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Volumn 2, Issue C, 1995, Pages 239-273

Function of microtubules in protein secretion and organization of the Golgi complex

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Indexed keywords


EID: 77957055794     PISSN: 18746020     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6020(06)80021-2     Document Type: Review
Times cited : (5)

References (174)
  • 1
    • 0024370276 scopus 로고
    • Role of microtubules in polarized delivery of apical membrane proteins to the brush border of the intestinal epithelium
    • Achler, C., Filmer, D., Merte, C., Drenckhahn, D., Role of microtubules in polarized delivery of apical membrane proteins to the brush border of the intestinal epithelium. J. Cell Biol. 109 (1989), 179–189.
    • (1989) J. Cell Biol. , vol.109 , pp. 179-189
    • Achler, C.1    Filmer, D.2    Merte, C.3    Drenckhahn, D.4
  • 2
    • 0024463358 scopus 로고
    • Membrane-bound myosin-I provides new mechanisms in cell motility
    • Adams, R.J., Pollard, T.D., Membrane-bound myosin-I provides new mechanisms in cell motility. Cell Motil. Cytoskel. 14 (1989), 178–182.
    • (1989) Cell Motil. Cytoskel. , vol.14 , pp. 178-182
    • Adams, R.J.1    Pollard, T.D.2
  • 3
    • 0023019044 scopus 로고
    • A microtubule-binding protein associated with membranes of the Golgi apparatus
    • Allan, V.J., Kreis, T.E., A microtubule-binding protein associated with membranes of the Golgi apparatus. J. Cell Biol. 103 (1986), 2229–2239.
    • (1986) J. Cell Biol. , vol.103 , pp. 2229-2239
    • Allan, V.J.1    Kreis, T.E.2
  • 4
    • 0021673303 scopus 로고
    • Direct visualization of protein transport and processing in the living cell by microinjection of specific antibodies
    • Arnheiter, H., Dubois-Dalcq, M., Lazzarini, R.A., Direct visualization of protein transport and processing in the living cell by microinjection of specific antibodies. Cell 39 (1984), 99–109.
    • (1984) Cell , vol.39 , pp. 99-109
    • Arnheiter, H.1    Dubois-Dalcq, M.2    Lazzarini, R.A.3
  • 5
    • 0027755212 scopus 로고
    • Stacking of Golgi cisternae in Schizosaccharomyces pombe requires intact microtubules
    • Ayscough, K., Hajibagheri, N.M.A., Watson, R., Warren, G., Stacking of Golgi cisternae in Schizosaccharomyces pombe requires intact microtubules. J. Cell Sci. 106 (1993), 1227–1237.
    • (1993) J. Cell Sci. , vol.106 , pp. 1227-1237
    • Ayscough, K.1    Hajibagheri, N.M.A.2    Watson, R.3    Warren, G.4
  • 6
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao, R., Antony, C., Dotti, C., Karsenti, E., Stelzer, E.H.K., Simons, K., The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109 (1989), 2817–2832.
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.K.5    Simons, K.6
  • 7
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein (VSV-G) is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., McCaffery, M., Plutner, H., Farquhar, M.G., Vesicular stomatitis virus glycoprotein (VSV-G) is sorted and concentrated during export from the endoplasmic reticulum. Cell 76 (1994), 841–852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, M.2    Plutner, H.3    Farquhar, M.G.4
  • 8
    • 0024002767 scopus 로고
    • Plasma membrane protein sorting in epithelial cells: do secretory pathways hold the key?
    • Bartles, J.R., Hubbard, A.L., Plasma membrane protein sorting in epithelial cells: do secretory pathways hold the key?. Trends Biochem. Sci. 13 (1988), 181–184.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 181-184
    • Bartles, J.R.1    Hubbard, A.L.2
  • 9
    • 0020725023 scopus 로고
    • Membrane insertion at the leading edge of motile fibroblasts
    • Bergmann, J.E., Kupfer, A., Singer, S.J., Membrane insertion at the leading edge of motile fibroblasts. Proc. Natl. Acad. Sci. USA, 80, 1983, 1367–1371.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1367-1371
    • Bergmann, J.E.1    Kupfer, A.2    Singer, S.J.3
  • 10
    • 0024462447 scopus 로고
    • A novel 58-kDa protein associates with the Golgi apparatus and microtubules
    • Bloom, G.S., Brashear, T.A., A novel 58-kDa protein associates with the Golgi apparatus and microtubules. J. Biol. Chem. 264 (1989), 16083–16092.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16083-16092
    • Bloom, G.S.1    Brashear, T.A.2
  • 11
    • 0026014467 scopus 로고
    • Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells
    • Boll, W., Partin, J.S., Katz, A.I., Caplan, M.J., Jamieson, J.D., Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells. Proc. Natl. Acad. Sci. USA, 88, 1991, 8592–8596.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8592-8596
    • Boll, W.1    Partin, J.S.2    Katz, A.I.3    Caplan, M.J.4    Jamieson, J.D.5
  • 12
    • 0025029828 scopus 로고
    • Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel, M., Parton, R., Kuznetsov, S.A., Schroer, T.A., Gruenberg, J., Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62 (1990), 719–731.
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 13
    • 0027769136 scopus 로고
    • The intermediate compartment between endoplasmic reticulum and Golgi complex in mammalian cells
    • Bonatti, S., Torrisi, M.R., The intermediate compartment between endoplasmic reticulum and Golgi complex in mammalian cells. Subcell. Biochem. 21 (1993), 121–142.
    • (1993) Subcell. Biochem. , vol.21 , pp. 121-142
    • Bonatti, S.1    Torrisi, M.R.2
  • 14
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum
    • Bonatti, S., Migliaggio, G., Simons, K., Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum. J. Biol. Chem. 264 (1989), 12590–12595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaggio, G.2    Simons, K.3
  • 15
    • 0025605057 scopus 로고
    • Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells
    • Breitfeld, P.P., McKinnon, W.C., Mostov, K.E., Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells. J. Cell Biol. 111 (1990), 2365–2373.
    • (1990) J. Cell Biol. , vol.111 , pp. 2365-2373
    • Breitfeld, P.P.1    McKinnon, W.C.2    Mostov, K.E.3
  • 16
    • 0026181461 scopus 로고
    • Stabilization and post-translational modification of microtubules during cellular morphogenesis
    • Bulinski, J.C., Gundersen, G.G., Stabilization and post-translational modification of microtubules during cellular morphogenesis. BioEssays 13 (1991), 285–293.
    • (1991) BioEssays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 17
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T.L., Kelly, R.B., Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 3 (1987), 243–293.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 18
    • 0026337490 scopus 로고
    • Disruption of the Golgi apparatus with brefeldin A does not destabilize the associated detyrosinated microtubule network
    • Burgess, T.L., Skoufias, D.A., Wilson, L., Disruption of the Golgi apparatus with brefeldin A does not destabilize the associated detyrosinated microtubule network. Cell Motil. Cytoskel. 20 (1991), 289–300.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 289-300
    • Burgess, T.L.1    Skoufias, D.A.2    Wilson, L.3
  • 19
    • 0027457958 scopus 로고
    • Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro
    • Burkhardt, J.K., McIlvain, J.M. Jr., Sheetz, M.P., Argon, Y., Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro. J. Cell Sci. 104 (1993), 151–162.
    • (1993) J. Cell Sci. , vol.104 , pp. 151-162
    • Burkhardt, J.K.1    McIlvain, J.M.2    Sheetz, M.P.3    Argon, Y.4
  • 20
    • 0020441456 scopus 로고
    • Microtubules and protein secretion in rat lacrimal glands: Localization of short-term effects of colchicine on the secretory process
    • Busson-Mabillot, S., Chambaut-Guérin, A.-M., Ovtracht, L., Muller, P., Rossignol, B., Microtubules and protein secretion in rat lacrimal glands: Localization of short-term effects of colchicine on the secretory process. J. Cell Biol. 95 (1982), 105–117.
