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Volumn 4, Issue 10, 2002, Pages E236-E242

Motoring around the Golgi

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MEMBRANE PROTEIN; MYOSIN; SECRETORY PROTEIN;

EID: 0036796991     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1002-e236     Document Type: Review
Times cited : (177)

References (100)
  • 1
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in the organization of the Golgi complex
    • Thyberg, J. & Moskalewski, S. Role of microtubules in the organization of the Golgi complex. Exp. Cell Res. 246, 263-279 (1999).
    • (1999) Exp. Cell Res , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 2
    • 0024600674 scopus 로고
    • Reclustering of scattered Golgi elements occurs along microtubules
    • Ho, W. C., Allan, V. J., van Meer, G., Berger, E. G. & Kreis, T. E. Reclustering of scattered Golgi elements occurs along microtubules. Eur. J. Cell Biol. 48, 250-263 (1989).
    • (1989) Eur. J. Cell Biol , vol.48 , pp. 250-263
    • Ho, W.C.1    Allan, V.J.2    Van Meer, G.3    Berger, E.G.4    Kreis, T.E.5
  • 3
    • 0021189557 scopus 로고
    • Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane
    • Rogaliski, A., Bergmann, J. & Singer, S. Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane. J. Cell Biol. 99, 1101-1109 (1984).
    • (1984) J. Cell Biol , vol.99 , pp. 1101-1109
    • Rogaliski, A.1    Bergmann, J.2    Singer, S.3
  • 4
    • 0025228404 scopus 로고
    • Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum
    • Cooper, M. S., Cornell-Bell, A. H., Chernjavsky, A., Dani, J. W. & Smith, S. J. Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum. Cell 61, 135-145 (1990).
    • (1990) Cell , vol.61 , pp. 135-145
    • Cooper, M.S.1    Cornell-Bell, A.H.2    Chernjavsky, A.3    Dani, J.W.4    Smith, S.J.5
  • 5
    • 0034678043 scopus 로고    scopus 로고
    • Distinct cytoplasmic dynein complexes are transported by different mechanisms in axons
    • Susalka, S., Hancock, W. & Pfister, K. Distinct cytoplasmic dynein complexes are transported by different mechanisms in axons. Biochim. Biophys. Acta 1496, 76-88 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 76-88
    • Susalka, S.1    Hancock, W.2    Pfister, K.3
  • 6
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S. The dynein microtubule motor. Biochim. Biophys. Acta 1496, 60-75 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.1
  • 7
    • 0033400723 scopus 로고    scopus 로고
    • Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment
    • Roghi, C. & Allan, V. Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment. J. Cell Sci. 112, 4673-4685 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 4673-4685
    • Roghi, C.1    Allan, V.2
  • 8
    • 0032584612 scopus 로고    scopus 로고
    • Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity
    • Tai, A. W., Chuang, J.-Z. & Sung, C.-H. Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity. J. Biol. Chem. 273, 19639-19649 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 19639-19649
    • Tai, A.W.1    Chuang, J.-Z.2    Sung, C.-H.3
  • 9
    • 0035147268 scopus 로고    scopus 로고
    • Immunolocalization of cytoplasmic dynein and dynactin subunits in cultured macrophages: Enrichment on early endocytic organelles
    • Habermann, A., Schroer, T., Griffiths, G. & Burkhardt, J. Immunolocalization of cytoplasmic dynein and dynactin subunits in cultured macrophages: enrichment on early endocytic organelles. J. Cell Sci. 114, 229-240 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 229-240
    • Habermann, A.1    Schroer, T.2    Griffiths, G.3    Burkhardt, J.4
  • 10
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B., Ebersold, M. & Helenius, A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136, 1007-1021 (1997).
    • (1997) J. Cell Biol , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.2    Helenius, A.3
  • 11
    • 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., Echeverri, C., Nilsson, T. & Vallee, R. 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).
