메뉴 건너뛰기




Volumn 9, Issue JULY, 2015, Pages

Ciliobrevins as tools for studying dynein motor function

Author keywords

Axon; Growth cone; Microtubule; Tension; Transport

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMYLOID BETA PROTEIN; CD40 ANTIGEN; CD40 LIGAND; CILIOBREVIN; CYTOPLASMIC DYNEIN; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; ENZYME INHIBITOR; F ACTIN; INTERLEUKIN 6; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; KINESIN; KINESIN 1; KINESIN 2; LAMININ; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; MYOSIN; MYOSIN II; NERVE GROWTH FACTOR; NONSTRUCTURAL PROTEIN 5A; RHEB PROTEIN; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR GLI2; TRANSCRIPTION FACTOR PITX2; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS RNA;

EID: 84936940426     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2015.00252     Document Type: Article
Times cited : (40)

References (104)
  • 1
    • 0032567765 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon
    • Ahmad, F. J., Echeverri, C. J., Vallee, R. B., and Baas, P. W. (1998). Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon. J. Cell Biol. 140, 391-401. doi: 10.1083/jcb.140.2.391
    • (1998) J. Cell Biol , vol.140 , pp. 391-401
    • Ahmad, F.J.1    Echeverri, C.J.2    Vallee, R.B.3    Baas, P.W.4
  • 2
    • 33745807269 scopus 로고    scopus 로고
    • Effects of dynactin disruption and dynein depletion on axonal microtubules
    • Ahmad, F. J., He, Y., Myers, K. A., Hasaka, T. P., Francis, F., Black, M. M., et al. (2006). Effects of dynactin disruption and dynein depletion on axonal microtubules. Traffic 7, 524-537. doi: 10.1111/j.1600-0854.2006.00403.x
    • (2006) Traffic , vol.7 , pp. 524-537
    • Ahmad, F.J.1    He, Y.2    Myers, K.A.3    Hasaka, T.P.4    Francis, F.5    Black, M.M.6
  • 3
    • 0033625536 scopus 로고    scopus 로고
    • Motor proteins regulate force interactions between microtubules and microfilaments in the axon
    • Ahmad, F. J., Hughey, J., Wittmann, T., Hyman, A., Greaser, M., and Baas, P. W. (2000). Motor proteins regulate force interactions between microtubules and microfilaments in the axon. Nat. Cell Biol. 2, 276-280. doi:10.1038/35010544
    • (2000) Nat. Cell Biol , vol.2 , pp. 276-280
    • Ahmad, F.J.1    Hughey, J.2    Wittmann, T.3    Hyman, A.4    Greaser, M.5    Baas, P.W.6
  • 4
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento, F., Emans, N., Griffiths, G., and Gruenberg, J. (1993). Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 123, 1373-1387. doi: 10.1083/jcb.123.6.1373.
    • (1993) J. Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 5
    • 33745868372 scopus 로고    scopus 로고
    • Axonal transport of microtubules: The long and short of it
    • Baas, P. W., Vidya Nadar, C., and Myers, K. A. (2006). Axonal transport of microtubules: the long and short of it. Traffic 7, 490-498. doi: 10.1111/j.1600-0854.2006.00392.x
    • (2006) Traffic , vol.7 , pp. 490-498
    • Baas, P.W.1    Vidya Nadar, C.2    Myers, K.A.3
  • 6
    • 84907343347 scopus 로고    scopus 로고
    • Axonally synthesized ATF4 transmits a neurodegenerative signal across brain regions
    • Baleriola, J., Walker, C. A., Jean, Y. Y., Crary, J. F., Troy, C. M., Nagy, P. L., et al. (2012). Axonally synthesized ATF4 transmits a neurodegenerative signal across brain regions. Cell 158, 1159-1172. doi: 10.1016/j.cell.2014.07.001
    • (2012) Cell , vol.158 , pp. 1159-1172
    • Baleriola, J.1    Walker, C.A.2    Jean, Y.Y.3    Crary, J.F.4    Troy, C.M.5    Nagy, P.L.6
  • 7
    • 84884787316 scopus 로고    scopus 로고
    • Recycling of kinesin-1 motors by diffusion after transport
    • Blasius, T. L., Reed, N., Slepchenko, B. M., and Verhey, K. J. (2013). Recycling of kinesin-1 motors by diffusion after transport. PLoS ONE 8:e76081. doi: 10.1371/journal.pone.0076081
    • (2013) Plos ONE
    • Blasius, T.L.1    Reed, N.2    Slepchenko, B.M.3    Verhey, K.J.4
  • 9
    • 0344254845 scopus 로고    scopus 로고
    • Expression of the mitotic kinesin Kif15 in postmitotic neurons: Implications for neuronal migration and development
    • Buster, D. W., Baird, D. H., Yu, W., Solowska, J. M., Chauviere, M., Mazurek, A., et al. (2003). Expression of the mitotic kinesin Kif15 in postmitotic neurons: implications for neuronal migration and development. J. Neurocytol. 32, 79-96. doi:10.1023/A:1027332432740
    • (2003) J. Neurocytol , vol.32 , pp. 79-96
    • Buster, D.W.1    Baird, D.H.2    Yu, W.3    Solowska, J.M.4    Chauviere, M.5    Mazurek, A.6
  • 10
    • 84925115083 scopus 로고    scopus 로고
    • Uni-directional ciliary membrane protein trafficking by a cytoplasmic retrograde IFT motor and ciliary ectosome shedding
    • Cao, M., Ning, J., Hernandez-Lara, C. I., Belzile, O., Wang, Q., Dutcher, S. K., et al. Uni-directional ciliary membrane protein trafficking by a cytoplasmic retrograde IFT motor and ciliary ectosome shedding. Elife 4:e05242. doi: 10.7554/eLife.05242
    • Elife
    • Cao, M.1    Ning, J.2    Hernandez-Lara, C.I.3    Belzile, O.4    Wang, Q.5    Dutcher, S.K.6
  • 11
    • 58149229093 scopus 로고    scopus 로고
    • Structure and functional role of dynein’s microtubule-binding domain
    • Carter, A. P., Garbarino, J. E., Wilson-Kubalek, E. M., Shipley, W. E., Cho, C., Milligan, R. A., et al. (2008). Structure and functional role of dynein’s microtubule-binding domain. Science 322, 1691-1695. doi:10.1126/science.1164424
    • (2008) Science , vol.322 , pp. 1691-1695
    • Carter, A.P.1    Garbarino, J.E.2    Wilson-Kubalek, E.M.3    Shipley, W.E.4    Cho, C.5    Milligan, R.A.6
  • 12
    • 84866489254 scopus 로고    scopus 로고
    • Dynein mediates the localization and activation of mTOR in normal and human cytomegalovirus-infected cells
    • Clippinger, A. J., and Alwine, J. C. (2012). Dynein mediates the localization and activation of mTOR in normal and human cytomegalovirus-infected cells. GenesDev. 26, 2015-2026. doi: 10.1101/gad.196147.112
    • (2012) Genesdev , vol.26 , pp. 2015-2026
    • Clippinger, A.J.1    Alwine, J.C.2
