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Volumn 11, Issue 1, 2000, Pages 287-304

Selective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac1

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MUTANT PROTEIN;

EID: 0033973134     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.287     Document Type: Article
Times cited : (57)

References (66)
  • 1
    • 0030015626 scopus 로고    scopus 로고
    • Rhodependent membrane folding causes Shigella entry into epithelial cells
    • Adam, T., Giry, M., Boquet, P., and Sansonetti, P. (1996). Rhodependent membrane folding causes Shigella entry into epithelial cells. EMBO J. 15, 3315-3321.
    • (1996) EMBO J. , vol.15 , pp. 3315-3321
    • Adam, T.1    Giry, M.2    Boquet, P.3    Sansonetti, P.4
  • 3
    • 0031452943 scopus 로고    scopus 로고
    • Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31
    • Annaert, W.G., Becker, B., Kistner, U., Reth, M., and Jahn, R. (1997). Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31. J. Cell Biol. 139, 1397-1410.
    • (1997) J. Cell Biol. , vol.139 , pp. 1397-1410
    • Annaert, W.G.1    Becker, B.2    Kistner, U.3    Reth, M.4    Jahn, R.5
  • 4
    • 0027213833 scopus 로고
    • Brefeldin-A inhibits the delivery of the polymeric immunoglobulin receptor to the basolateral surface of MDCK cells
    • Apodaca, G., Aroeti, B., Tang, K., and Mostov, K.E. (1993). Brefeldin-A inhibits the delivery of the polymeric immunoglobulin receptor to the basolateral surface of MDCK cells. J. Biol. Chem. 268, 20380-20385.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20380-20385
    • Apodaca, G.1    Aroeti, B.2    Tang, K.3    Mostov, K.E.4
  • 5
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., Katz, L.A., and Mostov, K.E. (1994). Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125, 67-86.
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 6
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti, B., Kosen, P.A., Kuntz, I.D., Cohen, F.E., and Mostov, K.E. (1993). Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. J. Cell Biol. 123, 1149-1160.
    • (1993) J. Cell Biol. , vol.123 , pp. 1149-1160
    • Aroeti, B.1    Kosen, P.A.2    Kuntz, I.D.3    Cohen, F.E.4    Mostov, K.E.5
  • 7
    • 0028342843 scopus 로고
    • Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids
    • Aroeti, B., and Mostov, K.E. (1994). Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids. EMBO J. 13, 2297-2304.
    • (1994) EMBO J. , vol.13 , pp. 2297-2304
    • Aroeti, B.1    Mostov, K.E.2
  • 8
    • 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., and Simons, K. (1989). The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109, 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
  • 9
    • 0028009419 scopus 로고
    • Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome
    • Barroso, M., and Sztul, E. (1994). Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome. J. Cell Biol. 124, 83-100.
    • (1994) J. Cell Biol. , vol.124 , pp. 83-100
    • Barroso, M.1    Sztul, E.2
  • 10
    • 0030614352 scopus 로고    scopus 로고
    • 2-terminal deletion of beta-catenin results in stable colocalization of mutant beta-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion
    • 2-terminal deletion of beta-catenin results in stable colocalization of mutant beta-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion. J. Cell Biol. 136, 693-706.
    • (1997) J. Cell Biol. , vol.136 , pp. 693-706
    • Barth, A.I.1    Pollack, A.L.2    Altschuler, Y.3    Mostov, K.E.4    Nelson, W.J.5
  • 12
    • 0025025877 scopus 로고
    • Deletions in the cytoplasmic domain of the polymeric immunoglobulin receptor differentially affect endocytotic rate and postendocytotic traffic
    • Breitfeld, P.P., Casanova, J.E., McKinnon, W.C., and Mostov, K.E. (1990). Deletions in the cytoplasmic domain of the polymeric immunoglobulin receptor differentially affect endocytotic rate and postendocytotic traffic. J. Biol. Chem. 265, 13750-13757.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13750-13757
    • Breitfeld, P.P.1    Casanova, J.E.2    McKinnon, W.C.3    Mostov, K.E.4
  • 13
    • 0024374567 scopus 로고
    • Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby canine kidney cells
    • Breitfeld, P.P., Harris, J.M., and Mostov, K.M. (1989b). Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby canine kidney cells. J. Cell Biol. 109, 475-486.