    • (1997) J. Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.1    Echeverri, C.2    Nilsson, T.3    Vallee, R.4
  • 12
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of Brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J. et al. Microtubule-dependent retrograde transport of proteins into the ER in the presence of Brefeldin A suggests an ER recycling pathway. Cell 60, 821-836 (1990).
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1
  • 13
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada, A. et al. Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 141, 51-59 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 51-59
    • Harada, A.1
  • 14
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan, P., Lesyzk, J. & Vaughan, K. Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin. J. Biol. Chem. 276, 26171-26179 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 26171-26179
    • Vaughan, P.1    Lesyzk, J.2    Vaughan, K.3
  • 15
    • 0030955328 scopus 로고    scopus 로고
    • ER-to-Golgi transport visualized in living cells
    • Presley, J. F. et al. ER-to-Golgi transport visualized in living cells. Nature 389, 81-85 (1997).
    • (1997) Nature , vol.389 , pp. 81-85
    • Presley, J.F.1
  • 16
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • Stephens, D. J. & Pepperkok, R. Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J. Cell Sci. 115, 1149-1160 (2002).
    • (2002) J. Cell Sci , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 17
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King, S. & Schroer, T. Dynactin increases the processivity of the cytoplasmic dynein motor. Nature Cell Biol. 2, 20-24 (1999).
    • (1999) Nature Cell Biol , vol.2 , pp. 20-24
    • King, S.1    Schroer, T.2
  • 18
    • 0001147917 scopus 로고    scopus 로고
    • Structure and function of dynactin
    • Schroer, T. Structure and function of dynactin. Seminars Cell Dev. Biol. 7, 321-328 (1996).
    • (1996) Seminars Cell Dev. Biol , vol.7 , pp. 321-328
    • Schroer, T.1
  • 19
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S. & Holzbaur, E. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 11, 45-53 (1999).
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.2
  • 20
    • 0034069115 scopus 로고    scopus 로고
    • ARP1 in Golgi organisation and attachment of manchette microtubules to the nucleus during mammalian spermatogenesis
    • Fouquet, J., Kann, M., Soues, S. & Melki, R. ARP1 in Golgi organisation and attachment of manchette microtubules to the nucleus during mammalian spermatogenesis. J. Cell Sci. 113, 877-886 (2000).
    • (2000) J. Cell Sci , vol.113 , pp. 877-886
    • Fouquet, J.1    Kann, M.2    Soues, S.3    Melki, R.4
  • 21
    • 0035965256 scopus 로고    scopus 로고
    • βIII spectrin binds to the Arp1 subunit of dynactin
    • Holleran, E. et al. βIII spectrin binds to the Arp1 subunit of dynactin. J. Biol. Chem. 276, 36598-36605 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 36598-36605
    • Holleran, E.1
  • 22
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran, E. A., Tokito, M. K., Karki, S. & Holzbaur, E. L. F. Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol. 135, 1815-1829 (1996).
    • (1996) J. Cell Biol , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 23
    • 0030923518 scopus 로고    scopus 로고
    • Na, K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin ankyrin G119 skeleton in Madin Darby canine kidney cells
    • Devarajan, P., Stabach, P., DeMatteis, M. & Morrow, J. Na, K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin ankyrin G119 skeleton in Madin Darby canine kidney cells. Proc. Natl Acad. Sci. USA 94, 10711-10716 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10711-10716
    • Devarajan, P.1    Stabach, P.2    DeMatteis, M.3    Morrow, J.4
  • 24
    • 0032564278 scopus 로고    scopus 로고
    • A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
    • Stankewich, M. et al. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proc. Natl Acad. Sci. USA 95, 14158-14163 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14158-14163
    • Stankewich, M.1
  • 25
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterisation of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organisation during mitosis
    • Echeverri, C. J., Paschal, B. M., Vaughan, K. T. & Vallee, R. B. Molecular characterisation of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organisation during mitosis. J. Cell Biol. 132, 617-633 (1996).
