813 822 (Pubitemid 36367631)
    • (2003) Journal of Cell Science , vol.116 , Issue.5 , pp. 813-822
    • Niggli, V.1
  • 92
    • 0034044992 scopus 로고    scopus 로고
    • A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein Pkl1p
    • J.L. Paluh, E. Nogales, B.R. Oakley, K. McDonald, A.L. Pidoux, and W.Z. Cande A mutation in gamma-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein pkl1p Mol Biol Cell 11 2000 1225 1239 (Pubitemid 30211026)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.4 , pp. 1225-1239
    • Paluh, J.L.1    Nogales, E.2    Oakley, B.R.3    McDonald, K.4    Pidoux, A.L.5    Cande, W.Z.6
  • 93
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: More than just a post-translational modification?
    • D. Perdiz, R. Mackeh, C. Poüs, and A. Baillet The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23 2011 763 771
    • (2011) Cell Signal , vol.23 , pp. 763-771
    • Perdiz, D.1    MacKeh, R.2    Poüs, C.3    Baillet, A.4
  • 94
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • F. Perez, G.S. Diamantopoulos, R. Stalder, and T.E. Kreis CLIP-170 highlights growing microtubule ends in vivo Cell 96 1999 517 527 (Pubitemid 29106839)
    • (1999) Cell , vol.96 , Issue.4 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 97
    • 79953304482 scopus 로고    scopus 로고
    • The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized
    • G.B. Quinones, B.A. Danowski, A. Devaraj, V. Singh, and L.A. Ligon The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized Mol Biol Cell 22 2011 1045 1057
    • (2011) Mol Biol Cell , vol.22 , pp. 1045-1057
    • Quinones, G.B.1    Danowski, B.A.2    Devaraj, A.3    Singh, V.4    Ligon, L.A.5
  • 98
    • 33846278768 scopus 로고    scopus 로고
    • Gamma-tubulin complexes and microtubule organization
    • B. Raynaud-Messina, and A. Merdes Gamma-tubulin complexes and microtubule organization Curr Opin Cell Biol 19 2007 24 30
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 24-30
    • Raynaud-Messina, B.1    Merdes, A.2
  • 99
    • 69449090753 scopus 로고    scopus 로고
    • Bringing KASH under the SUN: The many faces of nucleo-cytoskeletal connections
    • D. Razafsky, and D. Hodzic Bringing KASH under the SUN: the many faces of nucleo-cytoskeletal connections J Cell Biol 186 2009 461 472
    • (2009) J Cell Biol , vol.186 , pp. 461-472
    • Razafsky, D.1    Hodzic, D.2
  • 100
    • 18344370261 scopus 로고    scopus 로고
    • APC is a component of an organizing template for cortical microtubule networks
    • DOI 10.1038/ncb1248
    • A. Reilein, and W.J. Nelson APC is a component of an organizing template for cortical microtubule networks Nat Cell Biol 7 2005 463 473 (Pubitemid 40637406)
    • (2005) Nature Cell Biology , vol.7 , Issue.5 , pp. 463-473
    • Reilein, A.1    Nelson, W.J.2
  • 101
    • 0026075806 scopus 로고
    • Binding of pp170 to microtubules is regulated by phosphorylation
    • J.E. Rickard, and T.E. Kreis Binding of pp170 to microtubules is regulated by phosphorylation J Biol Chem 266 1991 17597 17605 (Pubitemid 21907980)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17597-17605
    • Rickard, J.E.1    Kreis, T.E.2
  • 102
    • 0037223631 scopus 로고    scopus 로고
    • The Golgi apparatus at the cell centre
    • DOI 10.1016/S0955-0674(02)00013-3
    • R.M. Rios, and M. Bornens The Golgi apparatus at the cell centre Curr Opin Cell Biol 15 2003 60 66 (Pubitemid 36044716)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.1 , pp. 60-66
    • Rios, R.M.1    Bornens, M.2
  • 103
    • 4043107077 scopus 로고    scopus 로고
    • GMAP-210 recruits γ-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation
    • DOI 10.1016/j.cell.2004.07.012, PII S0092867404006701
    • R.M. Rios, A. Sanchis, A.M. Tassin, C. Fedriani, and M. Bornens GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation Cell 118 2004 323 335 (Pubitemid 39061113)
    • (2004) Cell , vol.118 , Issue.3 , pp. 323-335