    • (1989) J. Cell Biol. , vol.109 , pp. 475-486
    • Breitfeld, P.P.1    Harris, J.M.2    Mostov, K.M.3
  • 14
    • 0031696158 scopus 로고    scopus 로고
    • Induction of exocytosis from permeabilized mast cells by the guanosine triphosphatases Rac and Cdc42
    • Brown, A.M., O'Sullivan, A.J., and Gomperts, B.D. (1998). Induction of exocytosis from permeabilized mast cells by the guanosine triphosphatases Rac and Cdc42. Mol. Biol. Cell 9, 1053-1063.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1053-1063
    • Brown, A.M.1    O'Sullivan, A.J.2    Gomperts, B.D.3
  • 15
    • 0028267096 scopus 로고
    • Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells
    • Cardone, M.H., Smith, B.L., Song, W., Mochley-Rosen, D., and Mostov, K.E. (1994). Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells. J. Cell Biol. 124, 717-727.
    • (1994) J. Cell Biol. , vol.124 , pp. 717-727
    • Cardone, M.H.1    Smith, B.L.2    Song, W.3    Mochley-Rosen, D.4    Mostov, K.E.5
  • 16
    • 0025766194 scopus 로고
    • An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor
    • Casanova, J.E., Apodaca, G., and Mostov, K.E. (1991). An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor. Cell 66, 65-75.
    • (1991) Cell , vol.66 , pp. 65-75
    • Casanova, J.E.1    Apodaca, G.2    Mostov, K.E.3
  • 18
    • 0030448437 scopus 로고    scopus 로고
    • Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses
    • Chen, L-M., Hobbie, S., and Galán, J.E. (1996). Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses. Science 274, 2115-2118.
    • (1996) Science , vol.274 , pp. 2115-2118
    • Chen, L.-M.1    Hobbie, S.2    Galán, J.E.3
  • 19
    • 0029891129 scopus 로고    scopus 로고
    • Rho proteins are localized with different membrane compartments involved in vesicular trafficking in anterior pituitary cells
    • Cussac, D., Leblanc, P., L'Heritier, A., Bertoglio, J., Lang, P., Kordon, C., Enjalbert, A., and Saltarelli, D. (1996). Rho proteins are localized with different membrane compartments involved in vesicular trafficking in anterior pituitary cells. Mol. Cell. Endocrinol. 119, 195-206.
    • (1996) Mol. Cell. Endocrinol. , vol.119 , pp. 195-206
    • Cussac, D.1    Leblanc, P.2    L'Heritier, A.3    Bertoglio, J.4    Lang, P.5    Kordon, C.6    Enjalbert, A.7    Saltarelli, D.8
  • 20
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli, P., Emr, S.D., McPherson, P.S., and Novick, P. (1996). Phosphoinositides as regulators in membrane traffic. Science 271, 1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 21
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D.G., and Nelson, W.J. (1996). Origins of cell polarity. Cell 84, 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 22
    • 0023039366 scopus 로고
    • Transferrin receptor polarity and recycling accuracy in "tight" and "leaky" strains of Madin-Darby canine kidney cells
    • Fuller, S.D., and Simons, K. (1986). Transferrin receptor polarity and recycling accuracy in "tight" and "leaky" strains of Madin-Darby canine kidney cells. J. Cell Biol. 103, 1767-1779.
    • (1986) J. Cell Biol. , vol.103 , pp. 1767-1779
    • Fuller, S.D.1    Simons, K.2
  • 24
    • 0031891269 scopus 로고    scopus 로고
    • Apionuclear organization of microtubules does not specify protein delivery from the trans-Golgi network to different membrane domains in polarized epithelial cells
    • Grindstaff, K.K., Bacallao, R.L., and Nelson, W.J. (1998a). Apionuclear organization of microtubules does not specify protein delivery from the trans-Golgi network to different membrane domains in polarized epithelial cells. Mol. Biol. Cell 9, 685-699.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 685-699
    • Grindstaff, K.K.1    Bacallao, R.L.2    Nelson, W.J.3
  • 25
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff, K.K., Yeaman, C., Anandasabapathy, N., Hsu, S.C., Rodriquez-Boulan, E., Scheller, R.H., and Nelson, W.J. (1998b). Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93, 731-740.
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.C.4    Rodriquez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 26
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 27
    • 0028167863 scopus 로고
    • Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A
    • Hansen, S.H., and Casanova, J.E. (1994). Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A. J. Cell Biol. 126, 677-688.
    • (1994) J. Cell Biol. , vol.126 , pp. 677-688
    • Hansen, S.H.1    Casanova, J.E.2
  • 28
    • 0028862325 scopus 로고
    • Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells
    • Hansen, S.H., Olsson, A., and Casanova, J.E. (1995). Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells. J. Biol. Chem. 270, 28425-28432.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28425-28432
    • Hansen, S.H.1    Olsson, A.2    Casanova, J.E.3
  • 29
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity
    • Jou, T.-S., and Nelson, W.J. (1998). Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity. J. Cell Biol. 142, 85-100.