    • (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
  • 26
    • 0032701651 scopus 로고    scopus 로고
    • Dynactin is required for microtubule anchoring at centrosomes
    • Quintyne, N. et al. Dynactin is required for microtubule anchoring at centrosomes. J. Cell Biol. 147, 321-334 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 321-334
    • Quintyne, N.1
  • 27
    • 0032756658 scopus 로고    scopus 로고
    • Role of dynactin in endocytic traffic: Effects of dynamitin overexpression and colocalization with CLIP-170
    • Valetti, C. et al. Role of dynactin in endocytic traffic: effects of dynamitin overexpression and colocalization with CLIP-170. Mol. Biol. Cell 10, 4107-4120 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4107-4120
    • Valetti, C.1
  • 28
    • 0034693225 scopus 로고    scopus 로고
    • Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin
    • Tynan, S. H., Purohit, A., Doxsey, S. J. & Vallee, R. B. Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin. J. Biol. Chem. 275, 32763-32768 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 32763-32768
    • Tynan, S.H.1    Purohit, A.2    Doxsey, S.J.3    Vallee, R.B.4
  • 29
    • 0035954436 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport
    • Tai, A., Chuang, J.-Z. & Sung, C.-H. Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport. J. Cell Biol. 153, 1499-1509 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 1499-1509
    • Tai, A.1    Chuang, J.-Z.2    Sung, C.-H.3
  • 30
    • 0035422303 scopus 로고    scopus 로고
    • Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes
    • Hoogenraad, C. C. et al. Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes. EMBO J. 20, 4041-4054 (2001).
    • (2001) EMBO J , vol.20 , pp. 4041-4054
    • Hoogenraad, C.C.1
  • 31
    • 0029905303 scopus 로고    scopus 로고
    • Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles
    • Vaisberg, E. A., Grissom, P. M. & McIntosh, J. R. Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles. J. Cell Biol. 133, 831-842 (1996).
    • (1996) J. Cell Biol , vol.133 , pp. 831-842
    • Vaisberg, E.A.1    Grissom, P.M.2    McIntosh, J.R.3
  • 32
    • 0036198506 scopus 로고    scopus 로고
    • Identification of a novel light intermediate chain (D2LIC) for mammalian cytoplasmic dynein
    • Grissom, P., Vaisberg, E. & McIntosh, J. Identification of a novel light intermediate chain (D2LIC) for mammalian cytoplasmic dynein. Mol. Biol. Cell 13, 817-829 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 817-829
    • Grissom, P.1    Vaisberg, E.2    McIntosh, J.3
  • 33
    • 0035912738 scopus 로고    scopus 로고
    • All kinesin superfamily protein, KIF, genes in mouse and human
    • Miki, H., Setou, M., Kaneshiro, K. & Hirokawa, N. All kinesin superfamily protein, KIF, genes in mouse and human. Proc. Natl Acad. Sci. USA 98, 7004-7011 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7004-7011
    • Miki, H.1    Setou, M.2    Kaneshiro, K.3    Hirokawa, N.4
  • 34
    • 0029449733 scopus 로고
    • Motor proteins 1: Kinesins
    • Bloom, G. & Endow, S. Motor proteins 1: kinesins. Protein Profile 2, 1105-1171 (1995).
    • (1995) Protein Profile , vol.2 , pp. 1105-1171
    • Bloom, G.1    Endow, S.2
  • 35
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee, R. & Sheetz, M. Targeting of motor proteins. Science 271, 1539-1544 (1996).
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.1    Sheetz, M.2
  • 36
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526 (1998).
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 37
    • 0028104096 scopus 로고
    • Association of kinesin with the Golgi apparatus in rat hepatocytes
    • Marks, D., Larkin, J. & McNiven, M. Association of kinesin with the Golgi apparatus in rat hepatocytes. J. Cell. Sci. 107, 2417-2426 (1994).
