Role of microtubules in the organization of the Golgi complex

Experimental Cell Research

Volumn 246, Issue 2, 1999, Pages 263-279

  Thyberg, Johan ^a   Moskalewski, Stanislaw ^b  

^a KAROLINSKA INSTITUTE   (Sweden)

^b MEDICAL UNIVERSITY OF WARSAW   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; CELL MEMBRANE TRANSPORT; CELL ORGANELLE; CELL STRUCTURE; GOLGI COMPLEX; MAMMAL CELL; MICROTUBULE; MITOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN TRANSPORT; REVIEW; STRUCTURE ANALYSIS;

ANIMALIA; MAMMALIA;

EID: 0033080404     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4326     Document Type: Review

References (234)

1. Alberts B., Bray D., Lewis J., Raff M., Roberts K., Watson J. D. Molecular Biology of the Cell. 1994;Garland, New York.
2. Thyberg J., Moskalewski S. Microtubules and the organization of the Golgi complex. Exp. Cell Res. 159:1985;1-16.
3. Kirschner M., Mitchison T. Beyond self-assembly: From microtubules to morphogenesis. Cell. 45:1986;329-342.
4. Gelfand V. I., Bershadsky A. D. Microtubule dynamics: Mechanism, regulation, and function. Annu. Rev. Cell Biol. 7:1991;93-116.
5. Desai A., Mitchison T. J. Microtubule polymerization dynamics. Annu. Rev. Cell Dev. Biol. 13:1997;83-117.
6. Walker R. A., Sheetz M. P. Cytoplasmic microtubule-associated motors. Annu. Rev. Biochem. 62:1993;429-451.
7. Scholey J. M., Vale R. D. Kinesin-based organelle transport. Microtubules. 1994;Wiley-Liss, New York. p. 343-365.
8. Collins C. A. Dynein-based organelle movement. Hyams J. S., Lloyd C. W. Microtubules. 1994;367-380 Wiley-Liss, New York.
9. Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 279:1998;519-526.
10. Pelham H. R. B., Munro S. Sorting of membrane proteins in the secretory pathway. Cell. 75:1993;603-605.
11. Nilsson T., Warren G. Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol. 6:1994;517-521.
12. Rothman J. E. The protein machinery of vesicle budding and fusion. Protein Sci. 5:1996;185-194.
13. Mandelkow E., Mandelkow E.-M. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7:1995;72-81.
14. Wade R. H., Hyman A. A. Microtubule structure and dynamics. Curr. Opin. Cell Biol. 9:1997;12-17.
15. Cleveland D. W. Autoregulated instability of tubulin mRNAs:A. Trends Biochem. Sci. 13:1988;339-343.
16. Gonzalez-Garay M. L., Cabral F. α-Tubulin limits its own synthesis: Evidence for a mechanism involving translational repression. J. Cell Biol. 135:1996;1525-1534.
17. Joshi H. C. Microtubule organizing centers and γ-tubulin. Curr. Opin. Cell Biol. 6:1994;55-62.
18. Kellogg D. R., Moritz M., Alberts B. M. The centrosome and cellular organization. Annu. Rev. Biochem. 63:1994;639-674.
19. Zheng Y., Jung M. K., Oakley B. R. γ-Tubulin is present inDrosophila melanogasterHomo sapiens. Cell. 65:1991;817-823.
20. Stearns T., Evans L., Kirschner M. γ-Tubulin is a highly conserved component of the centrosome. Cell. 65:1991;825-836.
21. Zheng Y., Wong M. L., Alberts B., Mitchison T. Nucleation of microtubule assembly by a γ-tubulin-containing ring complex. Nature. 378:1995;578-583.
22. Moritz M., Braunfeld M. B., Sedat J. W., Alberts B., Agard D. A. Microtubule nucleation by γ-tubulin-containing rings in the centrosome. Nature. 378:1995;638-640.