  • 13
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthesy-Theulaz, I., Pauloin, A., and Pfeffer, S. R. (1992). Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol.118, 1333-1345. doi: 10.1083/jcb.118.6.1333
    • (1992) J. Cell Biol , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 14
    • 84855828496 scopus 로고    scopus 로고
    • Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains
    • Dewitt, M. A., Chang, A. Y., Combs, P. A., and Yildiz, A. (2012). Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains. Science 335, 221-225. doi: 10.1126/science.1215804
    • (2012) Science , vol.335 , pp. 221-225
    • Dewitt, M.A.1    Chang, A.Y.2    Combs, P.A.3    Yildiz, A.4
  • 15
    • 33845905221 scopus 로고    scopus 로고
    • Dynein is required for receptor sorting and the morphogenesis of early endosomes
    • Driskell, O. J., Mironov, A., Allan, V. J., and Woodman, P. G. (2007). Dynein is required for receptor sorting and the morphogenesis of early endosomes. Nat. CellBiol. 9, 113-120. doi: 10.1038/ncb1525
    • (2007) Nat. Cellbiol , vol.9 , pp. 113-120
    • Driskell, O.J.1    Mironov, A.2    Allan, V.J.3    Woodman, P.G.4
  • 16
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • Echeverri, C. J., Paschal, B. M., Vaughan, K. T., and Vallee, R. B. (1996). Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J. CellBiol. 132, 617-633. doi: 10.1083/jcb.132.4.617
    • (1996) J. Cellbiol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 17
    • 0032728976 scopus 로고    scopus 로고
    • Analysis of dynactin subcomplexes reveals a novel actin- related protein associated with the arp1 minifilament pointed end
    • Eckley, D. M., Gill, S. R., Melkonian, K. A., Bingham, J. B., Goodson, H. V., Heuser, J. E., et al. (1999). Analysis of dynactin subcomplexes reveals a novel actin- related protein associated with the arp1 minifilament pointed end. J. Cell Biol.147, 307-320. doi: 10.1083/jcb.147.2.307
    • (1999) J. Cell Biol , vol.147 , pp. 307-320
    • Eckley, D.M.1    Gill, S.R.2    Melkonian, K.A.3    Bingham, J.B.4    Goodson, H.V.5    Heuser, J.E.6
  • 18
    • 0038107541 scopus 로고    scopus 로고
    • Interactions between the evolutionarily conserved, actin-related protein, Arp11, actin, and Arp1 Mol. Biol
    • Eckley, D. M., and Schroer, T. A. (2003). Interactions between the evolutionarily conserved, actin-related protein, Arp11, actin, and Arp1 Mol. Biol. Cell 14, 2645-2654. doi:10.1091/mbc.E03-01-0049
    • (2003) Cell , vol.14 , pp. 2645-2654
    • Eckley, D.M.1    Schroer, T.A.2
  • 19
    • 0024283152 scopus 로고
    • An ATPase with properties expected for the organelle motor of the giant amoeba, Reticulomyxa
    • Euteneuer, U., Koonce, M. P., Pfister, K. K., and Schliwa, M. (1988). An ATPase with properties expected for the organelle motor of the giant amoeba, Reticulomyxa. Nature 332, 176-178. doi: 10.1038/332176a0
    • (1988) Nature , vol.332 , pp. 176-178
    • Euteneuer, U.1    Koonce, M.P.2    Pfister, K.K.3    Schliwa, M.4
  • 20
    • 84895476594 scopus 로고    scopus 로고
    • Dynamic imaging of the hepatitis C virus NS5 A protein during a productive infection
    • Eyre, N. S., Fiches, G. N., Aloia, A. L., Helbig, K. J., McCartney, E. M., McErlean, C. S., et al. (2014). Dynamic imaging of the hepatitis C virus NS5 A protein during a productive infection. J. Virol. 88, 3636-3652. doi: 10.1128/JVI.02490-13
    • (2014) J. Virol , vol.88 , pp. 3636-3652
    • Eyre, N.S.1    Fiches, G.N.2    Aloia, A.L.3    Helbig, K.J.4    McCartney, E.M.5    McErlean, C.S.6
  • 21
    • 79955490607 scopus 로고    scopus 로고
    • Kinesin-5, a mitotic microtubule- associated motor protein, modulates neuronal migration. Mol. Biol
    • Falnikar, A., Tole, S., and Baas, P. W. (2011). Kinesin-5, a mitotic microtubule- associated motor protein, modulates neuronal migration. Mol. Biol. Cell 22, 1561-1574. doi: 10.1091/mbc.E10-11-0905
    • (2011) Cell , vol.22 , pp. 1561-1574
    • Falnikar, A.1    Tole, S.2    Baas, P.W.3
  • 22
    • 0032190094 scopus 로고    scopus 로고
    • Expression of the mitotic motor protein Eg5 in postmitotic neurons: Implications for neuronal development
    • Ferhat, L., Cook, C., Chauviere, M., Harper, M., Kress, M., Lyons, G. E., et al. (1998a). Expression of the mitotic motor protein Eg5 in postmitotic neurons: implications for neuronal development. J. Neurosci. 18, 7822-7835
    • (1998) J. Neurosci , vol.18 , pp. 7822-7835
    • Ferhat, L.1    Cook, C.2    Chauviere, M.3    Harper, M.4    Kress, M.5    Lyons, G.E.6
  • 23
    • 0031870960 scopus 로고    scopus 로고
    • Expression of the mitotic motor protein CH01/MKLP1 in postmitotic neurons
    • Ferhat, L., Kuriyama, R., Lyons, G. E., Micales, B., and Baas, P. W. (1998b). Expression of the mitotic motor protein CH01/MKLP1 in postmitotic neurons. Eur. J. Neurosci. 10, 1383-1393. doi: 10.1046/j.1460-9568.1998.00159.x
    • (1998) Eur. J. Neurosci , vol.10 , pp. 1383-1393
    • Ferhat, L.1    Kuriyama, R.2    Lyons, G.E.3    Micales, B.4    Baas, P.W.5
  • 24
    • 84862814996 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein
    • Firestone, A. J., Weinger, J. S., Maldonado, M., Barlan, K., Langston, L. D., O’donnell, M., et al. (2012). Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein. Nature 484, 125-129. doi: 10.1038/nature10936
    • (2012) Nature , vol.484 , pp. 125-129
    • Firestone, A.J.1    Weinger, J.S.2    Maldonado, M.3    Barlan, K.4    Langston, L.D.5    O’Donnell, M.6
  • 25
    • 84908488959 scopus 로고    scopus 로고
    • Integrated regulation of motor-driven organelle transport by scaffolding proteins
    • Fu, M. M., and Holzbaur, E. L. (2014a). Integrated regulation of motor-driven organelle transport by scaffolding proteins. Trends Cell Biol. 24, 564-574. doi: 10.1016/j.tcb.2014.05.002
    • (2014) Trends Cell Biol , vol.24 , pp. 564-574
    • Fu, M.M.1    Holzbaur, E.L.2
  • 26
    • 84903469617 scopus 로고    scopus 로고
    • Primary cilia control hedgehog signaling during muscle differentiation and are deregulated in rhabdomyosarcoma
