Regulation of membrane transport through the endocytic pathway by rabGTPases

References

• Advani, R. J., Bae, H. R., Bock, J. B., Chao, D. S., Doung, Y. C., Prekeris, R., Yoo, J. S., and Scheller, R. H., 1998, Seven novel mammalian SNARE proteins localize to distinct membrane compartments. Journal of Biological Chemistry, 273, 10317–10324.
   PubMed Web of Science ®Google Scholar
• Alexandrov, K., Horiuchi, H., Steele-Mortimer, O., Seabra, M., and Zerial, M., 1994, Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO Journal, 13, 5262–5273.
   PubMed Web of Science ®Google Scholar
• Andres, D. A., Seabra, M., Brown, M., Armstrong, S. A., Smeland, T. E., Cremers, F. P. M., and Goldstein, J. L., 1993, cDNA cloning of component A of rab geranylgeranyl transferase and demonstra-tion of its role as a rab escort protein. Cell, 73, 1091–1100.
   PubMed Web of Science ®Google Scholar
• Aridor, M., and Balch, W. E., 1996, Membrane fusion: timing is everything. Nature, 383, 220–221.
   PubMed Web of Science ®Google Scholar
• Ayad, N., Hull, M., and Mellman, I., 1997, Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosomes. EMBO Journal, 16, 4497–4507.
   PubMed Web of Science ®Google Scholar
• Bailly, E., Touchot, N., Zahraoui, A., Goud, B., and Bornens, M., 1991, p34cdc 2 protein kinase phosphorylates two small GTP-binding proteins of the rab family. Nature, 350, 715–718.
   PubMed Web of Science ®Google Scholar
• Barbieri, M. A., Li, G., Colombo, M. I., and Stahl, P. D., 1994, Rab5, an early acting endosomal GTPase supports in vitro endosome fusion without GTP hydrolysis. Journal of Biological Chemistry, 269, 18720–18722.
   PubMed Web of Science ®Google Scholar
• Bottger, G., Nagelkerken, B., and van der Sluijs, P., 1996, Rab4 and rab7 define distinct endocytic compartments. Journal of Biological Chemistry, 271, 29191–29197.
   PubMed Web of Science ®Google Scholar
• Bucci, C., Lütcke, A., Mortimer, O. S., Olkkonen, V. M., Dupree, P., Chiariello, M., Bruni, C. B., Simons, K., and Zerial, M., 1995, Co-operative regulation of endocytosis by three rab5 isoforms. FEBS Letters, 366, 65–71.
   PubMed Web of Science ®Google Scholar
• Bucci, C., Parton, R., Mather, I., Stunnenberg, H., Simons, K., and Zerial, M., 1992, The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell, 70, 715–728.
   PubMed Web of Science ®Google Scholar
• Bucci, C., Wandinger-Ness, A., Lütcke, A., Chiarello, M., Bruni, C. B., and Zerial, M., 1994, Rab5a is a common component of the apical and basolateral endocytic machinery in polarized epithelial cells. Proceedings of the National Academy of Sciences (USA), 91, 5061–5065.
   PubMed Web of Science ®Google Scholar
• Chavrier, P., Parton, R. G., Hauri, H. P., Simons, K., and Zerial, M., 1990, Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell, 62, 317–329.
   PubMed Web of Science ®Google Scholar
• Chavrier, P., van der Sluijs, P., Mishal, Z., Nagelkerken, B., and Gorvel, J. P., 1997, Early endosome dynamics characterized by flow cytometry. Cytometry, 29, 41–49.
   PubMedGoogle Scholar
• Cosulich, S. C., Horiuchi, H., Zerial, M., Clarke, P. R., and Woodman, P. G., 1997, Cleavage of rabaptin-5 blocks endosome fusion during apoptosis. EMBO Journal, 16, 6182–6191.
   PubMed Web of Science ®Google Scholar
• Daro, E., van der Sluijs, P., Galli, T., and Mellman, I., 1996, Rab4 and cellubrevin define different early endosome populations on the pathway of transferrin receptor recycling. Proceedings of the National Academy of Sciences (USA), 93, 9559–9564.