23. Kalt A., Schliwa M. Molecular components of the centrosome. Trends Cell Biol. 3:1993;118-128.
24. Kristofferson D., Mitchison T., Kirschner M. Direct observation of steady-state microtubule dynamics. J. Cell Biol. 102:1986;1007-1019.
25. Schulze E., Kirschner M. Microtubule dynamics in interphase cells. J. Cell Biol. 102:1986;1020-1031.
26. Schulze E., Kirschner M. c and stable populations of microtubules in cells. J. Cell Biol. 104:1987;277-288.
27. Erickson H. P., O'Brien E. T. Microtubule dynamic instability and GTP hydrolysis. Annu. Rev. Biophys. Biomol. Struct. 21:1992;145-166.
28. Drechsel D. N., Kirschner M. W. The minimum GTP cap required to stabilize microtubules. Curr. Biol. 4:1994;1053-1061.
29. Schulze E., Kirschner M. New features of microtubule behaviour observed in vivo. Nature. 334:1988;356-359.
30. Gundersen G. G., Kalnoski M. H., Bulinski J. C. Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo. Cell. 38:1984;779-789.
31. Piperno G., LeDizet M., Chang X. Microtubules containing acetylated α-tubulin in mammalian cells in culture. J. Cell Biol. 104:1987;289-302.
32. Bulinski J. C., Richards J. E., Piperno G. Posttranslational modifications of α tubulin: Detyrosination and acetylation differentiate populations of interphase microtubules in cultured cells. J. Cell Biol. 106:1988;1213-1220.
33. Greer, K. Rosenbaum, J. L. 1989, Post-translational modifications of tubulin, In, Cell Movement, 2, Kinesin, Dynein, and Microtubule Dynamics, F. D. WarnerP. SatirI. R. Gibbons, 47, 66, A. R. Liss, New York.
34. Bulinski J. C., Gundersen G. G. Stabilization and post-translational modification of microtubules during cellular morphogenesis. Bioessays. 13:1991;285-293.
35. Wilson L., Jordan M. A. Pharmacological probes of microtubule function. Hyams J. S., Lloyd C. W. Microtubules. 1994;59-83 Wiley-Liss, New York.
36. 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. Cancer Res. 36:1976;905-916.
37. Hoebeke J., Van Nijen G., De Brabander M. Interaction of oncodazole (R 17934), a new anti-tumoral drug, with rat brain tubulin. Biochem. Biophys. Res. Commun. 69:1976;319-324.
38. 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.
39. Schiff P. B., Horwitz S. B. Taxol stabilizes microtubules in mouse fibroblast cells. Proc. Natl. Acad. Sci. USA. 77:1980;1561-1565.
40. Rowinsky E. K., Donehower R. C. Paclitaxel (Taxol). N. Engl. J. Med. 332:1995;1004-1014.
41. Palade G. Intracellular aspects of the process of protein secretion. Science. 189:1975;347-358.
42. Farquhar M. G., Palade G. E. The Golgi apparatus (complex) - (1954-1981) - from artifact to center stage. J. Cell Biol. 91:1981;77s-103s.
43. Slot J. W., Geuze H. J. Immunoelectron microscopic exploration of the Golgi complex. J. Histochem. Cytochem. 31:1983;1049-1056.
44. Pavelka M., Ellinger A. Cytochemical characteristics of the Golgi apparatus. J. Electron Microsc. Tech. 17:1991;35-50.
45. Roth J. Localization of glycosylation sites in the Golgi apparatus using immunolabeling and cytochemistry. J. Electron Microsc. Tech. 17:1991;121-131.
46. Rambourg A., Clermont Y. Three-dimensional electron microscopy: Structure of the Golgi apparatus. Eur. J. Cell Biol. 51:1990;189-200.
47. Tanaka K., Fukudome H. Three-dimensional organization of the Golgi complex observed by scanning electron microscopy. J. Electron Microsc. Tech. 17:1991;15-23.
48. Clermont Y., Rambourg A., Hermo L. Trans-Golgi network (TGN) of different cell types: Three-dimensional structural characteristics and variability. Anat. Rec. 242:1995;289-301.