    • (1982) J. Cell Biol. , vol.95 , pp. 105-117
    • Busson-Mabillot, S.1    Chambaut-Guérin, A.-M.2    Ovtracht, L.3    Muller, P.4    Rossignol, B.5
  • 21
    • 0001947012 scopus 로고
    • Sorting of membrane and secretory proteins in polarized epithelial cells
    • Caplan, M., Matlin, K.S., Sorting of membrane and secretory proteins in polarized epithelial cells. Modern Cell Biol. 8 (1989), 71–127.
    • (1989) Modern Cell Biol. , vol.8 , pp. 71-127
    • Caplan, M.1    Matlin, K.S.2
  • 22
    • 0020085615 scopus 로고
    • Ultrastructure of human natural killer cells: Nature of the cytolytic contacts in relation to cellular secretion
    • Carpén, O., Virtanen, I., Saksela, E., Ultrastructure of human natural killer cells: Nature of the cytolytic contacts in relation to cellular secretion. J. Immunol. 128 (1982), 2691–2697.
    • (1982) J. Immunol. , vol.128 , pp. 2691-2697
    • Carpén, O.1    Virtanen, I.2    Saksela, E.3
  • 23
    • 0025939531 scopus 로고
    • Regulation of p34cdc2 protein kinase: New insights into protein phosphorylation and the cell cycle
    • Clarke, P.R., Karsenti, E., Regulation of p34cdc2 protein kinase: New insights into protein phosphorylation and the cell cycle. J. Cell Sci. 100 (1991), 409–414.
    • (1991) J. Cell Sci. , vol.100 , pp. 409-414
    • Clarke, P.R.1    Karsenti, E.2
  • 24
    • 0027055402 scopus 로고
    • Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures
    • Cluett, E.B., Brown, W.J., Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures. J. Cell Sci. 103 (1992), 773–784.
    • (1992) J. Cell Sci. , vol.103 , pp. 773-784
    • Cluett, E.B.1    Brown, W.J.2
  • 25
    • 0027455337 scopus 로고
    • Tubulation of Golgi membranes in vivo and in vitro in the absence of brefeldin A
    • Cluett, E.B., Wood, S.A., Banta, M., Brown, W.J., Tubulation of Golgi membranes in vivo and in vitro in the absence of brefeldin A. J. Cell Biol. 120 (1993), 15–24.
    • (1993) J. Cell Biol. , vol.120 , pp. 15-24
    • Cluett, E.B.1    Wood, S.A.2    Banta, M.3    Brown, W.J.4
  • 26
    • 0025571426 scopus 로고
    • Association between microtubules and Golgi vesicles isolated from rat parotid glands
    • Coffe, G., Raymond, M.-N., Association between microtubules and Golgi vesicles isolated from rat parotid glands. Biol. Cell 70 (1990), 143–152.
    • (1990) Biol. Cell , vol.70 , pp. 143-152
    • Coffe, G.1    Raymond, M.-N.2
  • 27
    • 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 (1990), 135–145.
    • (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
  • 28
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthésy-Theulaz, I., Pauloin, A., Pfeffer, S.R., Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol. 118 (1992), 1333–1345.
    • (1992) J. Cell Biol. , vol.118 , pp. 1333-1345
    • Corthésy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 29
    • 0024041810 scopus 로고
    • The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts
    • Dabora, S.L., Sheetz, M.P., The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell 54 (1988), 27–35.
    • (1988) Cell , vol.54 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 30
    • 0026034581 scopus 로고
    • The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus-2 is microtubule binding
    • Dahllöf, B., Wallin, M., Kvist, S., The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus-2 is microtubule binding. J. Biol. Chem. 266 (1991), 1804–1808.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1804-1808
    • Dahllöf, B.1    Wallin, M.2    Kvist, S.3
  • 31
    • 0025865353 scopus 로고
    • Disruption of microtubules alters the polarity of basement membrane proteoglycan secretion in epithelial cells
    • De Almeida, J.B., Stow, J.L., Disruption of microtubules alters the polarity of basement membrane proteoglycan secretion in epithelial cells. Am. J. Physiol. 260 (1991), C691–C700.
    • (1991) Am. J. Physiol. , vol.260 , pp. C691-C700
    • De Almeida, J.B.1    Stow, J.L.2
  • 32
    • 0017276478 scopus 로고
    • The effects of methyl[5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl]carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubules, on mammalian cells cultured in vitro
    • De Brabander, M.J., Van de Veire, R.M.L., Aerts, F.E.M., Borgers, M., Janssen, P.A.J., The effects of methyl[5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl]carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubules, on mammalian cells cultured in vitro. Cancer Res. 36 (1976), 905–916.
    • (1976) Cancer Res. , vol.36 , pp. 905-916
    • De Brabander, M.J.1    Van de Veire, R.M.L.2    Aerts, F.E.M.3    Borgers, M.4    Janssen, P.A.J.5
  • 33
    • 0019786282 scopus 로고
    • Microtubule assembly in living cells after release from nocodazole block: The effects of metabolic inhibitors, taxol and pH
    • De Brabander, M., Geuens, G., Nuydens, R., Willebrords, R., De Mey, J., Microtubule assembly in living cells after release from nocodazole block: The effects of metabolic inhibitors, taxol and pH. Cell Biol. Int. Rep. 5 (1981), 913–920.
    • (1981) Cell Biol. Int. Rep. , vol.5 , pp. 913-920
    • De Brabander, M.1    Geuens, G.2    Nuydens, R.3    Willebrords, R.4    De Mey, J.5
  • 34
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson, J.G., Lippincott-Schwartz, J., Bloom, G.S., Kreis, T.E., Klausner, R.D., Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J. Cell Biol. 111 (1990), 2295–2306.
    • (1990) J. Cell Biol. , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 35
    • 0025126915 scopus 로고
    • What's new in cytoskeleton-organelle interactions? Relationship between microtubules and the Golgi apparatus
    • Duden, R., Ho, W.C., Allan, V.J., Kreis, T.E., What's new in cytoskeleton-organelle interactions? Relationship between microtubules and the Golgi apparatus. Pathol. Res. Pract. 186 (1990), 535–541.
    • (1990) Pathol. Res. Pract. , vol.186 , pp. 535-541
    • Duden, R.1    Ho, W.C.2    Allan, V.J.3    Kreis, T.E.4
  • 36
    • 0025817710 scopus 로고
    • Involvement of β-COP in membrane traffic through the Golgi complex
    • Duden, R., Allan, V., Kreis, T.E., Involvement of β-COP in membrane traffic through the Golgi complex. Trends Cell Biol. 1 (1991), 14–19.
    • (1991) Trends Cell Biol. , vol.1 , pp. 14-19
    • Duden, R.1    Allan, V.2    Kreis, T.E.3
  • 37
    • 0026034357 scopus 로고
    • β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin
    • Duden, R., Griffiths, G., Frank, R., Argos, P., Kreis, T.E., β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin. Cell 64 (1991), 649–665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 38
    • 0004028961 scopus 로고
    • Microtubules
    • 2nd ed. Springer Verlag New York
    • Dustin, P., Microtubules., 2nd ed., 1984, Springer Verlag, New York, 1–482.
    • (1984) , pp. 1-482
    • Dustin, P.1
  • 39
    • 0024509437 scopus 로고
    • Nocodazole, a microtubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2)
    • Eilers, U., Klumperman, J., Hauri, H.-P., Nocodazole, a microtubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2). J. Cell Biol. 108 (1989), 13–22.
    • (1989) J. Cell Biol. , vol.108 , pp. 13-22
    • Eilers, U.1    Klumperman, J.2    Hauri, H.-P.3
  • 41
    • 0026724955 scopus 로고
    • Centrosomes, microtubules, and microfilaments in the reendothelialization and remodeling of double-sided in vitro wounds
    • Ettenson, D.S., Gotlieb, A.I., Centrosomes, microtubules, and microfilaments in the reendothelialization and remodeling of double-sided in vitro wounds. Lab. Invest. 66 (1992), 722–733.