    • Fu, W., Asp, P., Canter, B., and Dynlacht, B. D. (2014b). Primary cilia control hedgehog signaling during muscle differentiation and are deregulated in rhabdomyosarcoma. Proc. Natl. Acad. Sci. U.S.A. 111, 9151-9156. doi: 10.1073/pnas.1323265111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 9151-9156
    • Fu, W.1    Asp, P.2    Canter, B.3    Dynlacht, B.D.4
  • 28
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule- binding structure within the dynein motor domain
    • Gee, M. A., Heuser, J. E., and Vallee, R. B. (1997). An extended microtubule- binding structure within the dynein motor domain. Nature 390, 636-639. doi: 10.1038/37663
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 29
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S. R., Schroer, T. A., Szilak, I., Steuer, E. R., Sheetz, M. P., and Cleveland, W. (1991). Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115, 1639-1650. doi: 10.1083/jcb.115.6.1639
    • (1991) J. Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, W.6
  • 30
    • 0342265157 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo
    • Gonczy, P., Pichler, S., Kirkham, M., and Hyman, A. A. (1999). Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo. J. Cell Biol. 147, 135-150. doi:10.1083/jcb.147.1.135
    • (1999) J. Cell Biol , vol.147 , pp. 135-150
    • Gonczy, P.1    Pichler, S.2    Kirkham, M.3    Hyman, A.A.4
  • 31
    • 27544447708 scopus 로고    scopus 로고
    • Mechanisms for focusing mitotic spindle poles by minus end-directed motor proteins
    • Goshima, G., Nedelec, F., and Vale, R. D. (2005). Mechanisms for focusing mitotic spindle poles by minus end-directed motor proteins. J. Cell Biol. 171, 229-240. doi: 10.1083/jcb.200505107
    • (2005) J. Cell Biol , vol.171 , pp. 229-240
    • Goshima, G.1    Nedelec, F.2    Vale, R.D.3
  • 32
    • 34250677626 scopus 로고    scopus 로고
    • Cytoplasmic dynein and LIS1 are required for microtubule advance during growth cone remodeling and fast axonal outgrowth
    • Grabham, P. W., Seale, G. E., Bennecib, M., Goldberg, D. J., and Vallee, R. B. (2007). Cytoplasmic dynein and LIS1 are required for microtubule advance during growth cone remodeling and fast axonal outgrowth. J. Neurosci. 27, 5823-5834. doi: 10.1523/JNEUR0SCI.1135-07.2007
    • (2007) J. Neurosci , vol.27 , pp. 5823-5834
    • Grabham, P.W.1    Seale, G.E.2    Bennecib, M.3    Goldberg, D.J.4    Vallee, R.B.5
  • 33
    • 84906933847 scopus 로고    scopus 로고
    • Bidirectional cargo transport: Moving beyond tug of war
    • Hancock, W. O. (2014). Bidirectional cargo transport: moving beyond tug of war.Nat. Rev.Mol. CellBiol. 15, 615-628. doi: 10.1038/nrm3853
    • (2014) Nat. Rev.Mol. Cellbiol , vol.15 , pp. 615-628
    • Hancock, W.O.1
  • 35
    • 0024445251 scopus 로고
    • Microtubules accelerate ADP release by dynein
    • Holzbaur, E. L., and Johnson, K. A. (1989). Microtubules accelerate ADP release by dynein. Biochemistry 28, 7010-7016. doi: 10.1021/bi00443a034
    • (1989) Biochemistry , vol.28 , pp. 7010-7016
    • Holzbaur, E.L.1    Johnson, K.A.2
  • 36
    • 84865679752 scopus 로고    scopus 로고
    • Lis 1 acts as a “clutch” between the ATPase and microtubule-binding domains of the dyneinmotor
    • Huang, J., Roberts, A. J., Leschziner, A. E., and Reck-Peterson, S. L. (2012). Lis 1 acts as a “clutch” between the ATPase and microtubule-binding domains of the dyneinmotor. Cell 150,975-986. doi: 10.1016/j.cell.2012.07.022
    • (2012) Cell , vol.150 , pp. 975-986
    • Huang, J.1    Roberts, A.J.2    Leschziner, A.E.3    Reck-Peterson, S.L.4
  • 37
    • 69549138464 scopus 로고    scopus 로고
    • Small-molecule inhibitors reveal multiple strategies for Hedgehog pathway blockade
    • Hyman, J. M., Firestone, A. J., Heine, V. M., Zhao, Y., Ocasio, C. A., Han, K., et al. (2009). Small-molecule inhibitors reveal multiple strategies for Hedgehog pathway blockade. Proc. Natl. Acad. Sci. U.S.A. 106, 14132-14137. doi: 10.1073/pnas.0907134106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 14132-14137
    • Hyman, J.M.1    Firestone, A.J.2    Heine, V.M.3    Zhao, Y.4    Ocasio, C.A.5    Han, K.6
  • 39
    • 36049016163 scopus 로고    scopus 로고
    • The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein
    • Imamula, K., Kon, T., Ohkura, R., and Sutoh, K. (2007). The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein. Proc. Natl. Acad. Sci. U.S.A. 104, 16134-16139. doi: 10.1073/pnas.0702370104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 16134-16139
    • Imamula, K.1    Kon, T.2    Ohkura, R.3    Sutoh, K.4
  • 40
    • 84879796952 scopus 로고    scopus 로고
    • Axonal degeneration in Alzheimer’s disease: When signaling abnormalities meet the axonal transport system. Exp
    • Kanaan, N. M., Pigino, G. F., Brady, S. T., Lazarov, O., Binder, L. I., and Morfini, G. A. (2013). Axonal degeneration in Alzheimer’s disease: when signaling abnormalities meet the axonal transport system. Exp. Neurol. 246, 44-53. doi: 10.1016/j.expneurol.2012.06.003
    • (2013) Neurol , vol.246 , pp. 44-53
    • Kanaan, N.M.1    Pigino, G.F.2    Brady, S.T.3    Lazarov, O.4    Binder, L.I.5    Morfini, G.A.6
  • 41
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki, S., and Holzbaur, E. L. (1995). Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol. Chem. 270,28806-28811. doi: 10.1074/jbc.270.48.28806
    • (1995) J. Biol. Chem , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.2
  • 42
    • 0034681316 scopus 로고    scopus 로고
    • A dynactin subunit with a highly conserved cysteine-rich motif interacts directlywith Arp1
    • Karki, S., Tokito, M. K., and Holzbaur, E. L. (2000). A dynactin subunit with a highly conserved cysteine-rich motif interacts directlywith Arp1 J. Biol. Chem. 275, 4834-4839. doi: 10.1074/jbc.275.7.4834
    • (2000) J. Biol. Chem , vol.275 , pp. 4834-4839
    • Karki, S.1    Tokito, M.K.2    Holzbaur, E.L.3
  • 43
    • 84880597484 scopus 로고    scopus 로고