49. Weidman P., Roth R., Heuser J. Golgi membrane dynamics imaged by freeze-etch electron microscopy: Views of different membrane coatings involved in tubulation versus vesiculation. Cell. 75:1993;123-133.
50. 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.
51. 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.
52. Saraste J., Svensson K. Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100:1991;415-430.
53. Bannykh S. I., Rowe T., Balch W. E. The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135:1996;19-35.
54. Hauri H.-P., Schweizer A. The endoplasmic reticulum-Golgi intermediate compartment. Curr. Opin. Cell Biol. 4:1992;600-608.
55. 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.
56. Pelham H. R. B. Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol. 7:1995;530-535.
57. Bannykh S. I., Balch W. E. Selective transport of cargo between the endoplasmic reticulum and Golgi compartments. Histochem. Cell Biol. 109:1998;463-475.
58. Presley J. F., Cole N. B., Schroer T. A., Hirschberg K., Zaal K. J. M., Lippincott-Schwartz J. ER-to-Golgi transport visualized in living cells. Nature. 389:1997;81-85.
59. Scales S. J., Pepperkok R., Kreis T. E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell. 90:1997;1137-1148.
60. Morré D. J., Kartenbeck J., Franke W. W. Membrane flow and interconversions among membranes. Biochim. Biophys. Acta. 559:1979;71-152.
61. Mollenhauer H. H., Morré D. J. Perspectives on Golgi apparatus form and function. J. Electron Microsc. Tech. 17:1991;2-14.
62. Pfeffer S. R., Rothman J. E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56:1987;829-852.
63. Mellman I., Simons K. The Golgi complex: In vitro veritas. Cell. 68:1992;829-840.
64. 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.
65. 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.
66. Velasco A., Hendricks L., Moremen K. W., Tulsiani D. R. P., Touster O., Farquhar M. G. Cell type-dependent variations in the subcellular distribution of α-mannosidase I and II. J. Cell Biol. 122:1993;39-51.
67. Glick B. S., Elston T., Oster G. A cisternal maturation mechanism can explain the asymmetry of the Golgi stack. FEBS Lett. 414:1997;177-181.
68. Mironov A. A., Weidman P., Luini A. Variations on the intracellular transport theme: Maturing cisternae and trafficking tubules. J. Cell Biol. 138:1997;481-484.
69. Füllekrug J., Nilsson T. Protein sorting in the Golgi complex. Biochim. Biophys. Acta. 1404:1998;77-84.
70. Lippincott-Schwartz J., Cole N., Presley J. Unravelling Golgi membrane traffic with green fluorescent protein chimeras. Trends Cell Biol. 8:1998;16-20.
71. 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.
72. Slusarewicz P., Nilsson T., Hui N., Watson R., Warren G. Isolation of a matrix that binds medial Golgi enzymes. J. Cell Biol. 124:1994;405-413.
73. Rabouille C., Nilsson T. Redrawing compartmental boundaries in the exocytic pathway. FEBS Lett. 369:1995;97-100.
74. Rothman J. E., Warren G. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4:1994;220-233.
75. Barr F. A., Warren G. Disassembly and reassembly of the Golgi apparatus. Semin. Cell Dev. Biol. 7:1996;505-510.
76. Nilsson T., Rabouille C., Hui N., Watson R., Warren G. The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J. Cell Sci. 109:1996;1975-1989.
77. Nakamura N., Rabouille C., Watson R., Nilsson T., Hui N., Slusarewicz P., Kreis T. E., Warren G. Characterization of a cis-Golgi matrix protein, GM130. J. Cell Biol. 131:1995;1715-1726.
78. Nakamura N., Lowe M., Levine T. P., Rabouille C., Warren G. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell. 89:1997;445-455.
79. Barr F. A., Puype M., Vandekerckhove J., Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell. 91:1997;253-262.
80. Schekman R., Orci L. Coat proteins and vesicle budding. Science. 271:1996;1526-1533.
81. Harter C., Wieland F. The secretory pathway: Mechanisms of protein sorting and transport. Biochim. Biophys. Acta. 1286:1996;75-93.