    • (1992) Lab. Invest. , vol.66 , pp. 722-733
    • Ettenson, D.S.1    Gotlieb, A.I.2
  • 42
    • 9244220411 scopus 로고
    • Protein traffic through the Golgi complex
    • Steer C.J. Hanover J.S. Cambridge University Press Berlin
    • Farquhar, M.G., Protein traffic through the Golgi complex. Steer, C.J., Hanover, J.S., (eds.) Intracellular Trafficking of Proteins, 1991, Cambridge University Press, Berlin, 431–471.
    • (1991) Intracellular Trafficking of Proteins , pp. 431-471
    • Farquhar, M.G.1
  • 43
    • 0019769965 scopus 로고
    • The Golgi apparatus (complex)—(1954–1981)—from artifact to center stage
    • Farquhar, M.G., Palade, G.E., The Golgi apparatus (complex)—(1954-1981)—from artifact to center stage. J. Cell Biol. 91 (1981), 77s–103s.
    • (1981) J. Cell Biol. , vol.91 , pp. 77s-103s
    • Farquhar, M.G.1    Palade, G.E.2
  • 44
    • 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 (1993), 117–127.
    • (1993) J. Cell Biol. , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 45
    • 0020365635 scopus 로고
    • Spatial relationships of microtubule-organizing centers and the contact area in cytotoxic T lymphocytes and target cells
    • Geiger, B., Rosen, D., Berke, G., Spatial relationships of microtubule-organizing centers and the contact area in cytotoxic T lymphocytes and target cells. J. Cell Biol. 95 (1982), 137–143.
    • (1982) J. Cell Biol. , vol.95 , pp. 137-143
    • Geiger, B.1    Rosen, D.2    Berke, G.3
  • 46
    • 0025887459 scopus 로고
    • Microtubule dynamics: mechanism, regulation, and function
    • Gelfand, V.I., Bershadsky, A.D., Microtubule dynamics: mechanism, regulation, and function. Annu. Rev. Cell Biol. 7 (1991), 93–116.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 93-116
    • Gelfand, V.I.1    Bershadsky, A.D.2
  • 48
    • 0025905152 scopus 로고
    • Microtubular organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells
    • Gilbert, T., Le Bivic, A., Quaroni, A., Rodriguez-Boulan, E., Microtubular organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells. J. Cell Biol. 113 (1991), 275–288.
    • (1991) J. Cell Biol. , vol.113 , pp. 275-288
    • Gilbert, T.1    Le Bivic, A.2    Quaroni, A.3    Rodriguez-Boulan, E.4
  • 49
    • 0026475176 scopus 로고
    • Okadaic acid induces interphase to mitotic-like microtubule dynamic instability by inactivating rescue
    • Gliksman, N.R., Parsons, S.F., Salmon, E.D., Okadaic acid induces interphase to mitotic-like microtubule dynamic instability by inactivating rescue. J. Cell Biol. 119 (1992), 1271–1276.
    • (1992) J. Cell Biol. , vol.119 , pp. 1271-1276
    • Gliksman, N.R.1    Parsons, S.F.2    Salmon, E.D.3
  • 50
    • 0019791275 scopus 로고
    • Distribution of microtubule organizing centers in migrating sheets of endothelial cells
    • Gotlieb, A.I., McBurnie-May, L., Subrahmanyan, L., Kalnins, V.I., Distribution of microtubule organizing centers in migrating sheets of endothelial cells. J. Cell Biol. 91 (1981), 589–594.
    • (1981) J. Cell Biol. , vol.91 , pp. 589-594
    • Gotlieb, A.I.1    McBurnie-May, L.2    Subrahmanyan, L.3    Kalnins, V.I.4
  • 51
    • 0002405182 scopus 로고
    • Post-translational modifications of tubulin
    • Warner F.D. Satir P. Gibbons I.R. Alan R. Liss Cambridge
    • Greer, K., Rosenbaum, J.L., Post-translational modifications of tubulin. Warner, F.D., Satir, P., Gibbons, I.R., (eds.) Cell Movement, Vol. 2, Kinesin, Dynein, and Microtubule Dynamics, 1989, Alan R. Liss, Cambridge, 47–66.
    • (1989) Cell Movement , pp. 47-66
    • Greer, K.1    Rosenbaum, J.L.2
  • 52
    • 0022975133 scopus 로고
    • The trans-Golgi network: Sorting at the exit site of the Golgi complex
    • Griffiths, G., Simons, K., The trans-Golgi network: Sorting at the exit site of the Golgi complex. Science 234 (1986), 438–443.
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 53
    • 0027515613 scopus 로고
    • Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells
    • Gurland, G., Gundersen, G.G., Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells. Proc. Natl. Acad. Sci. USA, 90, 1993, 8827–8831.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8827-8831
    • Gurland, G.1    Gundersen, G.G.2
  • 54
    • 0026908206 scopus 로고
    • The endoplasmic reticulum-Golgi intermediate compartment
    • Hauri, H.-P., Schweizer, A., The endoplasmic reticulum-Golgi intermediate compartment. Curr. Opin. Cell Biol. 4 (1992), 600–608.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 600-608
    • Hauri, H.-P.1    Schweizer, A.2
  • 55
    • 0021364598 scopus 로고
    • Time-lapse video intensification analyses of cytoplasmic organelle movements during endosome translocation
    • Herman, B., Albertini, D.F., Time-lapse video intensification analyses of cytoplasmic organelle movements during endosome translocation. J. Cell Biol. 98 (1984), 565–576.
    • (1984) J. Cell Biol. , vol.98 , pp. 565-576
    • Herman, B.1    Albertini, D.F.2
  • 56
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser, J., Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell Biol. 108 (1989), 855–864.
    • (1989) J. Cell Biol. , vol.108 , pp. 855-864
    • Heuser, J.1
  • 58
    • 0017227021 scopus 로고
    • Interaction of nocodazole (R 17934), a new anti-tumoral drug, with rat brain tubulin
    • Hoebeke, J., Van Nijen, G., De Brabander, M., Interaction of nocodazole (R 17934), a new anti-tumoral drug, with rat brain tubulin. Biochem. Biophys. Res. Commun. 69 (1976), 319–324.
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 319-324
    • Hoebeke, J.1    Van Nijen, G.2    De Brabander, M.3
  • 59
    • 0027287516 scopus 로고
    • Retrograde movement of membrane lipids from the Golgi apparatus to the endoplasmic reticulum of perforated cells: Evidence for lipid recycling
    • Hoffmann, P.M., Pagano, R.E., Retrograde movement of membrane lipids from the Golgi apparatus to the endoplasmic reticulum of perforated cells: Evidence for lipid recycling. Eur. J. Cell Biol. 60 (1993), 371–375.
    • (1993) Eur. J. Cell Biol. , vol.60 , pp. 371-375
    • Hoffmann, P.M.1    Pagano, R.E.2
  • 60
    • 0025045429 scopus 로고
    • Radial extension of macrophage tubular lysosomes supported by kinesin
    • Hollenbeck, P.J., Swanson, J.A., Radial extension of macrophage tubular lysosomes supported by kinesin. Nature 346 (1990), 864–866.
    • (1990) Nature , vol.346 , pp. 864-866
    • Hollenbeck, P.J.1    Swanson, J.A.2
  • 62
    • 0025775723 scopus 로고
    • A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules
    • Hsu, V.W., Yuan, L.C., Nuchtern, J.G., Lipppincott-Schwartz, J., Hammerling, G.J., Klausner, R.D., A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules. Nature 352 (1991), 441–444.
    • (1991) Nature , vol.352 , pp. 441-444
    • Hsu, V.W.1    Yuan, L.C.2    Nuchtern, J.G.3    Lipppincott-Schwartz, J.4    Hammerling, G.J.5    Klausner, R.D.6
  • 63
    • 0025168710 scopus 로고
    • Differential microtubule requirements for transcytosis in MDCK cells
    • Hunziker, W., Male, P., Mellman, I., Differential microtubule requirements for transcytosis in MDCK cells. EMBO J. 9 (1990), 3515–3525.
