메뉴 건너뛰기




Volumn 122, Issue 12, 2009, Pages 1979-1989

Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells

Author keywords

Dynein; ER; Kinesin; Microtubule

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN 1; DYNACTIN; KINESIN; MICROTUBULE ASSOCIATED PROTEIN;

EID: 68949167657     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.041962     Document Type: Article
Times cited : (107)

References (60)
  • 1
    • 0028943648 scopus 로고
    • Protein phosphatase 1 regulates the cytoplasmic dynein-driven formation of endoplasmic reticulum networks in vitro
    • Allan, V. (1995). Protein phosphatase 1 regulates the cytoplasmic dynein-driven formation of endoplasmic reticulum networks in vitro. J. Cell Biol. 128, 879-891.
    • (1995) J. Cell Biol , vol.128 , pp. 879-891
    • Allan, V.1
  • 2
    • 0025829696 scopus 로고
    • Cell cycle control of microtubule-based membrane transport and tubule formation in vitro
    • Allan, V. J. and Vale, R. D. (1991). Cell cycle control of microtubule-based membrane transport and tubule formation in vitro. J. Cell Biol. 113, 347-359.
    • (1991) J. Cell Biol , vol.113 , pp. 347-359
    • Allan, V.J.1    Vale, R.D.2
  • 3
    • 33947607769 scopus 로고    scopus 로고
    • The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport
    • Araki, Y., Kawano, T., Taru, H., Saito, Y., Wada, S., Miyamoto, K., Kobayashi, H., Ishikawa, H. O., Ohsugi, Y., Yamamoto, T. et al. (2007). The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport. EMBO J. 26, 1475-1486.
    • (2007) EMBO J , vol.26 , pp. 1475-1486
    • Araki, Y.1    Kawano, T.2    Taru, H.3    Saito, Y.4    Wada, S.5    Miyamoto, K.6    Kobayashi, H.7    Ishikawa, H.O.8    Ohsugi, Y.9    Yamamoto, T.10
  • 5
    • 1242349907 scopus 로고    scopus 로고
    • Kinesin dependent, rapid, bi-directional transport of ER sub-compartment in dendrites of hippocampal neurons
    • Bannai, H., Inoue, T., Nakayama, T., Hattori, M. and Mikoshiba, K. (2004). Kinesin dependent, rapid, bi-directional transport of ER sub-compartment in dendrites of hippocampal neurons. J. Cell Sci. 117, 163-175.
    • (2004) J. Cell Sci , vol.117 , pp. 163-175
    • Bannai, H.1    Inoue, T.2    Nakayama, T.3    Hattori, M.4    Mikoshiba, K.5
  • 6
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann, O. and Walz, B. (2001). Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int. Rev. Cytol. 205, 149-214.
    • (2001) Int. Rev. Cytol , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 7
    • 33745752369 scopus 로고    scopus 로고
    • Endoplasmic reticulum architecture: Structures in flux
    • Borgese, N., Francolini, M. and Snapp, E. (2006). Endoplasmic reticulum architecture: structures in flux. Curr. Opin. Cell Biol. 18, 358-364.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 358-364
    • Borgese, N.1    Francolini, M.2    Snapp, E.3
  • 8
    • 0032872611 scopus 로고    scopus 로고
    • Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex
    • Bridgman, P. C. (1999). Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex. J. Cell Biol. 146, 1045-1060.
    • (1999) J. Cell Biol , vol.146 , pp. 1045-1060
    • Bridgman, P.C.1
  • 9
    • 29144463168 scopus 로고    scopus 로고
    • Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility
    • Brough, D., Schell, M. J. and Irvine, R. F. (2005). Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility. Biochem. J. 392, 291-297.
    • (2005) Biochem. J , vol.392 , pp. 291-297
    • Brough, D.1    Schell, M.J.2    Irvine, R.F.3
  • 10
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
    • (1997) J. Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 11
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motot domain
    • Coy, D. L., Hancock, W. O., Wagenbach, M. and Howard, J. (1999). Kinesin's tail domain is an inhibitory regulator of the motot domain. Nat. Cell Biol. 1, 288-292.