82. Pfeffer S. R. Transport vesicle docking: SNAREs and associates. Annu. Rev. Cell Dev. Biol. 12:1996;441-461.
83. Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12:1996;575-625.
84. Schmid S. L. Clathrin-coated vesicle formation and protein sorting: An integrated process. Annu. Rev. Biochem. 66:1997;511-548.
85. Hirst J., Robinson M. S. Clathrin and adaptors. Biochim. Biophys. Acta. 1404:1998;173-193.
86. Barlowe C., Orci L., Yeung T., Hosobuchi M., Hamamoto S., Salama N., Rexach M. F., Ravazzola M., Amherdt M., Schekman R. COPII:A. Cell. 77:1994;895-907.
87. Bednarek S. Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R., Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 83:1995;1183-1196.
88. Kuehn M. J., Herrmann J. M., Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 391:1998;187-190.
89. Aridor M., Weissman J., Bannykh S., Nuoffer C., Balch W. E. Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol. 141:1998;61-70.
90. Barlowe C. COPII and selective export from the endoplasmic reticulum. Biochim. Biophys. Acta. 1404:1998;67-76.
91. Bannykh S. I., Balch W. E. Selective transport of cargo between the endoplasmic reticulum and Golgi compartments. Histochem. Cell Biol. 109:1998;463-475.
92. Schekman R., Mellman I. Does COPI go both ways. Cell. 90:1997;197-200.
93. Orci L., Stamnes M., Ravazzola M., Amherdt M., Perrelet A., Söllner T. H., Rothman J. E. Bidirectional transport by distinct populations of COPI-coated vesicles. Cell. 90:1997;335-349.
94. Tisdale E. J., Plutner H., Matteson J., Balch W. E. p53/p58 binds COPI and is required for selective transport through the early secretory pathway. J. Cell Biol. 137:1997;581-593.
95. Pepperkok R., Lowe M., Burke B., Kreis T. E. Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTPγS. J. Cell Sci. 111:1998;1877-1888.
96. Lowe M., Kreis T. E. Regulation of membrane traffic in animal cells by COPI. Biochim. Biophys. Acta. 1404:1998;53-66.
97. Dinter A., Berger E. G. Golgi-disturbing agents. Histochem. Cell Biol. 109:1998;571-590.
98. Storrie B., Yang W. Dynamics of the interphase mammalian Golgi complex as revealed through drugs producing reversible Golgi disassembly. Biochim. Biophys. Acta. 1404:1998;127-137.
99. Fujiwara T., Oda K., Yokata S., Takatsuki A., Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263:1988;18545-18552.
100. Lippincott-Schwartz J., Yuan L. C., Bonifacino J. S., Klausner R. D. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER. Cell. 56:1989;801-813.
101. Doms R. W., Russ G., Yewdell J. W. Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109:1989;61-72.
102. Lippincott-Schwartz J., Donaldson J. G., Schweizer A., Berger E. G., Hauri H.-P., Yuan 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.
103. Orci L., Tagaya M., Amherdt M., Perrelet A., Donaldson J. G., Lippincott-Schwartz J., Klausner R. D., Rothman J. E. Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae. Cell. 64:1991;1183-1195.
104. 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.
105. Lucocq J., Warren G., Pryde J. Okadaic acid induces Golgi apparatus fragmentation and arrest of intracellular transport. J Cell Sci. 100:1991;753-759.
106. 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.
107. Reaven E., Tsai L., Maffe B., Azhar S. Effect of okadaic acid on hepatocyte structure and function. Cell. Mol. Biol. Res. 39:1993;275-288.
108. Horn M., Banting G. Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surface. Biochem. J. 301:1994;69-73.
109. Lucocq J., Berger E., Hug C. The pathway of Golgi cluster formation in okadaic acid-treated cells. J. Struct. Biol. 115:1995;318-330.
110. Takizawa P. A., Yucel J. K., Veit B., Faulkner 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.
111. Veit B., Yucel J. K., Malhotra V. Microtubule independent vesiculation of Golgi membranes and the reassembly of vesicles into Golgi stacks. J. Cell Biol. 122:1993;1197-1206.
