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Volumn 135, Issue 1, 1996, Pages 139-152

apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism

Author keywords

[No Author keywords available]

Indexed keywords

TRANSFERRIN RECEPTOR;

EID: 0029820888     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.1.139     Document Type: Article
Times cited : (130)

References (44)
  • 1
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., L.A. Katz, and K.E. Mostov. 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
  • 2
    • 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 K.E. Mostov. 1994. Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids. EMBO (Eur. Mol. Biol. Organ.) J. 13:2297-2304.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2297-2304
    • Aroeti, B.1    Mostov, K.E.2
  • 3
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti, B., P.A. Kosen, I.D. Kuntz, F.E., Cohen, and K.E. Mostov. 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
  • 4
    • 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 E.S. Sztul. 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.S.2
  • 5
    • 0027421873 scopus 로고
    • A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor
    • Bates, P., J.A.T. Young, and H.E. Varmus. 1993. A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor. Cell. 74:1043-1051.
    • (1993) Cell , vol.74 , pp. 1043-1051
    • Bates, P.1    Young, J.A.T.2    Varmus, H.E.3
  • 6
  • 7
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn, K.W., T.E. McGraw, and F.R. Maxfield. 1989. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J. Cell Biol. 109:3303-3314.
    • (1989) J. Cell Biol. , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 8
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K., and K. Simons. 1995. The role of N-glycans in the secretory pathway. Cell. 81:309-311.
    • (1995) Cell , vol.81 , pp. 309-311
    • Fiedler, K.1    Simons, K.2
  • 9
    • 0028969528 scopus 로고
    • Newly synthesised transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter, C.E., C.N. Connolly, D.F. Cutler, and C.R. Hopkins. 1995. Newly synthesised transferrin receptors can be detected in the endosome before they appear on the cell surface. J. Biol. Chem. 270:10999-11003.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 10
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes
    • Futter, C.E., A. Pearse, L.J. Hewlett, and C.R. Hopkins. 1996. Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes. J. Cell Biol. 132:1011-1023.
    • (1996) J. Cell Biol. , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.J.3    Hopkins, C.R.4
  • 11
  • 13
    • 0021926009 scopus 로고
    • The appearance and internalization of transferrin receptors at the margins of speading human tumor cells
    • Hopkins, C.R. 1985. The appearance and internalization of transferrin receptors at the margins of speading human tumor cells. Cell. 40:199-208.
    • (1985) Cell , vol.40 , pp. 199-208
    • Hopkins, C.R.1
  • 14
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in epidermoid carcinoma cells
    • Hopkins, C.R., and I.S. Trowbridge. 1983. Internalization and processing of transferrin and the transferrin receptor in epidermoid carcinoma cells. J. Cell Biol. 97:508-521.
    • (1983) J. Cell Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 15
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins, C.R., A Gibson, M. Shipman, and K. Miller. 1990. Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature (Lond.). 346:335-339.
    • (1990) Nature (Lond.) , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 16
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins, C.R., A. Gibson, M. Shipman, D.K. Strickland, and I.S. Trowbridge. 1994. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J. Cell Biol. 125:1265-1274.
    • (1994) J. Cell Biol. , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 17
    • 0025173762 scopus 로고
    • Endocytic pathways in polarized caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces
    • Hughson, E.J., and C.R. Hopkins. 1990. Endocytic pathways in polarized caco-2 cells: identification of an endosomal compartment accessible from both apical and basolateral surfaces. J. Cell Biol. 110:337-348.
    • (1990) J. Cell Biol. , vol.110 , pp. 337-348
    • Hughson, E.J.1    Hopkins, C.R.2
  • 18