    • (1990) EMBO J. , vol.9 , pp. 3515-3525
    • Hunziker, W.1    Male, P.2    Mellman, I.3
  • 64
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T., Peterson, P.A., Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9 (1990), 3153–3162.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 65
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T., Peterson, P.A., Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121 (1993), 317–333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 66
    • 0027673952 scopus 로고
    • γ-Tubulin: The hub of cellular microtubule assemblies
    • Joshi, H.C., γ-Tubulin: The hub of cellular microtubule assemblies. Bioessays 15 (1993), 637–643.
    • (1993) Bioessays , vol.15 , pp. 637-643
    • Joshi, H.C.1
  • 67
    • 0027447972 scopus 로고
    • Molecular components of the centrosome
    • Kalt, A., Schliwa, M., Molecular components of the centrosome. Trends Cell Biol. 3 (1993), 118–128.
    • (1993) Trends Cell Biol. , vol.3 , pp. 118-128
    • Kalt, A.1    Schliwa, M.2
  • 68
    • 0026508429 scopus 로고
    • Interaction of membranes of the Golgi complex with microtubules in vitro
    • Karecla, P.I., Kreis, T.E., Interaction of membranes of the Golgi complex with microtubules in vitro. Eur. J. Cell Biol. 57 (1992), 139–146.
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 139-146
    • Karecla, P.I.1    Kreis, T.E.2
  • 69
    • 0001426487 scopus 로고
    • Centrosomes and the spatial distribution of microtubules in animal cells
    • Karsenti, E., Maro, B., Centrosomes and the spatial distribution of microtubules in animal cells. Trends Biochem. Sci. 11 (1986), 460–463.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 460-463
    • Karsenti, E.1    Maro, B.2
  • 70
    • 0025261707 scopus 로고
    • Microtubules, membrane traffic, and cell organization
    • Kelly, R.B., Microtubules, membrane traffic, and cell organization. Cell 61 (1990), 5–7.
    • (1990) Cell , vol.61 , pp. 5-7
    • Kelly, R.B.1
  • 71
    • 0022919318 scopus 로고
    • Beyond self-assembly: From microtubules to morphogenesis
    • Kirschner, M., Mitchison, T., Beyond self-assembly: From microtubules to morphogenesis. Cell 45 (1986), 329–342.
    • (1986) Cell , vol.45 , pp. 329-342
    • Kirschner, M.1    Mitchison, T.2
  • 72
    • 0024410381 scopus 로고
    • Sorting and traffic in the central vacuolar system
    • Klausner, R.D., Sorting and traffic in the central vacuolar system. Cell 57 (1989), 703–706.
    • (1989) Cell , vol.57 , pp. 703-706
    • Klausner, R.D.1
  • 73
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., Donaldson, J.G., Lippincott-Schwartz, J., Brefeldin A: Insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116 (1992), 1071–1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 75
    • 0025267442 scopus 로고
    • Role of microtubules in the organization of the Golgi apparatus
    • Kreis, T.E., Role of microtubules in the organization of the Golgi apparatus. Cell Motil. Cytoskel. 15 (1990), 67–70.
    • (1990) Cell Motil. Cytoskel. , vol.15 , pp. 67-70
    • Kreis, T.E.1
  • 76
    • 0024405097 scopus 로고
    • Secretory granules and endosomes show saltatory movement biased in anterograde and retrograde directions, respectively, along microtubules in AtT20 cells
    • Kreis, T., Matteoni, R., Hollinshead, M., Tooze, J., Secretory granules and endosomes show saltatory movement biased in anterograde and retrograde directions, respectively, along microtubules in AtT20 cells. Eur. J. Cell Biol. 49 (1989), 128–139.
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 128-139
    • Kreis, T.1    Matteoni, R.2    Hollinshead, M.3    Tooze, J.4
  • 77
    • 0024821099 scopus 로고
    • Low temperature-induced transport blocks as tools to manipulate membrane traffic
    • Kuismanen, E., Saraste, J., Low temperature-induced transport blocks as tools to manipulate membrane traffic. Methods Cell Biol. 32 (1989), 257–274.
    • (1989) Methods Cell Biol. , vol.32 , pp. 257-274
    • Kuismanen, E.1    Saraste, J.2
  • 78
    • 0344006229 scopus 로고
    • Polarization of the Golgi apparatus and the microtubule-organizing center within cloned natural killer cells bound to their targets
    • Kupfer, A., Dennert, G., Singer, S.J., Polarization of the Golgi apparatus and the microtubule-organizing center within cloned natural killer cells bound to their targets. Proc. Natl. Acad. Sci. USA, 80, 1983, 7224–7228.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7224-7228
    • Kupfer, A.1    Dennert, G.2    Singer, S.J.3
  • 79
    • 0020316410 scopus 로고
    • Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound
    • Kupfer, A., Louvard, D., Singer, S.J., Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound. Proc. Natl. Acad. Sci. USA, 79, 1982, 2603–2607.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2603-2607
    • Kupfer, A.1    Louvard, D.2    Singer, S.J.3
  • 80
    • 0030068935 scopus 로고    scopus 로고
    • Molecular cloning and expression of a 58 kDa cis-Golgi and intermediate compartment protein
    • (in press)
    • (in press)Lahtinen, V., Hellman, V., Wernstedt, C., Saraste, J., Pettersson, R., Molecular cloning and expression of a 58 kDa cis-Golgi and intermediate compartment protein. J. Biol. Chem., 1996.
    • (1996) J. Biol. Chem.
    • Lahtinen, V.1    Hellman, V.2    Wernstedt, C.3    Saraste, J.4    Pettersson, R.5
  • 81
    • 0023693945 scopus 로고
    • Dynamic behavior of endoplasmic reticulum in living cells
    • Lee, C., Chen, L.B., Dynamic behavior of endoplasmic reticulum in living cells. Cell 54 (1988), 37–46.
    • (1988) Cell , vol.54 , pp. 37-46
    • Lee, C.1    Chen, L.B.2
  • 82
    • 0027723952 scopus 로고
    • Motility and construction of the endoplasmic reticulum in living cells
    • Lee, C., Chen, L.B., Motility and construction of the endoplasmic reticulum in living cells. Subcell. Biochem. 21 (1993), 343–352.
    • (1993) Subcell. Biochem. , vol.21 , pp. 343-352
    • Lee, C.1    Chen, L.B.2
  • 83
    • 0027535384 scopus 로고
    • Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus
    • Lippincott-Schwartz, J., Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus. Trends Cell Biol. 3 (1993), 81–88.
    • (1993) Trends Cell Biol. , vol.3 , pp. 81-88
    • Lippincott-Schwartz, J.1
  • 84
    • 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., Donaldson, J.G., Schweizer, A., Berger, E.G., Hauri, H.-P., Yan, L.C., Klausner, R.D., Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60 (1990), 821–836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.-P.5    Yan, L.C.6    Klausner, R.D.7
  • 85
    • 0021802475 scopus 로고
    • A vital stain for the Golgi apparatus
    • Lipsky, N.G., Papano, R.E., A vital stain for the Golgi apparatus. Science 228 (1985), 745–747.
    • (1985) Science , vol.228 , pp. 745-747
    • Lipsky, N.G.1    Papano, R.E.2
  • 86
    • 0026777411 scopus 로고
    • Immunocytochemical analysis of the transfer from the intermediate compartment to the Golgi complex of VSV G-protein
    • Lotti, L., Porrisi, M., Pascale, M., Bonatti, S., Immunocytochemical analysis of the transfer from the intermediate compartment to the Golgi complex of VSV G-protein. J. Cell Biol. 118 (1992), 43–50.
    • (1992) J. Cell Biol. , vol.118 , pp. 43-50
    • Lotti, L.1    Porrisi, M.2    Pascale, M.3    Bonatti, S.4
  • 87
    • 0027102582 scopus 로고
    • Mimicking mitotic Golgi disassembly using okadaic acid
    • Lucocq, J., Mimicking mitotic Golgi disassembly using okadaic acid. J. Cell Sci. 103 (1992), 875–880.