    • Big steps toward understanding dynein
    • Kikkawa, M. (2013). Big steps toward understanding dynein. J. Cell Biol. 202, 15-23. doi: 10.1083/jcb.201304099
    • (2013) J. Cell Biol , vol.202 , pp. 15-23
    • Kikkawa, M.1
  • 44
    • 84905994558 scopus 로고    scopus 로고
    • Simultaneous measurement of smoothened entry into and exit from the primary cilium
    • Kim, J., Hsia, E. Y., Sever, N., Beachy, P. A., and Zheng, X. (2014). Simultaneous measurement of smoothened entry into and exit from the primary cilium. PLoS ONE 9:e104070. doi: 10.1371/journal.pone.0104070
    • (2014) Plos ONE , vol.9 , pp. 9
    • Kim, J.1    Hsia, E.Y.2    Sever, N.3    Beachy, P.A.4    Zheng, X.5
  • 45
    • 17844362989 scopus 로고    scopus 로고
    • Computer simulations and image processing reveal length-dependent pulling force as the primary mechanism for C. Elegans male pronuclear migration. Dev
    • Kimura, A., and Onami, S. (2005). Computer simulations and image processing reveal length-dependent pulling force as the primary mechanism for C. elegans male pronuclear migration. Dev. Cell 8, 765-775. doi: 10.1016/j.devcel.2005.03.007
    • (2005) Cell , vol.8 , pp. 765-775
    • Kimura, A.1    Onami, S.2
  • 46
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor. Nat
    • King, S. J., and Schroer, T. A. (2000). Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2, 20-24. doi: 10.1038/71338
    • (2000) Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 47
    • 22444450774 scopus 로고    scopus 로고
    • ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein
    • Kon, T., Mogami, T., Ohkura, R., Nishiura, M., and Sutoh, K. (2005). ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein. Nat. Struct. Mol. Biol. 12, 513-519. doi: 10.1038/nsmb930
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 513-519
    • Kon, T.1    Mogami, T.2    Ohkura, R.3    Nishiura, M.4    Sutoh, K.5
  • 48
    • 84859918439 scopus 로고    scopus 로고
    • The 2.8 A crystal structure of the dynein motor domain
    • Kon, T., Oyama, T., Shimo Kon, R., Imamula, K., Shima, T., Sutoh, K., et al. (2012). The 2.8 A crystal structure of the dynein motor domain. Nature 484, 345-350. doi: 10.1038/nature10955
    • (2012) Nature , vol.484 , pp. 345-350
    • Kon, T.1    Oyama, T.2    Shimo Kon, R.3    Imamula, K.4    Shima, T.5    Sutoh, K.6
  • 49
    • 0026733686 scopus 로고
    • Laminin selectively enhances axonal growth and accelerates the development of polarity by hippocampal neurons in culture. Brain Res. Dev
    • Lein, P. J., Banker, G. A., and Higgins, D. (1992). Laminin selectively enhances axonal growth and accelerates the development of polarity by hippocampal neurons in culture. Brain Res. Dev. Brain Res. 69, 191-197. doi:10.1016/0165-3806(92)90159-T
    • (1992) Brain Res , vol.69 , pp. 191-197
    • Lein, P.J.1    Banker, G.A.2    Higgins, D.3
  • 50
    • 84866990769 scopus 로고    scopus 로고
    • Mitotic motors coregulate microtubule patterns in axons and dendrites
    • Lin, S., Liu, M., Mozgova, O. I., Yu, W., and Baas, P. W. (2012). Mitotic motors coregulate microtubule patterns in axons and dendrites. J. Neurosci. 32, 14033-14049. doi: 10.1523/JNEUROSCI.3070-12.2012
    • (2012) J. Neurosci , vol.32 , pp. 14033-14049
    • Lin, S.1    Liu, M.2    Mozgova, O.I.3    Yu, W.4    Baas, P.W.5
  • 51
    • 84880381626 scopus 로고    scopus 로고
    • Diacylglycerol promotes centrosome polarization in T cells via reciprocal localization of dynein and myosin II
    • Liu, X., Kapoor, T. M., Chen, J. K., and Huse, M. (2013). Diacylglycerol promotes centrosome polarization in T cells via reciprocal localization of dynein and myosin II. Proc. Natl. Acad. Sci. U.S.A. 110, 11976-11981. doi: 10.1073/pnas.1306180110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 11976-11981
    • Liu, X.1    Kapoor, T.M.2    Chen, J.K.3    Huse, M.4
  • 52
    • 84878562310 scopus 로고    scopus 로고
    • Initial neurite outgrowth in Drosophila neurons is driven by kinesin-powered microtubule sliding
    • Lu, W., Fox, P., Lakonishok, M., Davidson, M. W., and Gelfand, V. I. (2013). Initial neurite outgrowth in Drosophila neurons is driven by kinesin-powered microtubule sliding. Curr. Biol. 23, 1018-1023. doi: 10.1016/j.cub.2013.04.050
    • (2013) Curr. Biol , vol.23 , pp. 1018-1023
    • Lu, W.1    Fox, P.2    Lakonishok, M.3    Davidson, M.W.4    Gelfand, V.I.5
  • 53
    • 0023663075 scopus 로고
    • Identification of a microtubule-based cytoplasmic motor in the nematode C. Elegans
    • Lye, R. J., Porter, M. E., Scholey, J. M., and McIntosh, J. R. (1987). Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. Cell 51, 309-318. doi: 10.1016/0092-8674(87)90157-7
    • (1987) Cell , vol.51 , pp. 309-318
    • Lye, R.J.1    Porter, M.E.2    Scholey, J.M.3    McIntosh, J.R.4
  • 54
    • 1342325553 scopus 로고    scopus 로고
    • Cytoplasmic dynein functions as a gear in response to load
    • Mallik, R., Carter, B. C., Lex, S. A., King, S. J., and Gross, S. P. (2004). Cytoplasmic dynein functions as a gear in response to load. Nature 427, 649-652. doi: 10.1038/nature02293
    • (2004) Nature , vol.427 , pp. 649-652
    • Mallik, R.1    Carter, B.C.2    Lex, S.A.3    King, S.J.4    Gross, S.P.5
  • 55
    • 59349084461 scopus 로고    scopus 로고
    • Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex
    • Markus, S. M., Punch, J. J., and Lee, W. L. (2009). Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex. Curr. Biol. 19, 196-205. doi: 10.1016/j.cub.2008.12.047
    • (2009) Curr. Biol , vol.19 , pp. 196-205
    • Markus, S.M.1    Punch, J.J.2    Lee, W.L.3
  • 56
    • 84891799739 scopus 로고    scopus 로고
    • Direct observation of microtubule pushing by cortical dynein in living cells. Mol. Biol
    • Mazel, T., Biesemann, A., Krejczy, M., Nowald, J., Muller, O., and Dehmelt, L. (2013). Direct observation of microtubule pushing by cortical dynein in living cells. Mol. Biol. Cell. 25, 95-106. doi: 10.1091/mbc.E13-07-0376
    • (2013) Cell , vol.25 , pp. 95-106