    • (1998) J. Cell Biol. , vol.142 , pp. 85-100
    • Jou, T.-S.1    Nelson, W.J.2
  • 30
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases
    • Jou, T.-S., Schneeberger, E.E., and Nelson, W.J. (1998). Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases. J. Cell Biol. 142, 101-115.
    • (1998) J. Cell Biol. , vol.142 , pp. 101-115
    • Jou, T.-S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 31
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A., and Lim, L. (1995). The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15, 1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 32
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A., and Mellman, I (1999). Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1, 8-13.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 33
  • 35
    • 0030929850 scopus 로고    scopus 로고
    • Uncoupling of membrane ruffling and pinocytosis during ras signal transduction
    • Li, G., D'Souza-Schorey, C., Barbieri, M.A., Cooper, J.A., and Stahl, P.D. (1997). Uncoupling of membrane ruffling and pinocytosis during ras signal transduction. J. Biol. Chem. 272, 10337-10340.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10337-10340
    • Li, G.1    D'Souza-Schorey, C.2    Barbieri, M.A.3    Cooper, J.A.4    Stahl, P.D.5
  • 36
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Lindstedt, A.D., and Hauri, H.P. (1993). Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Lindstedt, A.D.1    Hauri, H.P.2
  • 37
    • 0030250164 scopus 로고    scopus 로고
    • Phospholipase D: Role in signal transduction and membrane traffic
    • Liscovitch, M. (1996). Phospholipase D: role in signal transduction and membrane traffic. J. Lipid Mediators Cell Signal. 14, 215-221.
    • (1996) J. Lipid Mediators Cell Signal. , vol.14 , pp. 215-221
    • Liscovitch, M.1
  • 38
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and Cantley, L.C. (1995). Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell 81, 659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 40
    • 0029803812 scopus 로고    scopus 로고
    • Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells
    • Mariot, P., O'Sullivan, A.J., Brown, A.M., and Tatham, P.E.R. (1996). Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells. EMBO J. 15, 6476-6482.
    • (1996) EMBO J. , vol.15 , pp. 6476-6482
    • Mariot, P.1    O'Sullivan, A.J.2    Brown, A.M.3    Tatham, P.E.R.4
  • 41
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of furin proprotein convertase: Localization to the TGN and recycling from the cell surface
    • Molloy, S.S., Thomas, L., VanSlyke, J.K., Stenberg, P.E., and Thomas, G. (1994). Intracellular trafficking and activation of furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO J. 13, 18-33.
    • (1994) EMBO J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 42
    • 0029240448 scopus 로고
    • Regulation of protein traffic in polarized epithelial cells
    • Mostov, K.E., and Cardone, M.H. (1995). Regulation of protein traffic in polarized epithelial cells. BioEssays 17, 129-138.
    • (1995) BioEssays , vol.17 , pp. 129-138
    • Mostov, K.E.1    Cardone, M.H.2
  • 44
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes
    • Nabi, I.R., Le Bivic, A., Fambrough, D., and Rodriguez-Boulan, E. (1991). An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115, 1573-1584.
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Le Bivic, A.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 45
    • 0028070036 scopus 로고
    • Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins
    • Norman, J.C., Price, L.S., Ridley, A.J., Hall, A., and Koffer, A. (1994). Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J. Cell Biol. 126, 1005-1015.
    • (1994) J. Cell Biol. , vol.126 , pp. 1005-1015
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Hall, A.4    Koffer, A.5
  • 46
    • 0029809141 scopus 로고    scopus 로고
    • The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways
    • Norman, J.C., Price, L.S., Ridley, A.J., and Koffer, A. (1996). The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways. Mol. Biol. Cell 7, 1429-1442.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1429-1442
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Koffer, A.4
  • 47
    • 0029820888 scopus 로고    scopus 로고
    • Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism
    • Odorizzi, G., Pearse, A., Domingo, D., Trowbridge, I.S., and Hopkins, C.R. (1996). Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism. J. Cell Biol. 135, 139-152.
    • (1996) J. Cell Biol. , vol.135 , pp. 139-152
    • Odorizzi, G.1    Pearse, A.2    Domingo, D.3    Trowbridge, I.S.4    Hopkins, C.R.5
  • 48
    • 0029836564 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for the Rho GTPases: A role in human disease?
    • Olson, M.F. (1996). Guanine nucleotide exchange factors for the Rho GTPases: a role in human disease? J. Mol. Med. 74, 563-571.