    • (1992) J. Cell Sci. , vol.103 , pp. 875-880
    • Lucocq, J.1
  • 88
    • 0023441953 scopus 로고
    • Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells
    • Lucocq, J.M., Warren, G., Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J. 6 (1987), 3239–3246.
    • (1987) EMBO J. , vol.6 , pp. 3239-3246
    • Lucocq, J.M.1    Warren, G.2
  • 89
    • 0023252077 scopus 로고
    • A mitotic form of the Golgi apparatus in HeLa cells
    • Lucocq, J.M., Pryde, J.G., Berger, E.G., Warren, G., A mitotic form of the Golgi apparatus in HeLa cells. J. Cell Biol. 104 (1987), 865–874.
    • (1987) J. Cell Biol. , vol.104 , pp. 865-874
    • Lucocq, J.M.1    Pryde, J.G.2    Berger, E.G.3    Warren, G.4
  • 90
    • 0024409747 scopus 로고
    • Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway
    • Lucocq, J.M., Berger, E.G., Warren, G., Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway. J. Cell Biol. 109 (1989), 463–474.
    • (1989) J. Cell Biol. , vol.109 , pp. 463-474
    • Lucocq, J.M.1    Berger, E.G.2    Warren, G.3
  • 91
    • 0026318089 scopus 로고
    • Okadaic acid induces Golgi apparatus fragmentation and arrest of intracellular transport
    • Lucocq, J., Warren, G., Pryde, J., Okadaic acid induces Golgi apparatus fragmentation and arrest of intracellular transport. J. Cell Sci. 100 (1991), 753–759.
    • (1991) J. Cell Sci. , vol.100 , pp. 753-759
    • Lucocq, J.1    Warren, G.2    Pryde, J.3
  • 92
    • 0027517479 scopus 로고
    • Centrosome repositioning immediately following karyokinesis and prior to cytokinesis
    • Mack, G., Rattner, J.B., Centrosome repositioning immediately following karyokinesis and prior to cytokinesis. Cell Motil. Cytoskel. 26 (1993), 239–247.
    • (1993) Cell Motil. Cytoskel. , vol.26 , pp. 239-247
    • Mack, G.1    Rattner, J.B.2
  • 93
    • 0023905347 scopus 로고
    • Targeting of secretory vesicles to cytoplasmic domains in AtT20 and PC12 cells
    • Matsuuchi, L., Buckley, K., Lowe, A.W., Kelly, R.B., Targeting of secretory vesicles to cytoplasmic domains in AtT20 and PC12 cells. J. Cell Biol. 106 (1988), 239–251.
    • (1988) J. Cell Biol. , vol.106 , pp. 239-251
    • Matsuuchi, L.1    Buckley, K.2    Lowe, A.W.3    Kelly, R.B.4
  • 94
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni, R., Kreis, T.E., Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105 (1987), 1253–1265.
    • (1987) J. Cell Biol. , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 95
    • 0025184423 scopus 로고
    • Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2)
    • Matter, K., Bucher, K., Hauri, H.-P., Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2). EMBO J. 9 (1990), 3163–3170.
    • (1990) EMBO J. , vol.9 , pp. 3163-3170
    • Matter, K.1    Bucher, K.2    Hauri, H.-P.3
  • 97
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • Mellman, I., Simons, K., The Golgi complex: In vitro veritas?. Cell 68 (1992), 829–840.
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 98
    • 0027175236 scopus 로고
    • A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus
    • Mizuno, M., Singer, S.J., A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc. Natl. Acad. Sci. USA, 90, 1993, 5732–5736.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5732-5736
    • Mizuno, M.1    Singer, S.J.2
  • 99
    • 0028228643 scopus 로고
    • A possible role for stable microtubules in intra-cellular transport from the endoplasmic reticulum to the Golgi apparatus
    • Mizuno, M., Singer, S.J., A possible role for stable microtubules in intra-cellular transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Sci. 107 (1994), 1321–1331.
    • (1994) J. Cell Sci. , vol.107 , pp. 1321-1331
    • Mizuno, M.1    Singer, S.J.2
  • 100
    • 0025409872 scopus 로고
    • Disorganization and reorganization of the Golgi complex in association with mitosis
    • Moskalewski, S., Thyberg, J., Disorganization and reorganization of the Golgi complex in association with mitosis. J. Submicrosc. Cytol. Pathol. 22 (1990), 159–171.
    • (1990) J. Submicrosc. Cytol. Pathol. , vol.22 , pp. 159-171
    • Moskalewski, S.1    Thyberg, J.2
  • 101
    • 0026888733 scopus 로고
    • Synchronized shift in localization of the Golgi complex and the microtubule organizing center in the terminal phase of cytokinesis
    • Moskalewski, S., Thyberg, J., Synchronized shift in localization of the Golgi complex and the microtubule organizing center in the terminal phase of cytokinesis. J. Submicrosc. Cytol. Pathol. 24 (1992), 359–370.
    • (1992) J. Submicrosc. Cytol. Pathol. , vol.24 , pp. 359-370
    • Moskalewski, S.1    Thyberg, J.2
  • 102
    • 0028105461 scopus 로고
    • Functions of the Golgi complex in cell division: formation of cell-matrix contacts and cell-cell communication channels in the terminal phase of cytokinesis
    • Moskalewski, S., Popowicz, P., Thyberg, J., Functions of the Golgi complex in cell division: formation of cell-matrix contacts and cell-cell communication channels in the terminal phase of cytokinesis. J. Submicrosc. Cytol. Pathol. 26 (1994), 9–20.
    • (1994) J. Submicrosc. Cytol. Pathol. , vol.26 , pp. 9-20
    • Moskalewski, S.1    Popowicz, P.2    Thyberg, J.3
  • 103
    • 0026774954 scopus 로고
    • Interaction of the Golgi membranes isolated from rabbit liver with microtubules in vitro
    • Murata, M., Itoh, T.J., Kagiwada, S., Hishida, R., Hotani, H., Ohnishi, S., Interaction of the Golgi membranes isolated from rabbit liver with microtubules in vitro. Biol. Cell 75 (1992), 127–134.
    • (1992) Biol. Cell , vol.75 , pp. 127-134
    • Murata, M.1    Itoh, T.J.2    Kagiwada, S.3    Hishida, R.4    Hotani, H.5    Ohnishi, S.6
  • 104
    • 0026446341 scopus 로고
    • Regulation of cell surface polarity from bacteria to mammals
    • Nelson, W.J., Regulation of cell surface polarity from bacteria to mammals. Science 258 (1992), 948–955.
    • (1992) Science , vol.258 , pp. 948-955
    • Nelson, W.J.1
  • 105
    • 0021942168 scopus 로고
    • Reorientation of the Golgi apparatus and the microtubuleorganizing center inside macrophages subjected to a chemotactic gradient
    • Nemere, I., Kupfer, A., Singer, S.J., Reorientation of the Golgi apparatus and the microtubuleorganizing center inside macrophages subjected to a chemotactic gradient. Cell Motility 5 (1985), 17–29.
    • (1985) Cell Motility , vol.5 , pp. 17-29
    • Nemere, I.1    Kupfer, A.2    Singer, S.J.3
  • 106
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
    • Nilsson, T., Pypaert, M., Hoe, M.H., Slusarewicz, P., Berger, E.G., Warren, G., Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol. 120 (1993), 5–13.
    • (1993) J. Cell Biol. , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaert, M.2    Hoe, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 107
    • 0026586004 scopus 로고
    • γ-Tubulin: The microtubule organizer?
    • Oakley, B.R., γ-Tubulin: The microtubule organizer?. Trends Cell Biol. 2 (1992), 1–5.