    • (1994) J. Cell. Sci , vol.107 , pp. 2417-2426
    • Marks, D.1    Larkin, J.2    McNiven, M.3
  • 38
    • 0029918625 scopus 로고    scopus 로고
    • Kinesin localizes to the trans-Golgi network regardless of microtubule organization
    • Johnson, K., Hall, E. & Boekelheide, K. Kinesin localizes to the trans-Golgi network regardless of microtubule organization. Eur. J. Cell Biol. 69, 276-287 (1996).
    • (1996) Eur. J. Cell Biol , vol.69 , pp. 276-287
    • Johnson, K.1    Hall, E.2    Boekelheide, K.3
  • 39
    • 0034045587 scopus 로고    scopus 로고
    • An isoform of kinesin light chain specific for the Golgi complex
    • Gyoeva, F., Bybikova, E. & Minin, A. An isoform of kinesin light chain specific for the Golgi complex. J. Cell Sci. 113, 2047-2054 (2000).
    • (2000) J. Cell Sci , vol.113 , pp. 2047-2054
    • Gyoeva, F.1    Bybikova, E.2    Minin, A.3
  • 40
    • 0028019867 scopus 로고
    • Kinesin-mediated organelle translocation revealed by specific cellular manipulations
    • Feiguin, F., Ferreira, A., Kosik, K. S. & Caceres, A. Kinesin-mediated organelle translocation revealed by specific cellular manipulations. J. Cell Biol. 127, 1021-1039 (1994).
    • (1994) J. Cell Biol , vol.127 , pp. 1021-1039
    • Feiguin, F.1    Ferreira, A.2    Kosik, K.S.3    Caceres, A.4
  • 41
    • 0033224214 scopus 로고    scopus 로고
    • Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum
    • Girod, A. et al. Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum. Nature Cell Biol. 1, 423-430 (1999).
    • (1999) Nature Cell Biol , vol.1 , pp. 423-430
    • Girod, A.1
  • 42
    • 0033571602 scopus 로고    scopus 로고
    • Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells
    • White, J. et al. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147, 743-759 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 743-759
    • White, J.1
  • 43
    • 0032493768 scopus 로고    scopus 로고
    • Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum
    • Dorner, C. et al. Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. J. Biol. Chem. 273, 20267-20275 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 20267-20275
    • Dorner, C.1
  • 44
    • 0036140710 scopus 로고    scopus 로고
    • Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport
    • Nakajima, K. et al. Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport. Mol. Cell. Biol. 22, 866-873 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 866-873
    • Nakajima, K.1
  • 45
    • 0032517780 scopus 로고    scopus 로고
    • Role of xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus
    • Le Bot, N., Antony, C., White, J., Karsenti, E. & Vernos, I. Role of xklp3, a subunit of the Xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus. J. Cell Biol. 143, 1559-1573 (1998).
    • (1998) J. Cell Biol , vol.143 , pp. 1559-1573
    • Le Bot, N.1    Antony, C.2    White, J.3    Karsenti, E.4    Vernos, I.5
  • 46
    • 0031951034 scopus 로고    scopus 로고
    • Characterization of the KIF3C neural kinesin-like motor from mouse
    • Yang, Z. & Goldstein, L. S. B. Characterization of the KIF3C neural kinesin-like motor from mouse. Mol. Biol. Cell 9, 249-261 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 249-261
    • Yang, Z.1    Goldstein, L.S.B.2
  • 47
    • 0035203528 scopus 로고    scopus 로고
    • The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment
    • Marra, P. et al. The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment. Nature Cell Biol. 3, 1101-1113 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 1101-1113
    • Marra, P.1
  • 48
    • 0034071185 scopus 로고    scopus 로고
    • Brefeldin A-dependent membrane tubule formation reconstituted in vitro is driven by a cell cycle-regulated microtubule motor
    • Robertson, A. & Allan, V. Brefeldin A-dependent membrane tubule formation reconstituted in vitro is driven by a cell cycle-regulated microtubule motor. Mol. Biol. Cell 11, 941-955 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 941-955
    • Robertson, A.1    Allan, V.2
  • 49
    • 0031056545 scopus 로고    scopus 로고
    • GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum
    • Martinez, O. et al. GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 94, 1828-1833 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1828-1833
    • Martinez, O.1
  • 50
    • 0032559265 scopus 로고    scopus 로고
    • Interaction of a Golgi-associated kinesin-like protein with Rab6
    • Echard, A. et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science 279, 580-585 (1998).