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., M. Tagaya, O. Ullrich, C. Montecucco, and K. Simons. 1995. Different requirements for NSF, SNAP, and rab proteins in apical and basolateral transport in MDCK cells. Cell. 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 19
    • 0025014580 scopus 로고
    • Role of the human transferrin receptor cytoplasmic domain in endocytosis: Localization of a specific signal sequence for internalization
    • Jing, S., T. Spencer, K. Miller, C. Hopkins, and I.S. Trowbridge. 1990. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization. J. Cell Biol. 110:283-294.
    • (1990) J. Cell Biol. , vol.110 , pp. 283-294
    • Jing, S.1    Spencer, T.2    Miller, K.3    Hopkins, C.4    Trowbridge, I.S.5
  • 20
    • 0001166951 scopus 로고
    • A formaldehyde-glularaldehyde fixative of high osmolarity for use in electron microscopy
    • Karnovsky, M.J. 1965. A formaldehyde-glularaldehyde fixative of high osmolarity for use in electron microscopy. J. Cell Biol. 27:137.
    • (1965) J. Cell Biol. , vol.27 , pp. 137
    • Karnovsky, M.J.1
  • 21
    • 0029024637 scopus 로고
    • Membrane protein trafficking through the common apical endosome in Caco-2 cells
    • Knight, A., E. Hughson, C.R. Hopkins, and D.E. Cutler. 1995. Membrane protein trafficking through the common apical endosome in Caco-2 cells. Mol. Biol. Cell. 6:597-610.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 597-610
    • Knight, A.1    Hughson, E.2    Hopkins, C.R.3    Cutler, D.E.4
  • 22
    • 0022154733 scopus 로고
    • Exocytotic pathways exist to both the apical and the basolateral cell surface of the polarized epithelial cell MDCK
    • Kondor-Koch, C., R. Bravo, S.D. Fuller, D. Cutler, and H. Garoff. 1985. Exocytotic pathways exist to both the apical and the basolateral cell surface of the polarized epithelial cell MDCK. Cell. 43:247-306.
    • (1985) Cell , vol.43 , pp. 247-306
    • Kondor-Koch, C.1    Bravo, R.2    Fuller, S.D.3    Cutler, D.4    Garoff, H.5
  • 24
    • 0028871658 scopus 로고
    • Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes
    • Leitinger, B., A. Hille-Rehleld, and M. Spiess. 1995. Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes. Proc. Natl. Acad. Sci. USA. 92:10109-10113.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10109-10113
    • Leitinger, B.1    Hille-Rehleld, A.2    Spiess, M.3
  • 25
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and I. Mellman. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 26
    • 0027444967 scopus 로고
    • Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells
    • Matter, K., J.A. Whitney, E.M. Yamamoto, and I. Mellman. 1993. Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells. Cell. 74:1053-1064.
    • (1993) Cell , vol.74 , pp. 1053-1064
    • Matter, K.1    Whitney, J.A.2    Yamamoto, E.M.3    Mellman, I.4
  • 27
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor, S., J.F. Presley, and F.R. Maxfield 1993. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol. 121:1257-1269.
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 28
    • 0021685289 scopus 로고
    • The human transferrin receptor gene: Genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence
    • McClelland, A., L. Kuhn, and F.H. Ruddle. 1484. The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence. Cell. 39:267-274.
    • (1484) Cell , vol.39 , pp. 267-274
    • McClelland, A.1    Kuhn, L.2    Ruddle, F.H.3
  • 29
    • 0025823445 scopus 로고
    • Transferrin receptors promote the formation of clathrin lattices
    • Miller, K., M. Shipman, I.S. Trowbridge, and C.R. Hopkins. 1991. Transferrin receptors promote the formation of clathrin lattices. Cell. 65:621-632.
    • (1991) Cell , vol.65 , pp. 621-632
    • Miller, K.1    Shipman, M.2    Trowbridge, I.S.3    Hopkins, C.R.4
  • 30
    • 0026531638 scopus 로고
    • Plasma membrane protein sorting in polarized epithelial cells
    • Mostov, K., G. Apodaca, B. Aroeti, and C. Okamoto. 1992. Plasma membrane protein sorting in polarized epithelial cells. J. Cell Biol. 116:577-583.
    • (1992) J. Cell Biol. , vol.116 , pp. 577-583
    • Mostov, K.1    Apodaca, G.2    Aroeti, B.3    Okamoto, C.4
  • 31
    • 0029005390 scopus 로고
    • Apical- and basolateral-coated pits of MDCK cells differ in their rates of maturation into coated vesicles, hut not in the ability to distinguish between mutant hemagglutinin proteins with different internalization signals