112. Jamora C., Takizawa P. A., Zaarour R. F., Denesvre C., Faulkner D. J., Malhotra V. Regulation of Golgi structure through heterotrimeric G proteins. Cell. 91:1997;617-626.
113. Stults N. L., Fechheimer 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.
114. Van De Moortele, Picart R., Tixier-Vidal A., Tougard C. Nocodazole and Taxol affect subcellular compartments but not secretory activity of GH3B6 prolactin cells. Eur. J. Cell Biol. 60:1993;217-227.
115. Robin P., Rossignol B., Raymond M.-N. Effect of microtubule network disturbance by nocodazole and docetaxel (Taxotere) on protein secretion in rat extraorbital lacrimal and parotid glands. Eur. J. Cell Biol. 67:1995;227-237.
116. 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.
117. 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.
118. 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.
119. Parczyk K., Haase W., Kondor-Koch C. Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial cell, Madin-Darby canine kidney. J. Biol. Chem. 264:1989;16837-16846.
120. 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.
121. 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.
122. 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.
123. 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.
124. 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.
125. 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.
126. Cole N. B., Sciaky N., Marotta A., Song J., Lippincott-Schwartz J. Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell. 7:1996;631-650.
127. Yang W., Storrie B. Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins. Mol. Biol. Cell. 9:1998;191-207.
128. 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.
129. 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.
130. 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.
131. 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.
132. 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.
133. Cole N. B., Lippincott-Schwartz J. Organization of organelles and membrane traffic by microtubules. Curr. Opin. Cell Biol. 7:1995;55-64.
134. Saraste, J. Thyberg, J. 1996, Function of microtubules in protein secretion and organization of the Golgi complex, In, The Cytoskeleton, 2, Role in Cell Physiology, J. E. HeskethI. F. Pryme, 239, 273, JAI Press, Greenwich.
135. Lane J., Allan V. Microtubule-based membrane movement. Biochim. Biophys. Acta. 1376:1998;27-55.
136. Bloom G. S., Goldstein L. S. B. Cruising along microtubule highways: How membranes move through the secretory pathway. J. Cell Biol. 140:1998;1277-1280.
137. Langford G. M. Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7:1995;82-88.
138. Goodson H. V., Valetti C., Kreis T. E. Motors and membrane traffic. Curr. Opin. Cell Biol. 9:1997;18-28.
139. Lippincott-Schwartz J. Cytoskeletal proteins and Golgi dynamics. Curr. Opin. Cell Biol. 10:1998;52-59.
140. Mermall V., Post P. L., Mooseker M. S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
141. 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. 48:1989;250-263.
142. Ho W. C., Storrie B., Pepperkok R., Ansorge W., Karecla P., Kreis T. E. Movement of interphase Golgi apparatus in fused mammalian cells and its relationship to cytoskeletal elements and rearrangement of nuclei. Eur. J. Cell Biol. 52:1990;315-327.
143. 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.
144. 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.
145. Fath K. R., Trimbur G. M., Burgess D. R. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126:1994;661-675.
146. Marks D. L., Larkin J. M., McNiven M. A. Association of kinesin with the Golgi apparatus in rat hepatocytes. J. Cell Sci. 107:1994;2417-2426.
147. Lippincott-Schwartz J., Cole N. B., Marotta A., Conrad P. A., Bloom G. S. Kinesin is the motor for microtubule-mediated Golgi-to-ER membrane traffic. J. Cell Biol. 128:1995;293-306.
148. Johnson K. J., Hall E. S., Boekelheide K. Kinesin localizes to the trans-Golgi network regardless of microtubule organization. Eur. J. Cell Biol. 69:1996;276-287.
149. 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. 133:1996;831-842.
150. Fath K. R., Trimbur G. M., Burgess D. R. Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J. Cell Biol. 139:1997;1169-1181.
151. Harada A., Takei Y., Kanai Y., Nonaka S., Hirokawa N. Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 141:1998;51-59.