    • (1998) Science , vol.279 , pp. 580-585
    • Echard, A.1
  • 51
    • 0033841775 scopus 로고    scopus 로고
    • The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus
    • Opdam, F. et al. The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus. J. Cell. Sci. 113, 2725-2735 (2000).
    • (2000) J. Cell. Sci , vol.113 , pp. 2725-2735
    • Opdam, F.1
  • 52
    • 0034331310 scopus 로고    scopus 로고
    • The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis
    • Hill, E., Clarke, M. & Barr, F. The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis. EMBO J. 19, 5711-5719 (2000).
    • (2000) EMBO J , vol.19 , pp. 5711-5719
    • Hill, E.1    Clarke, M.2    Barr, F.3
  • 53
    • 0035079968 scopus 로고    scopus 로고
    • The human kinesin-like protein RB6K is under tight cell cycle control and is essential for cytokinesis
    • Fontijn, R. et al. The human kinesin-like protein RB6K is under tight cell cycle control and is essential for cytokinesis. Mol. Cell. Biol. 21, 2944-2955 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2944-2955
    • Fontijn, R.1
  • 54
    • 0032578031 scopus 로고    scopus 로고
    • Microtubule-based membrane movement
    • Lane, J. & Allan, V. Microtubule-based membrane movement. Biochim. Biophys. Acta 1376, 27-55 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 27-55
    • Lane, J.1    Allan, V.2
  • 55
    • 0036468983 scopus 로고    scopus 로고
    • Principles of cargo attachment to cytoplasmic motor proteins
    • Kamal, A. & Goldstein, L. Principles of cargo attachment to cytoplasmic motor proteins. Curr. Opin. Cell Biol. 14, 63-68 (2002).
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 63-68
    • Kamal, A.1    Goldstein, L.2
  • 56
    • 0035575592 scopus 로고    scopus 로고
    • Protein trafficking in the exocytic pathway of polarized epithelial cells
    • Nelson, W. & Yeaman, C. Protein trafficking in the exocytic pathway of polarized epithelial cells. Trends Cell Biol. 11, 483-486 (2001).
    • (2001) Trends Cell Biol , vol.11 , pp. 483-486
    • Nelson, W.1    Yeaman, C.2
  • 57
    • 0032954307 scopus 로고    scopus 로고
    • Contributions of molecular motor enzymes to vesicle-based protein transport in gastrointestinal epithelial cells
    • McNiven, M. A. & Marlowe, K. J. Contributions of molecular motor enzymes to vesicle-based protein transport in gastrointestinal epithelial cells. Gastroenterology 116, 438-451 (1999).
    • (1999) Gastroenterology , vol.116 , pp. 438-451
    • McNiven, M.A.1    Marlowe, K.J.2
  • 58
    • 0001549038 scopus 로고    scopus 로고
    • The role of microtubule-based motors in the exocytic transport of polarized cells
    • Lafont, F. & Simons, K. The role of microtubule-based motors in the exocytic transport of polarized cells. Semin. Cell Dev. Biol. 7, 343-355 (1996).
    • (1996) Semin. Cell Dev. Biol , vol.7 , pp. 343-355
    • Lafont, F.1    Simons, K.2
  • 59
    • 0035494465 scopus 로고    scopus 로고
    • KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated triton-insoluble membranes
    • Noda, Y. et al. KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated triton-insoluble membranes. J. Cell Biol. 155, 77-88 (2001).