    • Naim, H.Y., D.T. Dodds, C.B. Brewer, and M.G. Roth. 1995. Apical- and basolateral-coated pits of MDCK cells differ in their rates of maturation into coated vesicles, hut not in the ability to distinguish between mutant hemagglutinin proteins with different internalization signals. J. Cell Biol. 129:1241-1250.
    • (1995) J. Cell Biol. , vol.129 , pp. 1241-1250
    • Naim, H.Y.1    Dodds, D.T.2    Brewer, C.B.3    Roth, M.G.4
  • 32
    • 0028709374 scopus 로고
    • Recombinant Rous sarcoma virus vectors for avian cells
    • Odorizzi, G., and I.S. Trowbridge. 1994. Recombinant Rous sarcoma virus vectors for avian cells. Methods Cell Biol. 43:79-97.
    • (1994) Methods Cell Biol. , vol.43 , pp. 79-97
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 33
    • 0028282982 scopus 로고
    • Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment
    • Odorizzi, C.G., I.S. Trowbridge, L. Xue, C.R. Hopkins, C. Davis, and J.F. Collawn. 1994. Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment. J. Cell Biol. 126:317-330.
    • (1994) J. Cell Biol. , vol.126 , pp. 317-330
    • Odorizzi, C.G.1    Trowbridge, I.S.2    Xue, L.3    Hopkins, C.R.4    Davis, C.5    Collawn, J.F.6
  • 34
    • 0024810856 scopus 로고
    • Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes
    • Parton, R.G., K. Prydz, M. Bomsel, K. Simons, and G. Griffiths. 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
  • 36
    • 0025862051 scopus 로고
    • Molecular and cellular mechanisms involved in transepithelial transport
    • Schaerer, E., M.R. Neutra, and J.P. Kraehenbuhl. 1991. Molecular and cellular mechanisms involved in transepithelial transport. J. Memb. Biol. 123:93-103.
    • (1991) J. Memb. Biol. , vol.123 , pp. 93-103
    • Schaerer, E.1    Neutra, M.R.2    Kraehenbuhl, J.P.3
  • 37
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and A. Wandinger-Ness. 1990. Polarized sorting in epithelia. Cell. 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 38
    • 0021806048 scopus 로고
    • A new method for preparing gold probes for multiple labeling cytochemistry
    • Slot, J.W., and H.J. Geuze. 1985. A new method for preparing gold probes for multiple labeling cytochemistry. Eur. J. Cell Biol. 38:87-93.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 39
    • 0029610381 scopus 로고
    • Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex
    • Stinchcombe, J., D. Cutler, and C.R. Hopkins. 1995. Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex. J. Cell Biol. 131:1387-1401.
    • (1995) J. Cell Biol. , vol.131 , pp. 1387-1401
    • Stinchcombe, J.1    Cutler, D.2    Hopkins, C.R.3
  • 40
    • 0030047961 scopus 로고    scopus 로고
    • A novel class of clathrin-coated vesicles budding from endosomes
    • Stoorvogel, W., V. Oorschot, and H.J. Geuze. 1996. A novel class of clathrin-coated vesicles budding from endosomes. J. Cell Biol. 132:21-33.
    • (1996) J. Cell Biol. , vol.132 , pp. 21-33
    • Stoorvogel, W.1    Oorschot, V.2    Geuze, H.J.3
  • 41
    • 0026099060 scopus 로고
    • Protein traffic between distinct plasma membrane domains: Isolation and characterization of vesicular carriers involved in transcytosis
    • Sztul, E., A. Kaplin, L. Saucan, and G. Palade. 1991. Protein traffic between distinct plasma membrane domains: isolation and characterization of vesicular carriers involved in transcytosis. Cell. 64:81-89.
    • (1991) Cell , vol.64 , pp. 81-89
    • Sztul, E.1    Kaplin, A.2    Saucan, L.3    Palade, G.4
  • 42
    • 0023544865 scopus 로고
    • Constitutive apical secretion of an 80-kD sulfated glycoprotein complex in the polarized epithelial Madin-Darby canine kidney cell line
    • Urban, J., K. Parczyk, A. Leutz, M. Kayne, and C. Kondor-Koch. 1987. Constitutive apical secretion of an 80-kD sulfated glycoprotein complex in the polarized epithelial Madin-Darby canine kidney cell line. J. Cell Biol. 105: 2735-2743.
    • (1987) J. Cell Biol. , vol.105 , pp. 2735-2743
    • Urban, J.1    Parczyk, K.2    Leutz, A.3    Kayne, M.4    Kondor-Koch, C.5
  • 44
    • 0026747939 scopus 로고
    • Monoclonal antibodies against defined epitopes of the human transferrin receptor cytoplasmic tail
    • White, S., K. Miller, C. Hopkins, and I.S. Trowbridge. 1992. Monoclonal antibodies against defined epitopes of the human transferrin receptor cytoplasmic tail. Biochem. Biophys. Acta. 1136:28-34.
    • (1992) Biochem. Biophys. Acta , vol.1136 , pp. 28-34
    • White, S.1    Miller, K.2    Hopkins, C.3    Trowbridge, I.S.4


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