    • (1992) Trends Cell Biol. , vol.2 , pp. 1-5
    • Oakley, B.R.1
  • 108
    • 0027074388 scopus 로고
    • Antimicrotubule drugs inhibit the polarized insertion of an intracellular glycoprotein pool into the apical membrane of Madin-Darby canine kidney (MDCK) cells
    • Ojakian, G.K., Schwimmer, R., Antimicrotubule drugs inhibit the polarized insertion of an intracellular glycoprotein pool into the apical membrane of Madin-Darby canine kidney (MDCK) cells. J. Cell Sci. 103 (1992), 677–687.
    • (1992) J. Cell Sci. , vol.103 , pp. 677-687
    • Ojakian, G.K.1    Schwimmer, R.2
  • 110
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade, G., Intracellular aspects of the process of protein secretion. Science 189 (1975), 347–358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 111
    • 0024454714 scopus 로고
    • Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial MDCK cells
    • Parczyk, K., Haase, W., Kondor-Koch, C., Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial MDCK cells. J. Biol. Chem. 264 (1989), 16837–16846.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16837-16846
    • Parczyk, K.1    Haase, W.2    Kondor-Koch, C.3
  • 112
    • 0025829695 scopus 로고
    • pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton, R., Dotti, C., Bacallao, R., Kurtz, I., Simons, K., Prydz, K., pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells. J. Cell Biol. 113 (1991), 261–274.
    • (1991) J. Cell Biol. , vol.113 , pp. 261-274
    • Parton, R.1    Dotti, C.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 113
    • 0019859435 scopus 로고
    • Journey to the center of the cell: Role of the receptosome
    • Pastan, I., Willingham, M.C., Journey to the center of the cell: Role of the receptosome. Science 214 (1981), 504–509.
    • (1981) Science , vol.214 , pp. 504-509
    • Pastan, I.1    Willingham, M.C.2
  • 114
    • 0020555148 scopus 로고
    • Effect of colchicine on the Golgi complex of rat pancreatic acinar cells
    • Pavelka, M., Ellinger, A., Effect of colchicine on the Golgi complex of rat pancreatic acinar cells. J. Cell Biol. 97 (1983), 737–748.
    • (1983) J. Cell Biol. , vol.97 , pp. 737-748
    • Pavelka, M.1    Ellinger, A.2
  • 115
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H.R.B., Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol. 5 (1989), 1–23.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 116
    • 0025764613 scopus 로고
    • Recycling of proteins between the endoplasmic reticulum and the Golgi complex
    • Pelham, H.R.B., Recycling of proteins between the endoplasmic reticulum and the Golgi complex. Curr. Opin. Cell Biol. 3 (1991), 585–591.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 585-591
    • Pelham, H.R.B.1
  • 117
    • 0026737234 scopus 로고
    • Different sorting of lys-asp-glu-leu proteins in rat liver
    • Peter, F., Van, P.N., Soling, H.-D., Different sorting of lys-asp-glu-leu proteins in rat liver. J. Biol. Chem. 267 (1992), 10631–10637.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10631-10637
    • Peter, F.1    Van, P.N.2    Soling, H.-D.3
  • 118
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer, S., Rothman, J.E., Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56 (1987), 829–852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.1    Rothman, J.E.2
  • 119
    • 0026439921 scopus 로고
    • Morphological analysis of protein transport in digitonin-permeabilized cells: role of the p58-containing compartment
    • Plutner, H., Davidson, H.W., Saraste, J., Balch, W.E., Morphological analysis of protein transport in digitonin-permeabilized cells: role of the p58-containing compartment. J. Cell Biol. 119 (1992), 1097–1116.
    • (1992) J. Cell Biol. , vol.119 , pp. 1097-1116
    • Plutner, H.1    Davidson, H.W.2    Saraste, J.3    Balch, W.E.4
  • 121
    • 0027278049 scopus 로고
    • Mitotic Golgi clusters are not tubular endosomes
    • Pypaert, M., Nilsson, T., Berger, E.G., Warren, G., Mitotic Golgi clusters are not tubular endosomes. J. Cell Sci. 104 (1993), 811–818.
    • (1993) J. Cell Sci. , vol.104 , pp. 811-818
    • Pypaert, M.1    Nilsson, T.2    Berger, E.G.3    Warren, G.4
  • 122
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • Rambourg, A., Clermont, Y., Three-dimensional electron microscopy: Structure of the Golgi apparatus. Eur. J. Cell Biol. 51 (1990), 189–200.
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 123
    • 0023293841 scopus 로고
    • Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells
    • Rindler, M.J., Ivanov, I.E., Sabatini, D.D., Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells. J. Cell Biol. 104 (1987), 231–241.
    • (1987) J. Cell Biol. , vol.104 , pp. 231-241
    • Rindler, M.J.1    Ivanov, I.E.2    Sabatini, D.D.3
  • 124
    • 0000782723 scopus 로고
    • Histochemical and ultrastructural studies on HeLa cell cultures exposed to spindle inhibitors with special reference to the interphase cell
    • Robbins, E., Gonatas, N.K., Histochemical and ultrastructural studies on HeLa cell cultures exposed to spindle inhibitors with special reference to the interphase cell. J. Histochem. Cytochem. 12 (1964), 704–711.
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 704-711
    • Robbins, E.1    Gonatas, N.K.2
  • 125
    • 0000759314 scopus 로고
    • The ultrastructure of a mammalian cell during the mitotic cycle
    • Robbins, E., Gonatas, N.K., The ultrastructure of a mammalian cell during the mitotic cycle. J. Cell Biol. 21 (1964), 429–463.
    • (1964) J. Cell Biol. , vol.21 , pp. 429-463
    • Robbins, E.1    Gonatas, N.K.2
  • 126
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth, J., Taatjes, D.J., Lucocq, J., Weinstein, J., Paulson, J.C., Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43 (1985), 287–295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1    Taatjes, D.J.2    Lucocq, J.3    Weinstein, J.4    Paulson, J.C.5
  • 127
    • 0023024461 scopus 로고
    • Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells
    • Roth, J., Taatjes, D.J., Weinstein, J., Paulson, J.C., Greenwell, P., Watkins, W.M., Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J. Biol. Chem. 261 (1986), 14307–14312.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14307-14312
    • Roth, J.1    Taatjes, D.J.2    Weinstein, J.3    Paulson, J.C.4    Greenwell, P.5    Watkins, W.M.6
  • 129
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J.E., Orci, L., Molecular dissection of the secretory pathway. Nature 355 (1992), 409–415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 130
    • 0022479585 scopus 로고
    • Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity
    • Salas, D.J.I., Misek, D.E., Vega-Salas, D.E., Gundersen, D., Cereijido, M., Rodriguez-Bolan, E., Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity. J. Cell Biol. 102 (1986), 1853–1867.
    • (1986) J. Cell Biol. , vol.102 , pp. 1853-1867
    • Salas, D.J.I.1    Misek, D.E.2    Vega-Salas, D.E.3    Gundersen, D.4    Cereijido, M.5    Rodriguez-Bolan, E.6
  • 131
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J., Kuismanen, E., Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38 (1984), 535–549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 132
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex
    • Saraste, J., Kuismanen, E., Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. Semin. Cell Biol. 3 (1992), 343–355.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 133
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste, J., Svensson, K., Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100 (1991), 415–430.
    • (1991) J. Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 134
    • 0025173003 scopus 로고
    • Microtubule depolymerization inhibits transport of cathepsin D from the Golgi apparatus to lysosomes
    • Scheel, J., Matteoni, R., Ludwig, T., Hoflack, B., Kreis, T.E., Microtubule depolymerization inhibits transport of cathepsin D from the Golgi apparatus to lysosomes. J. Cell Sci. 96 (1990), 711–720.
    • (1990) J. Cell Sci. , vol.96 , pp. 711-720
    • Scheel, J.1    Matteoni, R.2    Ludwig, T.3    Hoflack, B.4    Kreis, T.E.5
  • 135
    • 0027328703 scopus 로고
    • ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER-retention motif
    • Schindler, R., Itin, C., Zerial, M., Lottspeich, F., Hauri, H.-P., ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER-retention motif. Eur. J. Cell Biol. 61 (1993), 1–9.