    • (2001) J. Cell Biol , vol.155 , pp. 77-88
    • Noda, Y.1
  • 60
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller, P., Toomre, D., Diaz, E., White, J. & Simons, K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nature Cell Biol. 3, 140-149 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 61
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol(4, 5)bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein, D., Tomishige, M., Stuurman, N. & Vale, R. Role of phosphatidylinositol(4, 5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109, 347-358 (2002).
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.1    Tomishige, M.2    Stuurman, N.3    Vale, R.4
  • 62
    • 0031779777 scopus 로고    scopus 로고
    • Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex
    • Valderrama, F. et al. Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex. Eur. J. Cell Biol. 76, 9-17 (1998).
    • (1998) Eur. J. Cell Biol , vol.76 , pp. 9-17
    • Valderrama, F.1
  • 63
    • 0032773274 scopus 로고    scopus 로고
    • Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements
    • di Campli, A. & et al. Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements. Cell Motil. Cytoskeleton 43, 334-348 (1999).
    • (1999) Cell Motil. Cytoskeleton , vol.43 , pp. 334-348
    • Di Campli, A.1
  • 64
    • 0031975510 scopus 로고    scopus 로고
    • Speculating about spectrin: New insights into the Golgi-associated cytoskeleton
    • Holleran, E. A. & Holzbaur, E. L. F. Speculating about spectrin: new insights into the Golgi-associated cytoskeleton. Trends Cell Biol. 8, 26-29 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 26-29
    • Holleran, E.A.1    Holzbaur, E.L.F.2
  • 65
    • 0030780090 scopus 로고    scopus 로고
    • Molecular motors and a spectrin matrix associate with Golgi membranes in vitro
    • Fath, K. R., Trimbur, G. M. & Burgess, D. R. Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J. Cell Biol. 139, 1169-1181 (1997).
    • (1997) J. Cell Biol , vol.139 , pp. 1169-1181
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 66
    • 0032516854 scopus 로고    scopus 로고
    • Vesicle budding on Golgi membranes: Regulation by G proteins and myosin motors
    • Stow, J. L. & Heimann, K. Vesicle budding on Golgi membranes: regulation by G proteins and myosin motors. Biochim. Biophys. Acta 1404, 161-171 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 161-171
    • Stow, J.L.1    Heimann, K.2
  • 67
    • 0033569627 scopus 로고    scopus 로고
    • Vesicle transport: The role of actin filaments and myosin motors
    • DePina, A. S. & Langford, G. M. Vesicle transport: The role of actin filaments and myosin motors. Microsc. Res. Tech. 47, 93-106 (1999).
    • (1999) Microsc. Res. Tech , vol.47 , pp. 93-106
    • DePina, A.S.1    Langford, G.M.2
  • 69
    • 0024078086 scopus 로고
    • Organization of the actin filament cytoskeleton in the intestinal brush border: A quantitative and qualitative immunoelectron microscope study
    • Drenckhahn, D. & Dermietzel, R. Organization of the actin filament cytoskeleton in the intestinal brush border: a quantitative and qualitative immunoelectron microscope study. J. Cell Biol. 107, 1037-1048 (1988).
    • (1988) J. Cell Biol , vol.107 , pp. 1037-1048
    • Drenckhahn, D.1    Dermietzel, R.2
  • 70
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath, K. R. & Burgess, D. R. Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. J. Cell Biol. 120, 117-127 (1993).
    • (1993) J. Cell Biol , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 71
    • 0028026746 scopus 로고
    • Molecular motors we are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath, K. R., Trimbur, G. M. & Burgess, D. R. Molecular motors we are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126, 661-675 (1994).