    • Mazel, T.1    Biesemann, A.2    Krejczy, M.3    Nowald, J.4    Muller, O.5    Dehmelt, L.6
  • 57
    • 77951701022 scopus 로고    scopus 로고
    • LIS1 and NudE induce a persistent dynein force-producing state
    • McKenney, R. J., Vershinin, M., Kunwar, A., Vallee, R. B., and Gross, S. P. (2010). LIS1 and NudE induce a persistent dynein force-producing state. Cell 141, 304-314. doi: 10.1016/j.cell.2010.02.035
    • (2010) Cell , vol.141 , pp. 304-314
    • McKenney, R.J.1    Vershinin, M.2    Kunwar, A.3    Vallee, R.B.4    Gross, S.P.5
  • 58
    • 84904424376 scopus 로고    scopus 로고
    • Local translation and retrograde axonal transport of CREB regulates IL-6-induced nociceptive plasticity. Mol
    • Melemedjian, O. K., Tillu, D. V., Moy, J. K., Asiedu, M. N., Mandell, E. K., Ghosh, S., et al. (2014). Local translation and retrograde axonal transport of CREB regulates IL-6-induced nociceptive plasticity. Mol. Pain 10:45. doi: 10.1186/1744-8069-10-45
    • (2014) Pain , vol.10
    • Melemedjian, O.K.1    Tillu, D.V.2    Moy, J.K.3    Asiedu, M.N.4    Mandell, E.K.5    Ghosh, S.6
  • 59
    • 17144420913 scopus 로고    scopus 로고
    • Direct observation demonstrates that Liprin-a is required for trafficking of synaptic vesicles
    • Miller, K. E., DeProto, J., Kaufmann, N., Patel, B. N., Duckworth, A., and van Vactor, D. (2005). Direct observation demonstrates that Liprin-a is required for trafficking of synaptic vesicles. Curr. Biol. 15, 684-689. doi: 10.1016/j.cub.2005.02.061
    • (2005) Curr. Biol , vol.15 , pp. 684-689
    • Miller, K.E.1    Deproto, J.2    Kaufmann, N.3    Patel, B.N.4    Duckworth, A.5    Van Vactor, D.6
  • 60
    • 33748541597 scopus 로고    scopus 로고
    • Antagonistic forces generated by cytoplasmic dynein and myosin-II during growth cone turning and axonal retraction
    • Myers, K. A., Tint, I., Nadar, C. V., He, Y., Black, M. M., and Baas, P. W. (2006). Antagonistic forces generated by cytoplasmic dynein and myosin-II during growth cone turning and axonal retraction. Traffic 7, 1333-1351. doi: 10.1111/j.1600-0854.2006.00476.x
    • (2006) Traffic , vol.7 , pp. 1333-1351
    • Myers, K.A.1    Tint, I.2    Nadar, C.V.3    He, Y.4    Black, M.M.5    Baas, P.W.6
  • 61
    • 57649188646 scopus 로고    scopus 로고
    • Kinesin-5 is essential for growth-cone turning
    • Nadar, V. C., Ketschek, A., Myers, K. A., Gallo, G., and Baas, P. W. (2008). Kinesin-5 is essential for growth-cone turning. Curr. Biol. 18, 1972-1977. doi: 10.1016/j.cub.2008.11.021
    • (2008) Curr. Biol , vol.18 , pp. 1972-1977
    • Nadar, V.C.1    Ketschek, A.2    Myers, K.A.3    Gallo, G.4    Baas, P.W.5
  • 62
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassemblyofprotein 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 disassemblyofprotein complexes. GenomeRes. 9,27-43. doi: 10.1101/gr.9.1.27
    • (1999) Genomeres , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 63
    • 35548975477 scopus 로고    scopus 로고
    • Coupling of cortical dynein and G alpha proteins mediates spindle positioning in Caenorhabditis elegans. Nat
    • Nguyen-Ngoc, T., Afshar, K., and Gonczy, P. (2007). Coupling of cortical dynein and G alpha proteins mediates spindle positioning in Caenorhabditis elegans. Nat. Cell Biol. 9, 1294-1302. doi: 10.1038/ncb1649
    • (2007) Cell Biol , vol.9 , pp. 1294-1302
    • Nguyen-Ngoc, T.1    Afshar, K.2    Gonczy, P.3
  • 64
    • 0034026122 scopus 로고    scopus 로고
    • Mammalian spindle orientation and position respond to changes in cell shape in a dynein-dependent fashion. Mol. Biol
    • O’connell, C. B., and Wang, Y. L. (2000). Mammalian spindle orientation and position respond to changes in cell shape in a dynein-dependent fashion. Mol. Biol. Cell 11, 1765-1774. doi: 10.1091/mbc.11.5.1765
    • (2000) Cell , vol.11 , pp. 1765-1774
    • O’Connell, C.B.1    Wang, Y.L.2
  • 65
    • 0023608935 scopus 로고
    • MAP 1 C is a microtubule- activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal, B. M., Shpetner, H. S., and Vallee, R. B. (1987). MAP 1 C is a microtubule- activated ATPase which translocates microtubules in vitro and has dynein-like properties. J. CellBiol. 105, 1273-1282. doi: 10.1083/jcb.105.3.1273
    • (1987) J. Cellbiol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 66
    • 0023205148 scopus 로고
    • Retrograde transport by the microtubule- associated protein MAP 1 C
    • Paschal, B. M., and Vallee, R. B. (1987). Retrograde transport by the microtubule- associated protein MAP 1 C. Nature 330, 181-183. doi: 10.1038/330181a0
    • (1987) Nature , vol.330 , pp. 181-183
    • Paschal, B.M.1    Vallee, R.B.2
  • 67
    • 0033343738 scopus 로고    scopus 로고
    • Cytoplasmic dynein and microtubule transport in the axon: The action connection. Mol
    • Pfister, K. K. (1999). Cytoplasmic dynein and microtubule transport in the axon: the action connection. Mol. Neurobiol. 20, 81-91. doi: 10.1007/BF02742435
    • (1999) Neurobiol , vol.20 , pp. 81-91
    • Pfister, K.K.1
  • 68
    • 84929287474 scopus 로고    scopus 로고
    • Distinct functional roles of cytoplasmic dynein defined by the intermediate chain isoforms. Exp
    • Pfister, K. K. (2015). Distinct functional roles of cytoplasmic dynein defined by the intermediate chain isoforms. Exp. Cell Res. 334, 54-60. doi: 10.1016/j.yexcr.2014.12.013
    • (2015) Cell Res , vol.334 , pp. 54-60
    • Pfister, K.K.1
  • 69
    • 33646759268 scopus 로고    scopus 로고
    • Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons. Mol. Biol
    • Pilling, A. D., Horiuchi, D., Lively, C. M., and Saxton, W. M. (2006). Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons. Mol. Biol. Cell 17, 2057-2068. doi: 10.1091/mbc.E05-06-0526
    • (2006) Cell , vol.17 , pp. 2057-2068
    • Pilling, A.D.1    Horiuchi, D.2    Lively, C.M.3    Saxton, W.M.4
  • 70
    • 0021112029 scopus 로고
    • Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex
    • Porter, M. E., and Johnson, K. A. (1983). Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex. J. Biol. Chem. 258, 6582-6587.