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 1-9
    • Schindler, R.1    Itin, C.2    Zerial, M.3    Lottspeich, F.4    Hauri, H.-P.5
  • 136
    • 0026080525 scopus 로고
    • Functions of microtubule-based motors
    • Schroer, T.A., Sheetz, M.P., Functions of microtubule-based motors. Annu. Rev. Physiol. 53 (1991), 629–652.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 629-652
    • Schroer, T.A.1    Sheetz, M.P.2
  • 137
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Schweizer, A., Fransen, J.A.M., Matter, K., Kreis, T.E., Ginsel, L., Hauri, H.-P., Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to the Golgi apparatus. Eur. J. Cell Biol. 53 (1990), 185–196.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.M.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.-P.6
  • 138
    • 0026069437 scopus 로고
    • A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin
    • Serafini, T., Stenbeck, G., Brecht, A., Lottspeich, F., Orci, L., Rothman, J.E., Wieland, F.T., A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin. Nature 349 (1991), 215–220.
    • (1991) Nature , vol.349 , pp. 215-220
    • Serafini, T.1    Stenbeck, G.2    Brecht, A.3    Lottspeich, F.4    Orci, L.5    Rothman, J.E.6    Wieland, F.T.7
  • 139
    • 0027336491 scopus 로고
    • Mammalian G1 cyclins
    • Sherr, C.J., Mammalian G1 cyclins. Cell 73 (1993), 1059–1065.
    • (1993) Cell , vol.73 , pp. 1059-1065
    • Sherr, C.J.1
  • 140
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., Wandinger-Ness, A., Polarized sorting in epithelia. Cell 62 (1990), 207–210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 141
    • 0022854872 scopus 로고
    • The directed migration of eukaryotic cells
    • Singer, S.J., Kupfer, A., The directed migration of eukaryotic cells. Annu. Rev. Cell Biol. 2 (1986), 337–365.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 337-365
    • Singer, S.J.1    Kupfer, A.2
  • 142
    • 0025094169 scopus 로고
    • Spatial and temporal colocalization of the Golgi apparatus and microtubules rich in detyrosinated tubulin
    • Skoufias, D.A., Burgess, T.L., Wilson, L., Spatial and temporal colocalization of the Golgi apparatus and microtubules rich in detyrosinated tubulin. J. Cell Biol. 111 (1990), 1929–1937.
    • (1990) J. Cell Biol. , vol.111 , pp. 1929-1937
    • Skoufias, D.A.1    Burgess, T.L.2    Wilson, L.3
  • 143
    • 0027274611 scopus 로고
    • The Golgi stack reassembles during telophase before arrival of proteins transported from the endoplasmic reticulum
    • Souter, E., Pypaert, M., Warren, G., The Golgi stack reassembles during telophase before arrival of proteins transported from the endoplasmic reticulum. J. Cell Biol. 122 (1993), 533–540.
    • (1993) J. Cell Biol. , vol.122 , pp. 533-540
    • Souter, E.1    Pypaert, M.2    Warren, G.3
  • 144
    • 0025849047 scopus 로고
    • γ-Tubulin is a highly conserved component of the centrosome
    • Stearns, T., Evans, L., Kirschner, M., γ-Tubulin is a highly conserved component of the centrosome. Cell 65 (1991), 825–836.
    • (1991) Cell , vol.65 , pp. 825-836
    • Stearns, T.1    Evans, L.2    Kirschner, M.3
  • 145
    • 0025766292 scopus 로고
    • Brefeldin A induces a microtubule-dependent fusion of galactosyltransferase-containing vesicles with the rough endoplasmic reticulum
    • Strous, G.J., Berger, E.G., van Kerkhof, P., Bosshart, H., Berger, B., Geuze, H.J., Brefeldin A induces a microtubule-dependent fusion of galactosyltransferase-containing vesicles with the rough endoplasmic reticulum. Biol. Cell 71 (1991), 25–31.
    • (1991) Biol. Cell , vol.71 , pp. 25-31
    • Strous, G.J.1    Berger, E.G.2    van Kerkhof, P.3    Bosshart, H.4    Berger, B.5    Geuze, H.J.6
  • 146
    • 0024357921 scopus 로고
    • Relationship between Golgi architecture and glycoprotein biosynthesis and transport in chinese hamster ovary cells
    • Stults, N.L., Felhheimer, M., Cummings, R.D., Relationship between Golgi architecture and glycoprotein biosynthesis and transport in chinese hamster ovary cells. J. Biol. Chem. 264 (1989), 19956–19966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19956-19966
    • Stults, N.L.1    Felhheimer, M.2    Cummings, R.D.3
  • 147
    • 0346018912 scopus 로고
    • Tubular lysosome morphology and distribution within macrophages depend on the integrity of cytoplasmic microtubules
    • Swanson, J., Bushnell, A., Silverstein, S.C., Tubular lysosome morphology and distribution within macrophages depend on the integrity of cytoplasmic microtubules. Proc. Natl. Acad. Sci. USA, 84, 1987, 1921–1925.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1921-1925
    • Swanson, J.1    Bushnell, A.2    Silverstein, S.C.3
  • 148
    • 0027174945 scopus 로고
    • Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone
    • Takizawa, P.A., Yucel, J.K., Veit, B., Faulkner, D.J., Deerinck, T., Soto, G., Ellisman, M., Malhotra, V., Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone. Cell 73 (1993), 1079–1090.
    • (1993) Cell , vol.73 , pp. 1079-1090
    • Takizawa, P.A.1    Yucel, J.K.2    Veit, B.3    Faulkner, D.J.4    Deerinck, T.5    Soto, G.6    Ellisman, M.7    Malhotra, V.8
  • 149
    • 0025966562 scopus 로고
    • Three-dimensional organization of the Golgi complex observed by scanning electron microscopy
    • Tanaka, K., Fukudome, H., Three-dimensional organization of the Golgi complex observed by scanning electron microscopy. J. Electron. Microsc. Tech. 17 (1991), 15–23.
    • (1991) J. Electron. Microsc. Tech. , vol.17 , pp. 15-23
    • Tanaka, K.1    Fukudome, H.2
  • 150
    • 0022416553 scopus 로고
    • The Golgi apparatus remains associated with microtubule organizing centers during myogenesis
    • Tassin, A.M., Paintrand, M., Berger, E.G., Bornens, M., The Golgi apparatus remains associated with microtubule organizing centers during myogenesis. J. Cell Biol. 101 (1985), 630–638.
    • (1985) J. Cell Biol. , vol.101 , pp. 630-638
    • Tassin, A.M.1    Paintrand, M.2    Berger, E.G.3    Bornens, M.4
  • 151
    • 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., Chen, L.B., Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes. Cell 38 (1984), 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
  • 152
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki, M., Chen, L.B., Fujiwara, K., Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103 (1986), 1557–1568.
    • (1986) J. Cell Biol. , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.B.2    Fujiwara, K.3
  • 153
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg, J., Moskalewski, S., Microtubules and the organization of the Golgi complex. Exp. Cell Res. 159 (1985), 1–16.
    • (1985) Exp. Cell Res. , vol.159 , pp. 1-16
    • Thyberg, J.1    Moskalewski, S.2
  • 154
    • 0024542597 scopus 로고
    • Subpopulations of microtubules with differential sensitivity to nocodazole: Role in the structural organization of the Golgi complex and the lysosomal system
    • Thyberg, J., Moskalewski, S., Subpopulations of microtubules with differential sensitivity to nocodazole: Role in the structural organization of the Golgi complex and the lysosomal system. J. Submicrosc. Cytol. Pathol. 21 (1989), 259–274.