    • (1999) Nat. Cell Biol , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 13
    • 0024041810 scopus 로고
    • Microtubule dependent formation of a tubularvesicular network with characteristics of the endoplasmic reticulum from cultured cell extracts
    • Dabora, S. L. and Sheetz, M. P. (1988). Microtubule dependent formation of a tubularvesicular network with characteristics of the endoplasmic reticulum from cultured cell extracts. Cell 54, 27-35.
    • (1988) Cell , vol.54 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 15
    • 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. Cell Biol. 132, 617-633.
    • (1996) J. Cell Biol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 16
    • 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. and Schroer, T. A. (1999). Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end. J. Cell Biol. 147, 307-320.
    • (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    Schroer, T.A.7
  • 17
    • 0028019867 scopus 로고
    • Kinesin-mediated organelle translocation revealed by specific cellular manipulations
    • Feiguin, F., Ferreira, A., Kosik, K. S. and Caceres, A. (1994). Kinesin-mediated organelle translocation revealed by specific cellular manipulations. J. Cell Biol. 127, 1021-1039.
    • (1994) J. Cell Biol , vol.127 , pp. 1021-1039
    • Feiguin, F.1    Ferreira, A.2    Kosik, K.S.3    Caceres, A.4
  • 18
    • 34247140259 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum structure during mouse oocyte maturation are controlled by the cytoskeleton and cytoplasmic dynein
    • FitzHarris, G., Marangos, P. and Carroll, J. (2007). Changes in endoplasmic reticulum structure during mouse oocyte maturation are controlled by the cytoskeleton and cytoplasmic dynein. Dev. Biol. 305, 133-144.
    • (2007) Dev. Biol , vol.305 , pp. 133-144
    • FitzHarris, G.1    Marangos, P.2    Carroll, J.3
  • 19
    • 0032977841 scopus 로고    scopus 로고
    • The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment
    • Greenfield, J. J. and High, S. (1999). The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment. J. Cell Sci. 112, 1477-1486.
    • (1999) J. Cell Sci , vol.112 , pp. 1477-1486
    • Greenfield, J.J.1    High, S.2
  • 21
    • 53849087134 scopus 로고    scopus 로고
    • Kinesin-1 (uKHC/KIF5B) is required for bidirectional motility of ER exit sites and efficient ER-to-Golgi transport
    • Gupta, V., Palmer, K. J., Spence, P., Hudson, A. and Stephens, D. J. (2008). Kinesin-1 (uKHC/KIF5B) is required for bidirectional motility of ER exit sites and efficient ER-to-Golgi transport. Traffic 9, 1850-1866.
    • (2008) Traffic , vol.9 , pp. 1850-1866
    • Gupta, V.1    Palmer, K.J.2    Spence, P.3    Hudson, A.4    Stephens, D.J.5
  • 22
    • 26044483546 scopus 로고    scopus 로고
    • NSF/SNAPs and p97/ p47/VCIP135 are sequentially required for cell cycle-dependent reformation of the ER network
    • Kano, F., Kondo, H., Yamamoto, A., Kaneko, Y., Uchiyama, K., Hosokawa, N., Nagata, K. and Murata, M. (2005). NSF/SNAPs and p97/ p47/VCIP135 are sequentially required for cell cycle-dependent reformation of the ER network. Genes Cells 10, 989-999.
    • (2005) Genes Cells , vol.10 , pp. 989-999
    • Kano, F.1    Kondo, H.2    Yamamoto, A.3    Kaneko, Y.4    Uchiyama, K.5    Hosokawa, N.6    Nagata, K.7    Murata, M.8
  • 23
    • 0034674337 scopus 로고    scopus 로고
    • Temperature dependence of force, velocity and processivity of single kinesin molecules
    • Kawagishi, K. and Ishiwata, S. (2000). Temperature dependence of force, velocity and processivity of single kinesin molecules. Biochem. Biophys. Res. Commun. 272, 895-899.
    • (2000) Biochem. Biophys. Res. Commun , vol.272 , pp. 895-899
    • Kawagishi, K.1    Ishiwata, S.2
  • 24
    • 0035844877 scopus 로고    scopus 로고
    • Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment
    • Klopfenstein, D. R., Klumperman, J., Lustig, A., Kammerer, R. A., Oorschot, V. and Hauri, H. P. (2001). Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment. J. Cell Biol. 153, 1287-1300.