   PubMed Web of Science ®Google Scholar
• de Hoop, M., Huber, L. A., Stenmark, H., Williamson, E., Zerial, M., Parton, R. G., and Dotti, C. G., 1994, The involvement of the small GTP-binding protein rab5a in neuronal endocytosis. Neuron, 13, 11–22.
   PubMedGoogle Scholar
• Diaz, E., Schimmoller, F., and Pfeffer, S. R., A novel rab9 effector required for endosome to TGN transport. Journal of Cell Biology, 138, 283–290.
   Google Scholar
• Dirac-Svejstrup, A. B., Sumizawa, T., and Pfeffer, S. R., 1997, Identification of a GDI displacement factor that releases endoso-mal Rab GTPases from Rab-GDI. EMBO Journal, 16, 465–472.
   PubMed Web of Science ®Google Scholar
• Dotti, C. G., and Simons, K., 1990, Polarized sorting of viral glycoproteins to the axonal and dendrites of hipocampal neurons in culture. Cell, 62, 63–72.
   PubMed Web of Science ®Google Scholar
• Feng, Y., Press, B., and Wandinger Ness, A., 1995, Rab7: an important regulator of late endocytic membrane traffic. Journal of Cell Biology, 131, 1435–1452.
   PubMed Web of Science ®Google Scholar
• Galli, T., Chilcote, T., Mundigl, O., Binz, T., Niemann, H., and DeCamilli, P., 1994, TTX mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor containing vesicles in CHO cells. Journal of Cell Biology, 125, 1015–1024.
   PubMed Web of Science ®Google Scholar
• Gaullier, J. M., Simonsen, A., D’Arrigo, A., Bremnes, B., Stenmark, H., and Aasland, R., FYVE fingers bind PtdIns(3)P. Nature, 394, 432–433.
   Google Scholar
• Gorvel, J. P., Chavrier, P., Zerial, M., and Gruenberg, J., 1991, rab5 controls early endosome fusion in vitro. Cell, 64, 915–925.
   PubMed Web of Science ®Google Scholar
• Gournier, H., Stenmark, H., Rybin, V., Lippe, R., and Zerial, M., 1998, Two distinct effectors of the small GTPase rab5 cooperate in endocytic membrane fusion. EMBO Journal, 17, 1930-1940.
   PubMed Web of Science ®Google Scholar
• Horazdovski, B. F., Busch, G. R., and Emr, S., 1994, VPS21 encodes a rab5-like GTP binding protein that is required for the sorting of yeast vacuolar proteins. EMBO Journal, 13, 1297-1309.
   Google Scholar
• Horiuchi, H., Lippe, R., McBride, H. M., Rubino, M., Woodman, P., Stenmark, H., Rybin, V., Wilm, M., Ashman, K., Mann, M., and Zerial, M., 1997, A novel rab5 GDP/GTP exchange factor complexed to rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell, 90, 1149–1159.
   PubMed Web of Science ®Google Scholar
• Hunziker, W., and Peters, P. J., 1998, Rab17 localizes to recycling endosomes and regulates receptor mediated transcytosis in epithelialcells. Journalof Biological Chemistry, 273, 15734-15741.
   Google Scholar
• Jones, A. T., Mills, I. G., Scheidig, A. J., Alexandrov, K., and Clague, M. J., 1998, Inhibition of endosome fusion by wortmannin persists in the presence of activated rab5. Molecular Biology of the Cell, 9, 323–332.
   PubMed Web of Science ®Google Scholar
• Kornfeld, S., and Mellman, I., 1989, The biogenesis of lysosomes. Annual Review of Cell Biology, 5, 483–525.
   PubMedGoogle Scholar
• Kruger, S. B., Stenmark, H., Dusterhoft, A., Philippsen, P., Yoo, J. S., Gallwitz, D., and Zerial, M., 1994, Role of three rab5-like GTPases, Ypt51p, Ypt52p, and Ypt53p, in the endocytic and vacuolar protein sorting pathways of yeast. Journal of Cell Biology, 125, 283–298.