    • Rios, R.M.1    Sanchis, A.2    Tassin, A.M.3    Fedriani, C.4    Bornens, M.5
  • 104
    • 67349287493 scopus 로고    scopus 로고
    • Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130
    • S. Rivero, J. Cardenas, M. Bornens, and R.M. Rios Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130 EMBO J 28 2009 1016 1028
    • (2009) EMBO J , vol.28 , pp. 1016-1028
    • Rivero, S.1    Cardenas, J.2    Bornens, M.3    Rios, R.M.4
  • 105
    • 0035906940 scopus 로고    scopus 로고
    • Microtubule "plus-end-tracking proteins": The end is just the beginning
    • DOI 10.1016/S0092-8674(01)00364-6
    • S.C. Schuyler, and D. Pellman Microtubule "plus-end-tracking proteins": the end is just the beginning Cell 105 2001 421 424 (Pubitemid 32520848)
    • (2001) Cell , vol.105 , Issue.4 , pp. 421-424
    • Schuyler, S.C.1    Pellman, D.2
  • 106
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetylatransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • T. Shida, J.G. Cueva, Z. Xu, M.B. Goodman, and M.V. Nachury The major alpha-tubulin K40 acetylatransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation Proc Natl Acad Sci U S A 107 50 2010 21517 21522
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.50 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 110
    • 79955716605 scopus 로고    scopus 로고
    • Neuronal polarization: The cytoskeleton leads the way
    • M. Stiess, and F. Bradke Neuronal polarization: the cytoskeleton leads the way Dev Neurobiol 71 2011 430 444
    • (2011) Dev Neurobiol , vol.71 , pp. 430-444
    • Stiess, M.1    Bradke, F.2
  • 112
    • 78650285076 scopus 로고    scopus 로고
    • Kinetochore-microtubule interactions: Steps towards bi-orientation
    • T.U. Tanaka Kinetochore-microtubule interactions: steps towards bi-orientation EMBO J 29 2010 4070 4082
    • (2010) EMBO J , vol.29 , pp. 4070-4082
    • Tanaka, T.U.1
  • 113
    • 0019225458 scopus 로고
    • Effects of colchicine on the Golgi complex and GERL of cultured rat peritoneal macrophages and epiphyseal chondrocytes
    • J. Thyberg, A. Piasek, and S. Moskalewski Effects of colchicine on the Golgi complex and GERL of cultured rat peritoneal macrophages and epiphyseal chondrocytes J Cell Sci 45 1980 41 58 (Pubitemid 11208489)
    • (1980) Journal of Cell Science , vol.VOL.45 , pp. 41-58
    • Thyberg, J.1    Piasek, A.2    Moskalewski, S.3
  • 115
    • 0035897404 scopus 로고    scopus 로고
    • A mechanism for nuclear positioning in fission yeast based on microtubule pushing
    • DOI 10.1083/jcb.153.2.397
    • P.T. Tran, L. Marsh, V. Doye, S. Inoué, and F. Chang A mechanism for nuclear positioning in fission yeast based on microtubule pushing J Cell Biol 153 2001 397 411 (Pubitemid 34280223)
    • (2001) Journal of Cell Biology , vol.153 , Issue.2 , pp. 397-411
    • Tran, P.T.1    Marsh, L.2    Doye, V.3    Inoue, S.4    Chang, F.5
  • 116
    • 0024432435 scopus 로고
    • The response of the Golgi complex to microtubule alterations: The roles of metabolic energy and membrane traffic in Golgi complex organization
    • J.R. Turner, and A.M. Tartakoff The response of the Golgi complex to microtubule alterations: the roles of metabolic energy and membrane traffic in Golgi complex organization J Cell Biol 109 1989 2081 2088 (Pubitemid 19282596)
    • (1989) Journal of Cell Biology , vol.109 , Issue.5 , pp. 2081-2088
    • Turner, J.R.1    Tartakoff, A.M.2
  • 117
    • 79959468196 scopus 로고    scopus 로고
    • SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase
    • B. van der Vaart, C. Manatschal, I. Grigoriev, V. Olieric, S.M. Gouveia, and S. Bjelic SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase J Cell Biol 193 2011 1083 1099
    • (2011) J Cell Biol , vol.193 , pp. 1083-1099
    • Van Der Vaart, B.1    Manatschal, C.2    Grigoriev, I.3    Olieric, V.4    Gouveia, S.M.5    Bjelic, S.6
  • 118
    • 33646409613 scopus 로고    scopus 로고