    • (1983) J. Biol. Chem , vol.258 , pp. 6582-6587
    • Porter, M.E.1    Johnson, K.A.2
  • 71
    • 84856710211 scopus 로고    scopus 로고
    • Dynein achieves processive motion using both stochastic and coordinated stepping
    • Qiu, W., Derr, N. D., Goodman, B. S., Villa, E., Wu, D., Shih, W., et al. (2012). Dynein achieves processive motion using both stochastic and coordinated stepping. Nat. Struct.Mol. Biol. 19, 193-200. doi: 10.1038/nsmb.2205
    • (2012) Nat. Struct.Mol. Biol , vol.19 , pp. 193-200
    • Qiu, W.1    Derr, N.D.2    Goodman, B.S.3    Villa, E.4    Wu, D.5    Shih, W.6
  • 72
    • 33746253688 scopus 로고    scopus 로고
    • Single-molecule analysis of dynein processivity and stepping behavior
    • Reck-Peterson, S. L., Yildiz, A., Carter, A. P., Gennerich, A., Zhang, N., and Vale, R. D. (2006). Single-molecule analysis of dynein processivity and stepping behavior. Cell 126, 335-348. doi: 10.1016/j.cell.2006.05.046
    • (2006) Cell , vol.126 , pp. 335-348
    • Reck-Peterson, S.L.1    Yildiz, A.2    Carter, A.P.3    Gennerich, A.4    Zhang, N.5    Vale, R.D.6
  • 74
    • 84867367747 scopus 로고    scopus 로고
    • ATP-driven remodeling of the linker domain in the dynein motor
    • Roberts, A. J., Malkova, B., Walker, M. L., Sakakibara, H., Numata, N., Kon, T., et al. (2012). ATP-driven remodeling of the linker domain in the dynein motor. Structure 20, 1670-1680. doi: 10.1016/j.str.2012.07.003
    • (2012) Structure , vol.20 , pp. 1670-1680
    • Roberts, A.J.1    Malkova, B.2    Walker, M.L.3    Sakakibara, H.4    Numata, N.5    Kon, T.6
  • 75
    • 59049095230 scopus 로고    scopus 로고
    • AAA+ Ring and linker swing mechanism in the dynein motor
    • Roberts, A. J., Numata, N., Walker, M. L., Kato, Y. S., Malkova, B., Kon, T., et al. (2009). AAA+ Ring and linker swing mechanism in the dynein motor. Cell 136, 485-495. doi: 10.1016/j.cell.2008.11.049
    • (2009) Cell , vol.136 , pp. 485-495
    • Roberts, A.J.1    Numata, N.2    Walker, M.L.3    Kato, Y.S.4    Malkova, B.5    Kon, T.6
  • 76
    • 84906071016 scopus 로고    scopus 로고
    • Cytoplasmic dynein pushes the cytoskeletal meshwork forward during axonal elongation
    • Roossien, D. H., Lamoureux, P., and Miller, K. E. (2014). Cytoplasmic dynein pushes the cytoskeletal meshwork forward during axonal elongation. J. Cell Sci. 127, 3593-3602. doi: 10.1242/jcs.152611
    • (2014) J. Cell Sci , vol.127 , pp. 3593-3602
    • Roossien, D.H.1    Lamoureux, P.2    Miller, K.E.3
  • 77
    • 0037119990 scopus 로고    scopus 로고
    • Reorganization of the microtubule array in prophase/prometaphase requires cytoplasmic dynein-dependent microtubule transport
    • Rusan, N. M., Tulu, U. S., Fagerstrom, C., and Wadsworth, P. (2002). Reorganization of the microtubule array in prophase/prometaphase requires cytoplasmic dynein-dependent microtubule transport. J. Cell Biol. 158, 997-1003. doi: 10.1083/jcb.200204109
    • (2002) J. Cell Biol , vol.158 , pp. 997-1003
    • Rusan, N.M.1    Tulu, U.S.2    Fagerstrom, C.3    Wadsworth, P.4
  • 78
    • 84931022346 scopus 로고    scopus 로고
    • The dynein inhibitor Ciliobrevin D inhibits the bidirectional transport of organelles along sensory axons and impairs NGF- mediated regulation of growth cones and axon branches. Dev
    • Sainath, R., and Gallo, G. (2014). The dynein inhibitor Ciliobrevin D inhibits the bidirectional transport of organelles along sensory axons and impairs NGF- mediated regulation of growth cones and axon branches. Dev. Neurobiol. 75, 757-777. doi: 10.1002/dneu.22246
    • (2014) Neurobiol , vol.75 , pp. 757-777
    • Sainath, R.1    Gallo, G.2
  • 79
    • 0344390094 scopus 로고
    • Direction of active sliding of microtubules in Tetrahymena cilia
    • Sale, W. S., and Satir, P. (1977). Direction of active sliding of microtubules in Tetrahymena cilia. Proc. Natl. Acad. Sci. U.S.A. 74, 2045-2049.