   PubMed Web of Science ®Google Scholar
• Lombardi, D., Soldati, T., Riederer, M., Zerial, M., and Pfeffer, S., 1993, Rab 9 functions in transport between late endosomes and the trans Golgi network. EMBO Journal, 12, 677–682.
   PubMed Web of Science ®Google Scholar
• Lowe, M., Nakamura, N., and Warren, G., 1998, Golgi division and membrane traffic. Trends in Cell Biology, 8, 40–44.
   PubMed Web of Science ®Google Scholar
• Lütcke, A., Jansson, S., Parton, R., Chavrier, P., Valencia, A., Huber, L., Lehtonen, E., and Zerial, M., 1993, Rab17, a novel small GTPase, is specific for epithelial cells and is induced during cell polarization. Journal of Cell Biology, 121, 553–564.
   PubMed Web of Science ®Google Scholar
• McLaughlan, H., Newell, J., Morrice, N., Osborne, A., West, M., and Smythe, E., 1998, A novel role for rab-GDI in ligand sequestration into clathrin-coated pits. Current Biology, 8, 34–45.
   PubMed Web of Science ®Google Scholar
• McMahon, H. T., Ushkayov, Y. A., Edelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R., and Südhof, T. C., 1993, Cellubrevin is a ubiquitous ttx substrate homologous to a putative synaptic vesicle fusion protein. Nature, 364, 346–349.
   PubMed Web of Science ®Google Scholar
• Mellman, I. and Simons, K., 1992, The Golgi complex: in vitro veritas? Cell, 68, 829–840.
   PubMed Web of Science ®Google Scholar
• Nagelkerken, B., Mohrmann, K., Gerez, L., van Raak, M., Leijendekker, R. L., and van der Sluijs, P., 1997, A novel epitope tag for the detection of rab GTPases. Electrophoresis, 18, 2694–2698.
   PubMed Web of Science ®Google Scholar
• Novick, P. and Zerial, M., 1997, The diversity of rab proteins in vesicle transport. Current Opinion in Cell Biology, 9, 496–504.
   PubMed Web of Science ®Google Scholar
• Olkkonen, V., and Stenmark, H., 1997, Role of rabGTPases in membrane traffic. International Reviews of Cytology, 126, 1–85.
   Google Scholar
• Olkkonen, V. M., Dupree, P., Killisch, I., Lütcke, A., Zerial, M., and Simons, K., 1993, Molecular cloning and subcellular localization of three GTP binding proteins of the rab subfamily. Journal of Cell Science, 106, 1249–1261.
   PubMed Web of Science ®Google Scholar
• Press, B., Feng, Y., Hoflack, B., and Wandinger-Ness, A., 1998, Mutant rab7 causes the accumulation of cathepsin D and cation independent mannose 6-phosphate receptor in an early endocytic compartment. Journal of Cell Biology, 140, 1075–1089.
   PubMed Web of Science ®Google Scholar
• Ren, M., Xu, G., Zeng, J., Chiarandini, C. L., Adesnik, M., and Sabatini, D. D., 1998, Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from recycling endo-somes. Proceedings of the National Academy of Sciences (USA), 95, 6187–6192.
   PubMed Web of Science ®Google Scholar
• Riederer, M., Soldati, T., Shapiro, A. D., Lin, J., and Pfeffer, S. R., 1994, Lysosome biogenesis requires rab9 function and receptor recycling from endosomes to the trans Golgi network. Journal of Cell Biology, 125, 573–582.
   PubMed Web of Science ®Google Scholar
• Rybin, V., Ullrich, O., Rubino, M., Alexandrov, K., Simon, I., Seabra, M., Goody, R., and Zerial, M., 1996, GTPase activity of rab5 acts as a timer for endocytic membrane fusion. Nature, 383, 266–269.