    • (2001) J. Cell Biol , vol.153 , pp. 1287-1300
    • Klopfenstein, D.R.1    Klumperman, J.2    Lustig, A.3    Kammerer, R.A.4    Oorschot, V.5    Hauri, H.P.6
  • 26
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordingated movement?
    • Kural, C., Kim, H., Syed, S., Goshima, G., Gelfand, V. I. and Selvin, P. R. (2005). Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordingated movement? Science 308, 1469-1472.
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5    Selvin, P.R.6
  • 27
    • 0033052099 scopus 로고    scopus 로고
    • Microtubule-based endoplasmic reticulum motility in Xenopus laevis: Activation of membrane-associated kinesin during development
    • Lane, J. D. and Allan, V. J. (1999). Microtubule-based endoplasmic reticulum motility in Xenopus laevis: activation of membrane-associated kinesin during development. Mol. Biol. Cell 10, 1909-1922.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1909-1922
    • Lane, J.D.1    Allan, V.J.2
  • 28
    • 0023693945 scopus 로고
    • Dynamic behavior of endoplasmic reticulum in living cells
    • Lee, C. and Chen, L. B. (1988). Dynamic behavior of endoplasmic reticulum in living cells. Cell 54, 37-46.
    • (1988) Cell , vol.54 , pp. 37-46
    • Lee, C.1    Chen, L.B.2
  • 29
    • 0024456323 scopus 로고
    • Construction of the endoplasmic reticulum
    • Lee, C., Ferguson, M. and Chen, L. B. (1989). Construction of the endoplasmic reticulum. J. Cell Biol. 109, 2045-2055.
    • (1989) J. Cell Biol , vol.109 , pp. 2045-2055
    • Lee, C.1    Ferguson, M.2    Chen, L.B.3
  • 30
    • 0034642479 scopus 로고    scopus 로고
    • EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue
    • Nakagawa, H., Koyama, K., Murata, Y., Morito, M., Akiyama, T. and Nakamura, Y. (2000). EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue. Oncogene 19, 210-216.
    • (2000) Oncogene , vol.19 , pp. 210-216
    • Nakagawa, H.1    Koyama, K.2    Murata, Y.3    Morito, M.4    Akiyama, T.5    Nakamura, Y.6
  • 31
    • 0026632855 scopus 로고
    • Expression of the human kinesin heavy chain gene in CV-1 cells: Interaction of the C-terminal domain with cytoplasmic microtubules
    • Navone, F., Niclas, J., Hom-Booher, N., Sparks, L., Bernstein, H. D., McCaffrey, G. and Vale, R. D. (1992). Expression of the human kinesin heavy chain gene in CV-1 cells: interaction of the C-terminal domain with cytoplasmic microtubules. J. Cell Biol. 117, 1263-1275.
    • (1992) J. Cell Biol , vol.117 , pp. 1263-1275
    • Navone, F.1    Niclas, J.2    Hom-Booher, N.3    Sparks, L.4    Bernstein, H.D.5    McCaffrey, G.6    Vale, R.D.7
  • 32
    • 0029954709 scopus 로고    scopus 로고
    • Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport
    • Niclas, J., Allan, V. J. and Vale, R. D. (1996). Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J. Cell Biol. 133, 585-593.
    • (1996) J. Cell Biol , vol.133 , pp. 585-593
    • Niclas, J.1    Allan, V.J.2    Vale, R.D.3
  • 33
    • 34447519108 scopus 로고    scopus 로고
    • Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes
    • Nikonov, A. V., Hauri, H., Lauring, B. and Kreibich, G. (2007). Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes. J. Cell Sci. 120, 2248-2258.
    • (2007) J. Cell Sci , vol.120 , pp. 2248-2258
    • Nikonov, A.V.1    Hauri, H.2    Lauring, B.3    Kreibich, G.4
  • 34
    • 0344420336 scopus 로고    scopus 로고
    • LIS1 association with dynactin is required for nuclear motility and genomic union in the fertilized mammalian oocyte
    • Payne, C., St., John, J., CRamalho-Santos, J. and Schatten, G. (2003). LIS1 association with dynactin is required for nuclear motility and genomic union in the fertilized mammalian oocyte. Cell Motil. Cytoskeleton 56, 245-251.