    • (1977) Proc. Natl. Acad. Sci. U.S.A , vol.74 , pp. 2045-2049
    • Sale, W.S.1    Satir, P.2
  • 80
    • 84922537676 scopus 로고    scopus 로고
    • Bicaudal d family adaptor proteins control the velocity of Dynein-based movements
    • Schlager, M. A., Serra-Marques, A., Grigoriev, I., Gumy, G. F., Esteves da Silva, M., Wulf, P. S., et al. (2014). Bicaudal d family adaptor proteins control the velocity of Dynein-based movements. Cell Rep. 8, 1248-1256. doi: 10.1016/j.celrep.2014.07.052
    • (2014) Cell Rep , vol.8 , pp. 1248-1256
    • Schlager, M.A.1    Serra-Marques, A.2    Grigoriev, I.3    Gumy, G.F.4    Esteves Da Silva, M.5    Wulf, P.S.6
  • 81
    • 14844310234 scopus 로고    scopus 로고
    • Functional analysis of cytoplasmic dynein heavy chain in Caenorhabditis elegans with fast-acting temperature-sensitive mutations. Mol. Biol
    • Schmidt, D. J., Rose, D. J., Saxton, W. M., and Strome, S. (2005). Functional analysis of cytoplasmic dynein heavy chain in Caenorhabditis elegans with fast-acting temperature-sensitive mutations. Mol. Biol. Cell 16, 1200-1212. doi: 10.1091/mbc.E04-06-0523
    • (2005) Cell , vol.16 , pp. 1200-1212
    • Schmidt, D.J.1    Rose, D.J.2    Saxton, W.M.3    Strome, S.4
  • 82
    • 0006163872 scopus 로고
    • Dynein is the motor for retrograde axonal transport of organelles
    • Schnapp, B. J., and Reese, T. S. (1989). Dynein is the motor for retrograde axonal transport of organelles. Proc. Natl. Acad. Sci. U.S.A. 86, 1548-1552.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 1548-1552
    • Schnapp, B.J.1    Reese, T.S.2
  • 84
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer, T. A., and Sheetz, M. P. (1991). Two activators of microtubule-based vesicle transport. J. Cell Biol. 115, 1309-1318. doi: 10.1083/jcb.115.5.1309
    • (1991) J. Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 85
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus end-directed motor for membranous organelles
    • Schroer, T. A., Steuer, E. R., and Sheetz, M. P. (1989). Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell 56, 937-946. doi: 10.1016/0092-8674(89)90627-2
    • (1989) Cell , vol.56 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 86
    • 84881517528 scopus 로고    scopus 로고
    • Intraflagellar transport drives flagellar surface motility
    • Shih, S. M., Engel, B. D., Kocabas, F., Bilyard, T., Gennerich, A., Marshall, W. F., et al. (2013). Intraflagellar transport drives flagellar surface motility. Elife 2:e00744. doi: 10.7554/eLife.00744
    • (2013) Elife , vol.2 , pp. 2
    • Shih, S.M.1    Engel, B.D.2    Kocabas, F.3    Bilyard, T.4    Gennerich, A.5    Marshall, W.F.6
  • 87
    • 84904664537 scopus 로고    scopus 로고
    • Direct kinetochore-spindle pole connections are not required for chromosome segregation
    • Sikirzhytski, V., Magidson, V., Steinman, J. B., He, J., Le Berre, M., Tikhonenko, I., et al. (2014). Direct kinetochore-spindle pole connections are not required for chromosome segregation. J. Cell Biol. 206, 231-243. doi: 10.1083/jcb.201401090
    • (2014) J. Cell Biol , vol.206 , pp. 231-243
    • Sikirzhytski, V.1    Magidson, V.2    Steinman, J.B.3    He, J.4    Le Berre, M.5    Tikhonenko, I.6
  • 88
    • 84870551021 scopus 로고    scopus 로고
    • Nerve growth factor-induced formation of axonal filopodia and collateral branches involves the intra-axonal synthesis of regulators of the actin-nucleating Arp2/3 complex
    • Spillane, M., Ketschek, A., Donnelly, C. J., Pacheco, A., Twiss, J. L., and Gallo, G. (2012). Nerve growth factor-induced formation of axonal filopodia and collateral branches involves the intra-axonal synthesis of regulators of the actin-nucleating Arp2/3 complex. J. Neurosci. 32, 17671-17689. doi: 10.1523/JNEUROSCI.1079-12.2012
    • (2012) J. Neurosci , vol.32 , pp. 17671-17689
    • Spillane, M.1    Ketschek, A.2    Donnelly, C.J.3    Pacheco, A.4    Twiss, J.L.5    Gallo, G.6
  • 89
    • 78751539635 scopus 로고    scopus 로고
    • Functional dissection of LIS1 and NDEL1 towards understanding the molecular mechanisms of cytoplasmic dynein regulation
    • Torisawa, T., Nakayama, A., Furuta, K., Yamada, M., Hirotsune, S., and Toyoshima, Y. Y. (2011). Functional dissection of LIS1 and NDEL1 towards understanding the molecular mechanisms of cytoplasmic dynein regulation. J. Biol. Chem. 286, 1959-1965. doi: 10.1074/jbc.M1110.169847
    • (2011) J. Biol. Chem , vol.286 , pp. 1959-1965
    • Torisawa, T.1    Nakayama, A.2    Furuta, K.3    Yamada, M.4    Hirotsune, S.5    Toyoshima, Y.Y.6
  • 90
    • 84963853379 scopus 로고    scopus 로고
    • Lis1 regulates dynein by sterically blocking its mechanochemical cycle
    • Toropova, K., Zou, S., Roberts, A. J., Redwine, W. B., Goodman, B. S., Reck- Peterson, S. L., et al. (2014). Lis1 regulates dynein by sterically blocking its mechanochemical cycle. Elife 3:e03372. doi: 10.7554/eLife.03372
    • (2014) Elife , vol.3 , pp. 3
    • Toropova, K.1    Zou, S.2    Roberts, A.J.3    Redwine, W.B.4    Goodman, B.S.5    Reck-Peterson, S.L.6
  • 91
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale, R. D. (2003). The molecular motor toolbox for intracellular transport. Cell112, 467-480. doi: 10.1016/S0092-8674(03)00111-9
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 92
    • 0032756658 scopus 로고    scopus 로고
    • Role of dynactin in endocytic traffic: Effects of dynamitin overexpression andcolocalizationwithCLIP-170
    • Valetti, C., Wetzel, D. M., Schrader, M., Hasbani, M. J., Gill, S. R., Kreis, T., et al. (1999). Role of dynactin in endocytic traffic: effects of dynamitin overexpression andcolocalizationwithCLIP-170 Mol Biol. Cell 10,4107-4120. doi: 10.1091/mbc.10.12.4107
    • (1999) Mol Biol. Cell , vol.10 , pp. 4107-4120