    • Morphogenesis of the endoplasmic reticulum: Beyond active membrane expansion
    • DOI 10.1111/j.1600-0854.2006.00419.x
    • C. Vedrenne, and H.-P. Hauri Morphogenesis of the endoplasmic reticulum: beyond active membrane expansion Traffic 7 2006 639 646 (Pubitemid 43676973)
    • (2006) Traffic , vol.7 , Issue.6 , pp. 639-646
    • Vedrenne, C.1    Hauri, H.-P.2
  • 119
    • 68049104167 scopus 로고    scopus 로고
    • Microtubule network asymmetry in motile cells: Role of Golgi-derived array
    • T. Vinogradova, P.M. Miller, and I. Kaverina Microtubule network asymmetry in motile cells: role of Golgi-derived array Cell Cycle 8 2009 2168 2174
    • (2009) Cell Cycle , vol.8 , pp. 2168-2174
    • Vinogradova, T.1    Miller, P.M.2    Kaverina, I.3
  • 120
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins
    • DOI 10.1083/jcb.152.5.923
    • J.H. Walenta, A.J. Didier, X. Liu, and H. Krämer The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins J Cell Biol 152 2001 923 934 (Pubitemid 34286069)
    • (2001) Journal of Cell Biology , vol.152 , Issue.5 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 121
    • 33748577718 scopus 로고    scopus 로고
    • The Rac Activator DOCK7 Regulates Neuronal Polarity through Local Phosphorylation of Stathmin/Op18
    • DOI 10.1016/j.neuron.2006.07.020, PII S089662730600585X
    • Watabe-Uchida, K.A. John, J.A. Janas, S.E. Newey, and L. Van Aelst The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18 Neuron 51 6 2006 727 739 (Pubitemid 44374902)
    • (2006) Neuron , vol.51 , Issue.6 , pp. 727-739
    • Watabe-Uchida, M.1    John, K.A.2    Janas, J.A.3    Newey, S.E.4    Van Aelst, L.5
  • 122
    • 70350020891 scopus 로고    scopus 로고
    • Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules
    • T. Watanabe, J. Noritake, M. Kakeno, T. Matsui, T. Harada, and S. Wang Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules J Cell Sci 122 Pt16 2009 2969 2979
    • (2009) J Cell Sci , vol.122 , Issue.PART16 , pp. 2969-2979
    • Watanabe, T.1    Noritake, J.2    Kakeno, M.3    Matsui, T.4    Harada, T.5    Wang, S.6
  • 123
    • 13244269913 scopus 로고    scopus 로고
    • Regulation of microtubules in cell migration
    • DOI 10.1016/j.tcb.2004.12.006, PII S0962892404003381
    • T. Watanabe, J. Noritake, and K. Kaibuchi Regulation of microtubules in cell migration Trends Cell Biol 15 2005 76 83 (Pubitemid 40188217)
    • (2005) Trends in Cell Biology , vol.15 , Issue.2 , pp. 76-83
    • Watanabe, T.1    Noritake, J.2    Kaibuchi, K.3
  • 124
    • 0029128472 scopus 로고
    • Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts
    • C.M. Waterman-Storer, J. Gregory, S.F. Parsons, and E.D. Salmon Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts J Cell Biol 130 1995 1161 1169
    • (1995) J Cell Biol , vol.130 , pp. 1161-1169
    • Waterman-Storer, C.M.1    Gregory, J.2    Parsons, S.F.3    Salmon, E.D.4
  • 127
    • 39049099179 scopus 로고    scopus 로고
    • Microtubule stabilization specifies initial neuronal polarization
    • DOI 10.1083/jcb.200707042
    • H. Witte, D. Neukirchen, and F. Bradke Microtubule stabilization specifies initial neuronal polarization J Cell Biol 180 2008 619 632 (Pubitemid 351240708)
    • (2008) Journal of Cell Biology , vol.180 , Issue.3 , pp. 619-632
    • Witte, H.1    Neukirchen, D.2    Bradke, F.3
  • 128
    • 1242271991 scopus 로고    scopus 로고
    • Regulation of Microtubule Destabilizing Activity of Op18/Stathmin Downstream of Rac1
    • DOI 10.1074/jbc.M307261200
    • T. Wittmann, G.M. Bokoch, and C.M. Waterman-Storer Regulation of microtubule destabilizing activity of Op18/stathmin downstream of Rac1 J Biol Chem 279 2004 6196 6203 (Pubitemid 38220653)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 6196-6203
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3
  • 129
    • 0035178210 scopus 로고    scopus 로고
    • Cell motility: Can Rho GTPases and microtubules point the way?