   PubMed Web of Science ®Google Scholar
• Salminen, A. and Novick, P. J., 1987, A ras-like protein is required for a post Golgi event in yeast secretion. Cell, 49, 527–538.
   PubMed Web of Science ®Google Scholar
• Segev, N., Mullholland, J. and Botstein, D., 1988, The yeast GTP-binding YPT1 protein and a mammalian counterpart are asso-ciated with the secretion machinery. Cell, 52, 915–924.
   PubMed Web of Science ®Google Scholar
• Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J. M., Brech, A., Callaghan, J., Toh, B. H., Murphy, C., Zerial, M., and Stenmark, H., 1998, EEA1 links PI(3)K function to rab5 regulation of endosome fusion. Nature, 394, 494–498.
   PubMed Web of Science ®Google Scholar
• Stenmark, H., Aasland, R., Toh, B. H., and D’Arrigo, A., 1996, Endosomal localization of the autoantigen EEA1 is mediated by a Zinc-binding FYVE finger. Journal of Biological Chemistry, 271, 24048–24054.
   PubMed Web of Science ®Google Scholar
• Stenmark, H., Parton, R., Steele-Mortimer, O., Lütcke, A., Gruen-berg, J., and Zerial, M., 1994, Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis. EMBO Journal, 13, 1287–1296.
   PubMed Web of Science ®Google Scholar
• Stenmark, H., Vitale, G., Ullrich, O., and Zerial, M., 1995, Rabaptin-5 is a direct effector of the small GTPase rab5 in endocytic membrane fusion. Cell, 83, 423–432.
   PubMed Web of Science ®Google Scholar
• Tang, B. L., Tan, A. E. H., Lim, L. K., Lee, S. S., Low, D. Y. H. and Hong, W., 1998, Syntaxin 12, a member of the sdyntaxin family localized to the endosome. Journal of Biological Chemistry, 273, 6944–6950.
   PubMed Web of Science ®Google Scholar
• Ullrich, O., Horiuchi, H., Bucci, C., and Zerial, M., 1994, Membrane association of rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange. Nature, 368, 157–160.
   PubMed Web of Science ®Google Scholar
• Ullrich, O., Reinsch, O., Urbe, S., Zerial, M., and Parton, R., 1996, Rab11 regulates recycling through the pericentriolar recycling endosome. Journal of Cell Biology, 135, 913–924.
   PubMed Web of Science ®Google Scholar
• Ullrich, O., Stenmark, H., Alexandrov, K., Huber, L., Kaibuchi, K., Sasaki, T., Takai, Y., and Zerial, M., 1993, Rab GDI as a general regulator for the membrane association of rab proteins. Journal of Biological Chemistry, 268, 18143–18150.
   PubMed Web of Science ®Google Scholar
• Urbe, S., Huber, L. A., Zerial, M., Tooze, S. A., and Parton, R. G., 1993, Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells. FEBS Letters, 334, 175–182.
   PubMed Web of Science ®Google Scholar
• Valentijn, J. A., Civita, D. Q., Gumkowski, F. D., and Jamieson, J., 1997, Rab4 associates with the actin terminal web in developing rat pancreatic acinar cells. European Journal of Cell Biology, 72, 1–8.
   PubMed Web of Science ®Google Scholar
• van der Sluijs, P., Hull, M., Huber, L. A., Male, P., Goud, B., and Mellman, I., 1992b, Reversible phosphorylation-dephosphoryla-tion determines the localization of rab4 during the cell cycle. EMBO Journal, 11, 4379–4389.
   PubMed Web of Science ®Google Scholar
• van der Sluijs, P., Hull, M., Webster, P., Goud, B., and Mellman, I., 1992a, The small GTP binding protein rab4 controls an early sorting event on the endocytic pathway. Cell, 70, 729–740.
   PubMed Web of Science ®Google Scholar
• van der Sluijs, P., Hull, M., Zahraoui, A., Tavitian, A., Goud, B., and Mellman, I., 1991, The small GTP binding protein rab4 is associated with early endosomes. Proceedings of the National Acadamy of Sciences (USA), 88, 6313–6317.