152. Minin A. A. Dispersal of Golgi apparatus in nocodazole-treated fibroblasts is a kinesin-driven process. J. Cell Sci. 110:1997;2495-2505.
153. Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A., Hirokawa N. Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell. 93:1998;1147-1158.
154. Henley J. R., McNiven M. A. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:1996;761-775.
155. 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. 279:1998;573-577.
156. Burkhardt J. K., Echeverri C. J., Nilsson T., Vallee R. B. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139:1997;469-484.
157. Kumar J., Yu H., Sheetz M. P. Kinectin, an essential anchor for kinesin-driven vesicle motility. Science. 267:1995;1834-1837.
158. Burkhardt J. K. In search of membrane receptors for microtubule-based motors - Is kinectin a kinesin receptor. Trends Cell Biol. 6:1996;127-131.
159. Beck K. A., Buchanan J. A., Nelson W. J. Golgi membrane skeleton: Identification, localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex. J. Cell Sci. 110:1997;1239-1249.
160. Holleran E. A., Holzbaur E. L. F. Speculating about spectrin: New insights into the Golgi-associated cytoskeleton. Trends Cell Biol. 8:1998;26-29.
161. Ikonen E., De Almeid J. B., Fath K. R., Burgess D. R., Ashman K., Simons K., Stow J. L. Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles. J. Cell Sci. 110:1997;2155-2164.
162. Stow J. L., Fath K. R., Burgess D. R. Budding roles for myosin II on the Golgi. Trends Cell Biol. 8:1998;138-141.
163. Warren G. Membrane partitioning during cell division. Annu. Rev. Biochem. 62:1993;323-348.
164. Lowe M., Nakamura N., Warren G. Golgi division and membrane traffic. Trends Cell Biol. 8:1998;40-44.
165. Thyberg J., Moskalewski S. Partitioning of cytoplasmic organelles during mitosis with special reference to the Golgi complex. Microsc. Res. Tech. 40:1998;354-368.
166. King R. W., Jackson P. K., Kirschner M. W. Mitosis in transition. Cell. 79:1994;563-571.
167. 2. Cancer Surv. 29:1997;47-73.
168. Hepler P. K. Calcium and mitosis. Int. Rev. Cytol. 138:1992;239-268.
169. Shiina N., Gotoh Y., Nishida E. Microtubule-severing activity in M phase. Trends Cell Biol. 5:1995;283-286.
170. McNally F. J. Modulation of microtubule dynamics during the cell cycle. Curr. Opin. Cell Biol. 8:1996;23-29.
171. 2. J. Cell Biol. 135:1996;201-214.
172. Shiina N., Gotoh Y., Nishida E. A novel homo-oligomeric protein responsible for an MPF-dependent microtubule-severing activity. EMBO J. 11:1992;4723-4731.
173. Shiina N., Gotoh Y., Kubomura N., Iwamatsu A., Nishida E. Microtubule severing by elongation factor 1α Science. 266:1994;282-285.
174. McNally F. J., Vale R. D. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell. 75:1993;419-429.
175. McNally F. J., Okawa K., Iwamatsu A., Vale R. D. Katanin, the microtubule-severing ATPase, is concentrated at centrosomes. J. Cell Sci. 109:1996;561-567.
176. Hartman J. J., Mahr J., McNally K., Okawa K., Iwamatsu A., Thomas S., Cheesman S., Heuser J., Vale R. D., McNally F. J. Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell. 93:1998;277-287.
177. McNally F. J., Thomas S. Katanin is responsible for the M-phase microtubule-severing activity inXenopus. Mol. Biol. Cell. 9:1998;1847-1861.
178. cdc2. Cell. 60:1990;151-165.
179. Verde F., Labbé J.-C., Dorée M., Karsenti E. Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts ofXenopus. Nature. 343:1990;233-238.
180. Verde F., Dogterom M., Stelzer E., Karsenti E., Leibler S. Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases inXenopus. J. Cell Biol. 118:1992;1097-1108.