    • (1996) J. Mol. Med. , vol.74 , pp. 563-571
    • Olson, M.F.1
  • 49
    • 0029876343 scopus 로고    scopus 로고
    • Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a rac/rhoGDI complex
    • O'Sullivan, A.J., Brown, A.M., Freeman, H.N., and Gomperts, B.D. (1996). Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a rac/rhoGDI complex. Mol. Biol. Cell 7, 397-408.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 397-408
    • O'Sullivan, A.J.1    Brown, A.M.2    Freeman, H.N.3    Gomperts, B.D.4
  • 50
    • 0024810856 scopus 로고
    • Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes
    • Parton, R.G., Prydz, K., Bomsel, M., Simons, K., and Griffiths, G. (1989). Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes. J. Cell Biol. 109, 3259-3272.
    • (1989) J. Cell Biol. , vol.109 , pp. 3259-3272
    • Parton, R.G.1    Prydz, K.2    Bomsel, M.3    Simons, K.4    Griffiths, G.5
  • 51
    • 0029139385 scopus 로고
    • The small GTPases Rac and Rho as regulators of secretion in mast cells
    • Price, L.S., Norman, J.C., Ridley, A.J., and Koffer, A. (1995). The small GTPases Rac and Rho as regulators of secretion in mast cells. Curr. Biol. 5, 68-73.
    • (1995) Curr. Biol. , vol.5 , pp. 68-73
    • Price, L.S.1    Norman, J.C.2    Ridley, A.J.3    Koffer, A.4
  • 52
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R.-G., Chen, J., Kirn, D., McCormick, F., and Symons, M. (1995a). An essential role for Rac in Ras transformation. Nature 374, 457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.-G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 54
    • 0032568657 scopus 로고    scopus 로고
    • Hydrolysis of GTP on Rab11 is required for direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes
    • Ren, M., Xu, G., Zeng, J., De Lemos-Chiarandini, C., Adesnik, M., and Sabatini, D.D. (1998). Hydrolysis of GTP on Rab11 is required for direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes. Proc. Natl. Acad. Sci. USA 95, 6187-6192.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6187-6192
    • Ren, M.1    Xu, G.2    Zeng, J.3    De Lemos-Chiarandini, C.4    Adesnik, M.5    Sabatini, D.D.6
  • 55
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 56
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Paterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 57
    • 0029097640 scopus 로고
    • Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes
    • Schmalzing, G., Richter, H.-P., Hansen, A., Schwarz, W., Just, I., and Aktories, K. (1995). Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes. J. Cell Biol. 130, 1319-1332.
    • (1995) J. Cell Biol. , vol.130 , pp. 1319-1332
    • Schmalzing, G.1    Richter, H.-P.2    Hansen, A.3    Schwarz, W.4    Just, I.5    Aktories, K.6
  • 59
    • 0025977370 scopus 로고
    • Multilayering and loss of apical polarity in MDCK cells transformed with viral K-ras
    • Schoenenberger, C.-A., Zuk, A., Kendall, D., and Matlin, K.S. (1991). Multilayering and loss of apical polarity in MDCK cells transformed with viral K-ras. J. Cell Biol. 112, 873-889.
    • (1991) J. Cell Biol. , vol.112 , pp. 873-889
    • Schoenenberger, C.-A.1    Zuk, A.2    Kendall, D.3    Matlin, K.S.4
  • 60
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff, D.R., Daro, E.A., Hull, M., and Mellman, I. (1999). The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145, 123-139.
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 61
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M., and Parton, R.G. (1996). Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 235, 913-924.
    • (1996) J. Cell Biol. , vol.235 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 62
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbé, 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 Lett. 334, 175-182.
    • (1993) FEBS Lett. , vol.334 , pp. 175-182
    • Urbé, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 63
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 64
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • Vojtek, A.B., and Cooper, J.A. (1995). Rho family members: activators of MAP kinase cascades. Cell 82, 527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 65
    • 0032493812 scopus 로고    scopus 로고
    • Increasing complexity of the ras signaling pathway
    • Vojtek, A.B., and Der, C.J. (1998). Increasing complexity of the ras signaling pathway. J. Biol. Chem. 273, 19925-19928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19925-19928
    • Vojtek, A.B.1    Der, C.J.2
  • 66
    • 0031052018 scopus 로고    scopus 로고
    • Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells
    • Watarai, M., Kamata, Y., Kozaki, S., and Sasakawa, C. (1997). Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells. J. Exp. Med. 285, 281-292.
    • (1997) J. Exp. Med. , vol.285 , pp. 281-292
    • Watarai, M.1    Kamata, Y.2    Kozaki, S.3    Sasakawa, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.