    • (2003) Cell Motil. Cytoskeleton , vol.56 , pp. 245-251
    • Payne, C.1    St2    John, J.3    CRamalho-Santos, J.4    Schatten, G.5
  • 35
    • 36849012562 scopus 로고    scopus 로고
    • Endoplasmic reticulum remains continuous and undergoes sheet-to-tubule transformation during cell division in mammalian cells
    • Puhka, M., Vihinen, H., Joensuu, M. and Jokitalo, E. (2007). Endoplasmic reticulum remains continuous and undergoes sheet-to-tubule transformation during cell division in mammalian cells. J. Cell Biol. 179, 895-909.
    • (2007) J. Cell Biol , vol.179 , pp. 895-909
    • Puhka, M.1    Vihinen, H.2    Joensuu, M.3    Jokitalo, E.4
  • 36
    • 0027178714 scopus 로고
    • Structural reorganization of the rough endoplasmic reticulum without size expansion accounts for dexamethasone-induced secretory activity in AR42J cells
    • Rajasekaran, A. K., Morimoto, T., Hanzel, D. K., Rodriguez-Boulan, E. and Kreibich, G. (1993). Structural reorganization of the rough endoplasmic reticulum without size expansion accounts for dexamethasone-induced secretory activity in AR42J cells. J. Cell Sci. 105, 333-345.
    • (1993) J. Cell Sci , vol.105 , pp. 333-345
    • Rajasekaran, A.K.1    Morimoto, T.2    Hanzel, D.K.3    Rodriguez-Boulan, E.4    Kreibich, G.5
  • 37
    • 0031105358 scopus 로고    scopus 로고
    • Movement of nuclei along microtubules in Xenopus egg extracts
    • Reinsch, S. and Karsenti, E. (1997). Movement of nuclei along microtubules in Xenopus egg extracts. Curr. Biol. 7, 211-214.
    • (1997) Curr. Biol , vol.7 , pp. 211-214
    • Reinsch, S.1    Karsenti, E.2
  • 38
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N., Palmer, A. E. and Tsien, R. Y. (2004). Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22, 1567-1572.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 39
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata, Y., Voeltz, G. K. and Rapoport, T. A. (2006). Rough sheets and smooth tubules. Cell 126, 435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 40
  • 41
  • 42
    • 57149145788 scopus 로고    scopus 로고
    • Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplet movement
    • Shubeita, G. T., Tran, S. L., Xu, J., Cermelli, S., Cotton, S. L., Welte, M. A. and Gross, S. P. (2008). Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplet movement. Cell 135, 1098-1107.
    • (2008) Cell , vol.135 , pp. 1098-1107
    • Shubeita, G.T.1    Tran, S.L.2    Xu, J.3    Cermelli, S.4    Cotton, S.L.5    Welte, M.A.6    Gross, S.P.7
  • 44
  • 46
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • Tanaka, Y., Kanai, Y., Okada, Y., Nonaka, S., Takeda, S., Harada, A. and Hirokawa, N. (1998). Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93, 1147-1158.
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 47
    • 0027987340 scopus 로고
    • Interactions among endoplasmic reticulum, microtubules, and retrograde movements of the cell surface
    • Terasaki, M. and Reese, T. S. (1994). Interactions among endoplasmic reticulum, microtubules, and retrograde movements of the cell surface. Cell Motil. Cytoskeleton 29, 291-300.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 291-300
    • Terasaki, M.1    Reese, T.S.2
  • 48
    • 0021748350 scopus 로고
    • Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes
    • Terasaki, M., Song, J., Wong, J. R., Weiss, M. J. and Chen, L. B. (1984). Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes. Cell 38, 101-108.
    • (1984) Cell , vol.38 , pp. 101-108
    • Terasaki, M.1    Song, J.2    Wong, J.R.3    Weiss, M.J.4    Chen, L.B.5
  • 49
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki, M., Chen, L. B. and Fujiwara, K. (1986). Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103, 1557-1568.
    • (1986) J. Cell Biol , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.B.2    Fujiwara, K.3
  • 50
    • 33646409613 scopus 로고    scopus 로고
    • Morphogenesis of the endoplasmic reticulum: Beyond active membrane expansion
    • Vedrenne, C. and Hauri, H. (2006). Morphogenesis of the endoplasmic reticulum: beyond active membrane expansion. Traffic 7, 639-646.