    • (1989) J. Submicrosc. Cytol. Pathol. , vol.21 , pp. 259-274
    • Thyberg, J.1    Moskalewski, S.2
  • 155
    • 0026936078 scopus 로고
    • Reorganization of the Golgi complex in association with mitosis: redistribution of mannosidase II to the endoplasmic reticulum and effects of brefeldin A
    • Thyberg, J., Moskalewski, S., Reorganization of the Golgi complex in association with mitosis: redistribution of mannosidase II to the endoplasmic reticulum and effects of brefeldin A. J. Submicrosc. Cytol. Pathol. 24 (1992), 495–508.
    • (1992) J. Submicrosc. Cytol. Pathol. , vol.24 , pp. 495-508
    • Thyberg, J.1    Moskalewski, S.2
  • 156
    • 0027074332 scopus 로고
    • Disorganization of the Golgi complex and the cytoplasmic microtubule system in CHO cells exposed to okadaic acid
    • Thyberg, J., Moskalewski, S., Disorganization of the Golgi complex and the cytoplasmic microtubule system in CHO cells exposed to okadaic acid. J. Cell Sci. 103 (1992), 1167–1175.
    • (1992) J. Cell Sci. , vol.103 , pp. 1167-1175
    • Thyberg, J.1    Moskalewski, S.2
  • 157
    • 0027248928 scopus 로고
    • Relationship between the Golgi complex and microtubules enriched in detyrosinated or acetylated α-tubulin: Studies on cells recovering from nocodazole and cells in the terminal phase of cytokinesis
    • Thyberg, J., Moskalewski, S., Relationship between the Golgi complex and microtubules enriched in detyrosinated or acetylated α-tubulin: Studies on cells recovering from nocodazole and cells in the terminal phase of cytokinesis. Cell Tissue Res. 273 (1993), 457–466.
    • (1993) Cell Tissue Res. , vol.273 , pp. 457-466
    • Thyberg, J.1    Moskalewski, S.2
  • 158
    • 0023262142 scopus 로고
    • Accumulation of adrenocorticotropin secretory granules in the midbody of telophase AtT20 cells: Evidence that secretory granules move anterogradely along microtubules
    • Tooze, J., Burke, B., Accumulation of adrenocorticotropin secretory granules in the midbody of telophase AtT20 cells: Evidence that secretory granules move anterogradely along microtubules. J. Cell Biol. 1004 (1987), 1047–1057.
    • (1987) J. Cell Biol. , vol.1004 , pp. 1047-1057
    • Tooze, J.1    Burke, B.2
  • 159
    • 0026670214 scopus 로고
    • Evidence that globular Golgi clusters in mitotic HeLa cells are clustered tubular endosomes
    • Tooze, J., Hollinshead, M., Evidence that globular Golgi clusters in mitotic HeLa cells are clustered tubular endosomes. Eur. J. Cell Biol. 58 (1992), 228–242.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 228-242
    • Tooze, J.1    Hollinshead, M.2
  • 160
    • 0024418264 scopus 로고
    • Morphological and biochemical evidence showing neuronal properties in AtT20 cells and their growth cones
    • Tooze, J., Hollinshead, M., Fuller, S.D., Tooze, S.A., Huttner, W.B., Morphological and biochemical evidence showing neuronal properties in AtT20 cells and their growth cones. Eur. J. Cell Biol. 49 (1989), 259–273.
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 259-273
    • Tooze, J.1    Hollinshead, M.2    Fuller, S.D.3    Tooze, S.A.4    Huttner, W.B.5
  • 161
    • 0026332190 scopus 로고
    • Characterization of the immature secretory granule, an intermediate in granule biogenesis
    • Tooze, S., Flatmark, T., Tooze, J., Huttner, W.B., Characterization of the immature secretory granule, an intermediate in granule biogenesis. J. Cell Biol. 115 (1991), 1491–1503.
    • (1991) J. Cell Biol. , vol.115 , pp. 1491-1503
    • Tooze, S.1    Flatmark, T.2    Tooze, J.3    Huttner, W.B.4
  • 162
    • 0024432435 scopus 로고
    • The response of the Golgi complex to microtubule alterations: The roles of metabolic energy and membrane traffic in Golgi complex organization
    • Turner, J.R., Tartakoff, A.M., The response of the Golgi complex to microtubule alterations: The roles of metabolic energy and membrane traffic in Golgi complex organization. J. Cell Biol. 109 (1989), 2081–2088.
    • (1989) J. Cell Biol. , vol.109 , pp. 2081-2088
    • Turner, J.R.1    Tartakoff, A.M.2
  • 163
    • 0024211157 scopus 로고
    • Formation of membrane networks in vitro by kinesin-driven microtubule movement
    • Vale, R.D., Hotani, H., Formation of membrane networks in vitro by kinesin-driven microtubule movement. J. Cell Biol. 107 (1988), 2233–2241.
    • (1988) J. Cell Biol. , vol.107 , pp. 2233-2241
    • Vale, R.D.1    Hotani, H.2
  • 164
    • 0025134873 scopus 로고
    • Transfer of secretory proteins from the endoplasmic reticulum to the Golgi apparatus: Discrimination between homologous and heterologous transfer in intact heterokaryons
    • Valtersson, C., Dutton, A.H., Singer, S.J., Transfer of secretory proteins from the endoplasmic reticulum to the Golgi apparatus: Discrimination between homologous and heterologous transfer in intact heterokaryons. Proc. Natl. Acad. Sci. USA, 87, 1990, 8175–8179.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8175-8179
    • Valtersson, C.1    Dutton, A.H.2    Singer, S.J.3
  • 166
    • 0025518412 scopus 로고
    • Microtubule perturbation inhibits intracellular transport of an apical membrane glycoprotein in a substrate-dependent manner in polarized Madin-Darby canine kidney epithelial cells
    • van Zeijl, M.J.A.H., Matlin, K.S., Microtubule perturbation inhibits intracellular transport of an apical membrane glycoprotein in a substrate-dependent manner in polarized Madin-Darby canine kidney epithelial cells. Cell Regul. 1 (1990), 921–936.
    • (1990) Cell Regul. , vol.1 , pp. 921-936
    • van Zeijl, M.J.A.H.1    Matlin, K.S.2
  • 168
    • 0027267694 scopus 로고
    • Cytoplasmic microtubule-associated motors
    • Walker, R.A., Sheetz, M.P., Cytoplasmic microtubule-associated motors. Annu. Rev. Biochem. 62 (1993), 429–451.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 429-451
    • Walker, R.A.1    Sheetz, M.P.2
  • 169
    • 0022395805 scopus 로고
    • Membrane traffic and organelle division
    • Warren, G., Membrane traffic and organelle division. Trends Biochem. Sci. 10 (1985), 439–443.
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 439-443
    • Warren, G.1
  • 170
    • 0027183419 scopus 로고
    • Membrane partitioning during cell division
    • Warren, G., Membrane partitioning during cell division. Annu. Rev. Biochem. 62 (1993), 323–348.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 323-348
    • Warren, G.1
  • 171
    • 0006327768 scopus 로고
    • Role of microtubules in the distribution of the Golgi apparatus: Effect of taxol and microinjected anti-α-tubulin antibodies
    • Wehland, J., Henkart, M., Klausner, R., Sandoval, I.V., Role of microtubules in the distribution of the Golgi apparatus: Effect of taxol and microinjected anti-α-tubulin antibodies. Proc. Natl. Acad. Sci. USA, 80, 1983, 4286–4290.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4286-4290
    • Wehland, J.1    Henkart, M.2    Klausner, R.3    Sandoval, I.V.4
  • 172
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner, O.H., Murphy, J., Griffiths, G., Schleicher, M., Noegel, A.A., The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J. Cell Biol. 123 (1993), 23–34.
    • (1993) J. Cell Biol. , vol.123 , pp. 23-34
    • Weiner, O.H.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5
  • 174
    • 0025872685 scopus 로고
    • γ-Tubulin is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome
    • Zheng, Y., Jung, M.K., Oakley, B.R., γ-Tubulin is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome. Cell 65 (1991), 817–823.
    • (1991) Cell , vol.65 , pp. 817-823
    • Zheng, Y.1    Jung, M.K.2    Oakley, B.R.3


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