181. cdc2. J. Cell Biol. 128:1995;849-862.
182. Wang X. M., Peloquin J. G., Zhai Y., Bulinski J. C., Borisy G. G. Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level. J. Cell Biol. 132:1996;345-357.
183. Illenberger S., Drewes G., Trincczek B., Biernat J., Meyer H. E., Olmsted J. B., Mandelkow E.-M., Mandelkow E. Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. J. Biol. Chem. 271:1996;10834-10843.
184. Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:1997;297-308.
185. Moskalewski S., Thyberg J. Disorganization and reorganization of the Golgi complex and the lysosomal system in association with mitosis. J. Submicrosc. Cytol. Pathol. 22:1990;159-171.
186. 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.
187. Misteli T., Warren G. Mitotic disassembly of the Golgi apparatus in vivo. J. Cell Sci. 108:1995;2715-2727.
188. Allan V. J., Vale R. D. Cell cycle control of microtubule-based membrane transport and tubule formation in vitro. J. Cell Biol. 113:1991;347-359.
189. Niclas J., Allan V. J., Vale R. D. Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J. Cell Biol. 133:1996;585-593.
190. Yang L., Guan T., Gerace L. Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis. J. Cell Biol. 137:1997;1199-1210.
191. 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.
192. Lucocq J. M., Warren G. Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J. 6:1987;3239-3246.
193. Shima D. T., Haldar K., Pepperkok R., Watson R., Warren G. Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 137:1997;1211-1228.
194. Shima D. T., Cabrera-Poch N., Pepperkok R., Warren G. An ordered inheritance strategy for the Golgi apparatus: Visualization of mitotic disassembly reveals a role for the mitotic spindle. J. Cell Biol. 141:1998;955-966.
195. Jesch S. A., Linstedt A. D. The Golgi and endoplasmic reticulum remain independent during mitosis in HeLa cells. Mol. Biol. Cell. 9:1998;623-635.
196. Warren G., Featherstone C., Griffiths G., Burke B. Newly synthesized G protein of vesicular stomatitis virus is not transported to the cell surface during mitosis. J. Cell Biol. 97:1983;1623-1628.
197. Featherstone C., Griffiths G., Warren G. Newly synthesized G protein of vesicular stomatitis virus is not transported to the Golgi complex in mitotic cells. J. Cell Biol. 101:1985;2036-2046.
198. Kreiner T., Moore H. P. H. Membrane traffic between secretory compartments is differentially affected during mitosis. Cell Regul. 1:1990;415-424.
199. Kobayashi T., Pagano R. E. Lipid transport during mitosis. Alternative pathways for delivery of newly synthesized lipids to the cell surface. J. Biol. Chem. 264:1989;5966-5973.
200. Collins R. N., Warren G. Sphingolipid transport in mitotic HeLa cells. J. Biol. Chem. 267:1992;24906-24911.
201. Misteli T., Warren G. COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 125:1994;269-282.
202. Misteli T., Warren G. A role for tubular networks and a COP I-independent pathway in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 130:1995;1027-1039.
203. Sönnichsen B., Watson R., Clausen H., Misteli T., Warren G. Sorting by COP I-coated vesicles under interphase and mitotic conditions. J. Cell Biol. 134:1996;1411-1425.
204. Stuart R. A., Mackay D., Adamczewski J., Warren G. Inhibition of intra-Golgi transport in vitro by mitotic kinase. J. Biol. Chem. 268:1993;4050-4054.
205. Levine T. P., Rabouille C., Kieckbusch R. H., Warren G. Binding of the
206. Jackman M., Firth M., Pines J. Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO J. 14:1995;1646-1654.
207. Acharya U., Mallabiabarrena A., Acharya J. K., Malhotra V. Signaling via mitogen-activated protein kinase kinase (MEK1) is required for Golgi fragmentation during mitosis. Cell. 92:1998;183-192.
208. Berlin R. D., Oliver J. M., Walter R. J. Surface functions during mitosis. I. Phagocytosis, pinocytosis and mobility of surface-bound ConA. Cell. 15:1978;327-341.