    • (1994) J. Cell Biol , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 72
    • 0030823761 scopus 로고    scopus 로고
    • Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers
    • Montes de Oca, G., Lezama, R. A., Mondragon, R., Castillo, A. M. & Meza, I. Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers. Arch. Med Res. 28, 321-328 (1997).
    • (1997) Arch. Med Res , vol.28 , pp. 321-328
    • Montes de Oca, G.1    Lezama, R.A.2    Mondragon, R.3    Castillo, A.M.4    Meza, I.5
  • 73
    • 0033570102 scopus 로고    scopus 로고
    • Overlapping distribution of the 130- and 110-kDa myosin I isoforms, on rat liver membranes
    • Balish, M. F., Moeller, E. F. & Coluccio, L. M. Overlapping distribution of the 130- and 110-kDa myosin I isoforms, on rat liver membranes. Arch. Biochem. Biophys. 370, 285-293 (1999).
    • (1999) Arch. Biochem. Biophys , vol.370 , pp. 285-293
    • Balish, M.F.1    Moeller, E.F.2    Coluccio, L.M.3
  • 74
    • 0010977335 scopus 로고
    • Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes
    • Narula, N. et al. Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes. J. Cell Biol. 114, 1113-1124 (1992).
    • (1992) J. Cell Biol , vol.114 , pp. 1113-1124
    • Narula, N.1
  • 75
    • 0028920639 scopus 로고
    • Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes
    • Narula, N. & Stow, J. L. Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes. Proc. Natl Acad. Sci. USA 92, 2874-2878 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2874-2878
    • Narula, N.1    Stow, J.L.2
  • 76
    • 0029894049 scopus 로고    scopus 로고
    • Analysis of the role of p200 containing vesicles in post-Golgi traffic
    • Ikonen, E., Parton, R. G., Lafont, F. & Simons, K. Analysis of the role of p200 containing vesicles in post-Golgi traffic. Mol. Biol. Cell 7, 961-974 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 961-974
    • Ikonen, E.1    Parton, R.G.2    Lafont, F.3    Simons, K.4
  • 77
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes: Identification of p200 a nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen, E. et al. Myosin II is associated with Golgi membranes: identification of p200 a nonmuscle myosin II on Golgi-derived vesicles. J. Cell Sci. 110, 2155-2164 (1997).
    • (1997) J. Cell Sci , vol.110 , pp. 2155-2164
    • Ikonen, E.1
  • 78
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Müsch, A., Cohen, D. & Rodriguez-Boulan, E. Myosin II is involved in the production of constitutive transport vesicles from the TGN. J. Cell. Biol. 138, 291-306 (1997).
    • (1997) J. Cell. Biol , vol.138 , pp. 291-306
    • Müsch, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 79
    • 0031890696 scopus 로고    scopus 로고
    • Budding roles for myosin II on the Golgi
    • Stow, J. L., Fath, K. R. & Burgess, D. R. Budding roles for myosin II on the Golgi. Trends Cell Biol. 8, 138-141 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 138-141
    • Stow, J.L.1    Fath, K.R.2    Burgess, D.R.3
  • 81
    • 0027420994 scopus 로고
    • Brain myosin-V is a two-headed unconventional myosin with motor activity
    • Cheney, R. E. et al. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13-23 (1993).
    • (1993) Cell , vol.75 , pp. 13-23
    • Cheney, R.E.1
  • 83
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G. C., Prendergast, J. A. & Singer, R. A. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113, 539-551 (1991).
    • (1991) J. Cell Biol , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 84
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan, B., Bowser, R. & Novick, R. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128, 1055-1068 (1995).