    • (2006) Traffic , vol.7 , pp. 639-646
    • Vedrenne, C.1    Hauri, H.2
  • 51
    • 16344366871 scopus 로고    scopus 로고
    • Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules
    • Vedrenne, C., Klopfenstein, D. R. and Hauri, H. (2005). Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules. Mol. Biol. Cell 16, 1928-1937.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1928-1937
    • Vedrenne, C.1    Klopfenstein, D.R.2    Hauri, H.3
  • 52
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz, G. K., Prinz, W. A., Shibata, Y., Rist, J. M. and Rapoport, T. A. (2006). A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 53
    • 0032474825 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms
    • Waterman-Storer, C. M. and Salmon, E. D. (1998). Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms. Curr. Biol. 8, 798-806.
    • (1998) Curr. Biol , vol.8 , pp. 798-806
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 54
    • 12344277564 scopus 로고    scopus 로고
    • Coupling of ER exit to microtubules through direct interaction of COPII with dynactin
    • Watson, P., Forster, R., Palmer, K. J., Pepperkok, R. and Stephens, D. J. (2005). Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat. Cell Biol. 7, 48-55.
    • (2005) Nat. Cell Biol , vol.7 , pp. 48-55
    • Watson, P.1    Forster, R.2    Palmer, K.J.3    Pepperkok, R.4    Stephens, D.J.5
  • 55
    • 0036196575 scopus 로고    scopus 로고
    • Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis
    • Wedlich-Söldner, R., Schulz, I., Straube, A. and Steinberg, G. (2002). Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis. Mol. Biol. Cell 13, 965-977.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 965-977
    • Wedlich-Söldner, R.1    Schulz, I.2    Straube, A.3    Steinberg, G.4
  • 56
    • 3142642871 scopus 로고    scopus 로고
    • Bidirectional transport along microtubules
    • Welte, M. A. (2004). Bidirectional transport along microtubules. Curr. Biol. 14, R525-R537.
    • (2004) Curr. Biol , vol.14
    • Welte, M.A.1
  • 57
    • 0037175377 scopus 로고    scopus 로고
    • Activation of myosin V-based motility and F-actin-dependent network formation of endoplasmic reticulum during mitosis
    • Wollert, T., Weiss, D. G., Gerdes, H. and Kuznetsov, S. A. (2002). Activation of myosin V-based motility and F-actin-dependent network formation of endoplasmic reticulum during mitosis. J. Cell Biol. 159, 571-577.
    • (2002) J. Cell Biol , vol.159 , pp. 571-577
    • Wollert, T.1    Weiss, D.G.2    Gerdes, H.3    Kuznetsov, S.A.4
  • 58
    • 33751572018 scopus 로고    scopus 로고
    • Cargo selection by specific kinesin light chain 1 isoforms
    • Wozniak, M. J. and Allan, V. J. (2006). Cargo selection by specific kinesin light chain 1 isoforms. EMBO J. 25, 5457-5468.
    • (2006) EMBO J , vol.25 , pp. 5457-5468
    • Wozniak, M.J.1    Allan, V.J.2
  • 59
    • 0027496649 scopus 로고
    • Roles of kinesin and kinesin-like proteins in sea urchin embryonic cell division: Evaluation using antibody microinjection
    • Wright, B. D., Terasaki, M. and Scholey, J. M. (1993). Roles of kinesin and kinesin-like proteins in sea urchin embryonic cell division: evaluation using antibody microinjection. J. Cell Biol. 123, 681-689.
    • (1993) J. Cell Biol , vol.123 , pp. 681-689
    • Wright, B.D.1    Terasaki, M.2    Scholey, J.M.3
  • 60
    • 36849001214 scopus 로고    scopus 로고
    • Microtubule motors regulate ISOC activation necessary to increase endothelial cell permeability
    • Wu, S., Chen, H., Alexeyev, M. F., King, J. A. C., Moore, T. M., Stevens, T. and Balczon, R. D. (2007). Microtubule motors regulate ISOC activation necessary to increase endothelial cell permeability. J. Biol. Chem. 282, 34801-34808.
    • (2007) J. Biol. Chem , vol.282 , pp. 34801-34808
    • Wu, S.1    Chen, H.2    Alexeyev, M.F.3    King, J.A.C.4    Moore, T.M.5    Stevens, T.6    Balczon, R.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.