    • T. Wittmann, and C.M. Waterman-Storer Cell motility: can Rho GTPases and microtubules point the way? J Cell Sci 114 Pt 21 2001 3795 3803 (Pubitemid 33094694)
    • (2001) Journal of Cell Science , vol.114 , Issue.21 , pp. 3795-3803
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 130
    • 22344435165 scopus 로고    scopus 로고
    • Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3β in migrating epithelial cells
    • DOI 10.1083/jcb.200412114
    • T. Wittmann, and C.M. Waterman-Storer Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta in migrating epithelial cells J Cell Biol 169 2005 929 939 (Pubitemid 41002869)
    • (2005) Journal of Cell Biology , vol.169 , Issue.6 , pp. 929-939
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 131
    • 77957868249 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules
    • D. Wloga, and J. Gaertig Post-translational modifications of microtubules J Cell Sci 123 2010 3447 3455
    • (2010) J Cell Sci , vol.123 , pp. 3447-3455
    • Wloga, D.1    Gaertig, J.2
  • 132
    • 68949167657 scopus 로고    scopus 로고
    • Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells
    • M.J. Wozniak, B. Bola, K. Brownhill, Y.-C. Yang, V. Levakova, and V.J. Allan Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells J Cell Sci 122 2009 1979 1989
    • (2009) J Cell Sci , vol.122 , pp. 1979-1989
    • Wozniak, M.J.1    Bola, B.2    Brownhill, K.3    Yang, Y.-C.4    Levakova, V.5    Allan, V.J.6
  • 134
    • 0034722382 scopus 로고    scopus 로고
    • Region-specific microtubule transport in motile cells
    • A.M. Yvon, and P. Wadsworth Region-specific microtubule transport in motile cells J Cell Biol 151 2000 1003 1012
    • (2000) J Cell Biol , vol.151 , pp. 1003-1012
    • Yvon, A.M.1    Wadsworth, P.2
  • 135
    • 34247526438 scopus 로고    scopus 로고
    • Three microtubule severing enzymes contribute to the "Pacman- flux" machinery that moves chromosomes
    • DOI 10.1083/jcb.200612011
    • D. Zhang, G.C. Rogers, D.W. Buster, and D.J. Sharp Three microtubule severing enzymes contribute to the Pacman-flux machinery that moves chromosomes J Cell Biol 177 2007 231 242 (Pubitemid 46658635)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 231-242
    • Zhang, D.1    Rogers, G.C.2    Buster, D.W.3    Sharp, D.J.4
  • 136
    • 78649754101 scopus 로고    scopus 로고
    • Kinectin-mediated endoplasmic reticulum dynamics supports focal adhesion growth in the cellular lamella
    • X. Zhang, Y.H. Tee, J.K. Heng, Y. Zhu, X. Hu, and F. Margadant Kinectin-mediated endoplasmic reticulum dynamics supports focal adhesion growth in the cellular lamella J Cell Sci 123 2010 3901 3912
    • (2010) J Cell Sci , vol.123 , pp. 3901-3912
    • Zhang, X.1    Tee, Y.H.2    Heng, J.K.3    Zhu, Y.4    Hu, X.5    Margadant, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.