    • (1995) J. Cell Biol , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, R.3
  • 85
    • 0032915418 scopus 로고    scopus 로고
    • The tail of a yeast class V myosin, Myo2p, functions as a localization domain
    • Reck-Peterson, S. L., Novick P. J. & Mooseker, M. S. The tail of a yeast class V myosin, Myo2p, functions as a localization domain. Mol. Biol. Cell 10, 1001-1017 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1001-1017
    • Reck-Peterson, S.L.1    Novick, P.J.2    Mooseker, M.S.3
  • 86
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • Fukuda, M., Kuroda, T. S. & Mikoshiba, K. Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J. Biol. Chem. 277, 12432-12436 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 87
    • 0036226156 scopus 로고    scopus 로고
    • Identification of an organelle receptor for myosin-Va
    • Wu, X. S. et al. Identification of an organelle receptor for myosin-Va. Nature Cell Biol. 4, 271-278 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 271-278
    • Wu, X.S.1
  • 88
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- and actin-based transport motors
    • Huang, J. D. et al. Direct interaction of microtubule- and actin-based transport motors. Nature 397, 267-270 (1999).
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, J.D.1
  • 89
    • 0033619258 scopus 로고    scopus 로고
    • Myosin VI is an actin-based motor that moves backwards
    • Wells, A. L. et al. Myosin VI is an actin-based motor that moves backwards. Nature 401, 505-508 (1999).
    • (1999) Nature , vol.401 , pp. 505-508
    • Wells, A.L.1
  • 90
    • 0034683666 scopus 로고    scopus 로고
    • Myosin VI: Roles for a minus end-directed actin motor in cells
    • Cramer, L. P. Myosin VI: roles for a minus end-directed actin motor in cells. J. Cell Biol. 150, F121-F126 (2000).
    • (2000) J. Cell Biol , vol.150 , pp. F121-F126
    • Cramer, L.P.1
  • 91
    • 0032517817 scopus 로고    scopus 로고
    • The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation
    • Buss, F. et al. The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J. Cell Biol. 143, 1535-1545 (1998).
    • (1998) J. Cell Biol , vol.143 , pp. 1535-1545
    • Buss, F.1
  • 92
    • 0035898659 scopus 로고    scopus 로고
    • Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis
    • Buss, F., Arden, S. D., Lindsay, M, Luzio, J. P. & Kendrick-Jones, J. Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis. EMBO J. 20, 3676-3684 (2001).
    • (2001) EMBO J , vol.20 , pp. 3676-3684
    • Buss, F.1    Arden, S.D.2    Lindsay, M.3    Luzio, J.P.4    Kendrick-Jones, J.5
  • 93
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • Marks, B. et al. GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 410, 231-235 (2001).
    • (2001) Nature , vol.410 , pp. 231-235
    • Marks, B.1
  • 94
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer, S. M. & Hinshaw, J. E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93, 1021-1029 (1998).
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 95
    • 0032563156 scopus 로고    scopus 로고
    • Dynamin: A molecular motor with pinchase action
    • McNiven, M. A. Dynamin: A molecular motor with pinchase action. Cell 94, 151-154 (1998).
    • (1998) Cell , vol.94 , pp. 151-154
    • McNiven, M.A.1
  • 96
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: Pinching in new places
    • McNiven, M. A., Cao, H., Pitts, K. R. & Yoon, Y. The dynamin family of mechanoenzymes: pinching in new places. Trends Biochem. Sci. 25, 115-120 (2000).
    • (2000) Trends Biochem. Sci , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 97
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J. R. & McNiven, M. A. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133, 761-775 (1996).
    • (1996) J. Cell Biol , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 98
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S. M., Howell, K. E., Henley, J. R., Cao, H. & McNiven, M. A. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 279, 573-577 (1998).
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 99
  • 100
    • 0034094514 scopus 로고    scopus 로고
    • Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin
    • Cao, H., Thompson, H. M., Krueger, E. W. & McNiven, M. A. Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin. J. Cell Sci. 113, 1993-2002 (2000).
    • (2000) J. Cell Sci , vol.113 , pp. 1993-2002
    • Cao, H.1    Thompson, H.M.2    Krueger, E.W.3    McNiven, M.A.4


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