209. Berlin R. D., Oliver J. M. Surface functions during mitosis. II. Quantitation of pinocytosis and kinetic characterization of the mitotic cycle with a new fluorescence technique. J. Cell Biol. 85:1980;660-671.
210. Warren G., Davoust J., Cockcroft A. Recycling of transferrin receptors in A431 cells is inhibited during mitosis. EMBO J. 3:1984;2217-2225.
211. Sager P. R., Brown P. A., Berlin R. D. Analysis of transferrin recycling in mitotic and interphase HeLa cells by quantitative fluorescence microscopy. Cell. 39:1984;275-282.
212. Pypaert M., Lucocq J. M., Warren G. Coated pits in interphase and mitotic A431 cells. Eur. J. Cell Biol. 45:1987;23-29.
213. Pypaert M., Mundy D., Souter E., Labbé J.-C., Warren G. Mitotic cytosol inhibits invagination of coated pits in broken mitotic cells. J. Cell Biol. 114:1991;1159-1166.
214. Tuomikoski T., Felix M.-A., Dorée M., Gruenberg J. Inhibition of endocytic vesicle fusion in vitro by the cell-cycle control protein kinase cdc2. Nature. 342:1989;942-945.
215. Woodman P. G., Mundy D. I., Cohen P., Warren G. Cell-free fusion of endocytic vesicles is regulated by phosphorylation. J. Cell Biol. 116:1992;331-338.
216. Woodman P. G., Adamczewski J. P., Hunt T., Warren G. In vitro fusion of endocytic vesicles is inhibited by cyclin A-cdc2 kinase. Mol. Biol. Cell. 4:1993;541-553.
217. King R. W., Deshaies R. J., Peters J.-M., Kirschner M. W. How proteolysis drives the cell cycle. Science. 274:1996;1652-1659.
218. Pagano M. Cell cycle regulation by the ubiquitin pathway. FASEB J. 11:1997;1067-1075.
219. Nagata-Kuno K., Hino Y., Nanri H., Shibata Y., Minakami S. Fragmentation and re-formation of mitotic Golgi apparatus detected by a centrifugal method. Exp. Cell Res. 191:1990;273-277.
220. 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.
221. 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.
222. Rabouille C., Misteli T., Watson R., Warren G. Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J. Cell Biol. 129:1995;605-618.
223. Rabouille C., Levine T. P., Peters J.-M., Warren G. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell. 82:1995;905-914.
224. Kondo H., Rabouille C., Newman R., Levine T. P., Pappin D., Freemont P., Warren G. p47 is a cofactor for p97-mediated membrane fusion. Nature. 388:1997;75-78.
225. Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G. Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell. 92:1998;603-610.
226. 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.
227. Mack G., Rattner J. B. Centrosome repositioning immediately following karyokinesis and prior to cytokinesis. Cell Motil. Cytoskel. 26:1993;239-247.
228. 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.
229. Thyberg J., Sierakowska H., Edström J.-E., Burvall K., Pigon A. Mitochondrial distribution and ATP levels inChironomus. Dev. Biol. 90:1982;31-42.
230. Stanley H., Botas J., Malhotra V. The mechanism of Golgi segregation during mitosis is cell type-specific. Proc. Natl. Acad. Sci. USA. 94:1997;14467-14470.
231. Dupree P., Sherrier D. J. The plant Golgi apparatus. Biochim. Biophys. Acta. 1404:1998;259-270.
232. Ayscough K., Hajibagheri N. M. A., Watson R., Warren G. Stacking of Golgi cisternae inSchizosaccharomyces pombe. J. Cell Sci. 106:1993;1227-1237.
233. Preuss D., Mulholland J., Franzusoff A., Segev N., Botstein D. Characterization of theSaccharomyces. Mol. Biol. Cell. 3:1992;789-803.
234. Rambourg A., Gachet E., Clermont Y., Képès F. Modifications of the Golgi apparatus inSaccharomyces cerevisiae. Anat. Rec. 246:1996;162-168.