    • Valetti, C.1    Wetzel, D.M.2    Schrader, M.3    Hasbani, M.J.4    Gill, S.R.5    Kreis, T.6
  • 93
    • 84857717466 scopus 로고    scopus 로고
    • Multiple modes of cytoplasmic dynein regulation
    • Vallee, R. B., McKenney, R. J., and Ori-McKenney, K. M. (2012). Multiple modes of cytoplasmic dynein regulation. Nat. Cell Biol. 14, 224-230. doi: 10.1038/ncb2420
    • (2012) Nat. Cell Biol , vol.14 , pp. 224-230
    • Vallee, R.B.1    McKenney, R.J.2    Ori-McKenney, K.M.3
  • 94
    • 84857717466 scopus 로고    scopus 로고
    • Multiple modes of cytoplasmic dynein regulation
    • Vallee, R. B., McKenney, R. J., and Ori-McKenney, K. M. (2012). Multiple modes of cytoplasmic dynein regulation. Nat. Cell Biol. 14, 224-230. doi: 10.1038/ncb2420
    • (2012) Nat. Cell Biol , vol.14 , pp. 224-230
    • Vallee, R.B.1    McKenney, R.J.2    Ori-McKenney, K.M.3
  • 95
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dyne in with dyn act in and CLIP-170 at Microtubule distalends
    • Vaughan,K.T.,Tynan,S.H.,Faulkner,N.E.,Echeverri,C.J.,and Vallee,R.B. (1999).Colocalization of cytoplasmic dyne in with dyn act in and CLIP-170 at Microtubule distalends. J. Cell Sci. 112(Pt10),1437-1447
    • (1999) J. Cell Sci , vol.112 , Issue.Pt10 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 96
    • 0037157845 scopus 로고    scopus 로고
    • A role for regulated binding ofp150(Glued) to microtubule plus ends in organelle transport
    • Vaughan, P. S., Miura, P., Henderson, M., Byrne, B., and Vaughan, K. T. (2002). A role for regulated binding ofp150(Glued) to microtubule plus ends in organelle transport. J. CellBiol. 158, 305-319.doi: 10.1083/jcb.200201029
    • (2002) J. Cellbiol , vol.158 , pp. 305-319
    • Vaughan, P.S.1    Miura, P.2    Henderson, M.3    Byrne, B.4    Vaughan, K.T.5
  • 97
    • 84923914152 scopus 로고    scopus 로고
    • Scaffold protein JLP is critical for CD40 signaling in B lymphocytes
    • Wang, H. M., Yan, Q., Yang, T., Cheng, H., Du, J., Yoshioka, K., et al. (2015). Scaffold protein JLP is critical for CD40 signaling in B lymphocytes. J. Biol. Chem. 290, 5256-5266. doi: 10.1074/jbc.M114.618496
    • (2015) J. Biol. Chem , vol.290 , pp. 5256-5266
    • Wang, H.M.1    Yan, Q.2    Yang, T.3    Cheng, H.4    Du, J.5    Yoshioka, K.6
  • 98
    • 0028986631 scopus 로고
    • The p150 Glued component of the dynactin complex binds to both microtubules and the actin- related protein centractin (Arp-1)
    • Waterman-Storer, C. M., Karki, S., and Holzbaur, E. L. (1995). The p150 Glued component of the dynactin complex binds to both microtubules and the actin- related protein centractin (Arp-1). Proc. Natl. Acad. Sci. U.S.A. 92, 1634-1638
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 99
    • 0032622374 scopus 로고    scopus 로고
    • Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellular processes
    • Wittmann, T., and Hyman, T. (1999). Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellular processes. Methods Cell Biol. 61, 137-143.
    • (1999) Methods Cell Biol , vol.61 , pp. 137-143
    • Wittmann, T.1    Hyman, T.2
  • 100
    • 78649329736 scopus 로고    scopus 로고
    • A model for cleavage plane determination in early amphibian and fish embryos
    • Wuhr, M., Tan, E. S., Parker, S. K., Detrich, H. W. III, and Mitchison, T. J. (2010). A model for cleavage plane determination in early amphibian and fish embryos. Curr. Biol. 20, 2040-2045. doi: 10.1016/j.cub.2010.10.024
    • (2010) Curr. Biol , vol.20 , pp. 2040-2045
    • Wuhr, M.1    Tan, E.S.2    Parker, S.K.3    Detrich, H.4    Mitchison, T.J.5
  • 101
    • 53549119395 scopus 로고    scopus 로고
    • LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein
    • Yamada, M., Toba, S., Yoshida, Y., Haratani, K., Mori, D., Yano, Y., et al. (2008). LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein. EMBO J. 19, 2471-2483. doi:10.1038/emboj.2008.182
    • (2008) EMBO J , vol.19 , pp. 2471-2483
    • Yamada, M.1    Toba, S.2    Yoshida, Y.3    Haratani, K.4    Mori, D.5    Yano, Y.6
  • 102
    • 84881512243 scopus 로고    scopus 로고
    • Single molecule imaging reveals a major role for diffusion in the exploration of ciliary space by signaling receptors
    • Ye, F., Breslow, D. K., Koslover, E. F., Spakowitz, A. J., Nelson, W. J., and Nachury, M. V. (2013). Single molecule imaging reveals a major role for diffusion in the exploration of ciliary space by signaling receptors. Elife 2:e00654. doi: 10.7554/eLife.00654
    • (2013) Elife , vol.2 , pp. 2
    • Ye, F.1    Breslow, D.K.2    Koslover, E.F.3    Spakowitz, A.J.4    Nelson, W.J.5    Nachury, M.V.6
  • 103
    • 84884198012 scopus 로고    scopus 로고
    • Centrosome repositioning in T cells is biphasic and driven by microtubule end-on capture-shrinkage
    • Yi, J., Wu, X., Chung, A. H., Chen, J. K., Kapoor, T. M., and Hammer, J. A. (2013). Centrosome repositioning in T cells is biphasic and driven by microtubule end-on capture-shrinkage. J. Cell Biol. 202, 779-792. doi:10.1083/jcb.201301004
    • (2013) J. Cell Biol , vol.202 , pp. 779-792
    • Yi, J.1    Wu, X.2    Chung, A.H.3    Chen, J.K.4    Kapoor, T.M.5    Hammer, J.A.6
  • 104
    • 80155203800 scopus 로고    scopus 로고
    • High-resolution imaging reveals indirect coordination of opposite motors and a role for LIS1 in high-load axonal transport
    • Yi, J. Y., Ori-McKenney, K. M., Mckenney, R. J., Vershinin, M., Gross, S. P., and Vallee, R. B. (2011). High-resolution imaging reveals indirect coordination of opposite motors and a role for LIS1 in high-load axonal transport. J. Cell Biol. 195, 193-201. doi: 10.1083/jcb.201104076
    • (2011) J. Cell Biol , vol.195 , pp. 193-201
    • Yi, J.Y.1    Ori-McKenney, K.M.2    McKenney, R.J.3    Vershinin, M.4    Gross, S.P.5    Vallee, R.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.