   PubMed Web of Science ®Google Scholar
• van Slegtenhorst, M., de Hoogt, R., Hermans, C., Nellist, M., Janssen, B., Verhoef, S., Lindhout, D., van den Ouweland, A., Halley, D., Young, J., Burley, M., Jeremiah, S., Woodward, K., Nahmias, J., Fox, M., Ekong, R., Osborne, J., Wolfe, J., Povey, S., Snell, R. G., Cheadle, J. P., Jones, A. C., Tachataki, M., Ravine, D., Sampson, J. R., Reeve, M. P., Richardson, P., Wilmer, F., Munro, C., Hawkins, T. L., Sepp, T., Ali, J. B. M., Ward, S., Green, A. J., Yates, J. R. W., Kwiatkowska, J., Henske, E. P., Short, M. P., Haines, J. H., Jozwiak, S., and Kwiatkowski, D. J., 1997, Identification of the tuberous sclerosis gene TSC1 on chromo-some 9q34. Science, 277, 805–808.
   PubMed Web of Science ®Google Scholar
• van Slegtenhorst, M., Nellist, M., Nagelkerken, B., Cheadle, J., Snell, R., van den Ouweland, A., Reuser, A., Sampson, J., Halley, D., and van der Sluijs, P., 1998, Interactions between hamartin and tuberin, the TSC1 and TSC2 gene products. Human Molecular Genetics, 7, 1053–1057.
   PubMed Web of Science ®Google Scholar
• Vitale, G., Rybin, V., Christoforidis, S., Thornqvist, P. O., McCaffrey, M., Stenmark, H., and Zerial, M., 1998, Distinct rab-binding domains mediate the interaction of rabaptin-5 with GTP-bound rab4 and rab5. EMBO Journal, 17, 1941-1951.
   PubMed Web of Science ®Google Scholar
• Warren, G., 1993, Membrane partitioning during cell division. Annual Review of Biochemistry, 62, 323–48.
   PubMed Web of Science ®Google Scholar
• Wichmann, H., Hengst, L., and Gallwitz, D., 1992, Endocytosis in yeast: evidence for the involvement of a small GTP binding protein (Ypt7p). Cell, 71, 1131–1142.
   PubMed Web of Science ®Google Scholar
• Wilson, A. L., Erdman, R. A., and Maltese, W. A., 1996, Association of rab1b with GDI is required for recycling but not initial membrane targeting of the rab protein. Journal of Biological Chemistry, 271, 10932–10940.
   PubMed Web of Science ®Google Scholar
• Wong, S. H., Xu, Y., Zhang, T. and Hong, W., 1998a, Syntaxin 7, a novel syntaxin member associated with the early endosomal compartment. Journal of Biological Chemistry, 273, 375–380.
   PubMed Web of Science ®Google Scholar
• Wong, S. H., Zhang, T., Xu, Y., Subramaniam, V. N., Griffiths, G. and Hong, W., 1998b, Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with early endosome. Molecular Biology of the Cell, 9, 1549–1563.
   PubMed Web of Science ®Google Scholar
• Xiao, G. H., Shoarinejad, F., Jin, F., Golemis, E., and Yeung, R. S., 1997, The tuberous sclerosis 2 gene product, tuberin, functions as a rab5 GTPase activating protein (GAP) in modulating endocy-tosis. Journal of Biological Chemistry, 272, 6097–6100.
   PubMed Web of Science ®Google Scholar
• Yamashiro, D. J., Tycko, B., Fluss, S. R. and Maxfield, F. R., 1984, Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway. Cell, 37, 789–800.
   PubMed Web of Science ®Google Scholar
• Zacchi, P., Stenmark, H., Parton, R. G., Orioli, D., Lim, F., Giner, A., Zerial, M., and Murphy, C., 1998, Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells. Journal of Cell Biology, 140, 1039–1053.
   PubMed Web of Science ®Google Scholar