메뉴 건너뛰기




Volumn 144, Issue 4, 1999, Pages 687-699

Coupling assembly of the E-cadherin/β-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells

Author keywords

Adhesion; Epithelia; Membrane domains; Polarity; Protein targeting

Indexed keywords

BETA CATENIN; MUTANT PROTEIN; UVOMORULIN;

EID: 0033593803     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.4.687     Document Type: Article
Times cited : (251)

References (57)
  • 1
    • 0028578064 scopus 로고
    • Assembly of the cadherin-catenin complex in vitro with recombinant proteins
    • Aberle, H., S. Butz, J. Stappert, H. Weissig, R. Kemler, and H. Hoschuetzky. 1994. Assembly of the cadherin-catenin complex in vitro with recombinant proteins. J. Cell Sci. 107:3655-3663.
    • (1994) J. Cell Sci. , vol.107 , pp. 3655-3663
    • Aberle, H.1    Butz, S.2    Stappert, J.3    Weissig, H.4    Kemler, R.5    Hoschuetzky, H.6
  • 2
    • 0023514599 scopus 로고
    • Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system
    • Aruffo, A., and B. Seed. 1987a. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc. Natl. Acad. Sci. USA. 84:8573-8577.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8573-8577
    • Aruffo, A.1    Seed, B.2
  • 3
    • 0023440913 scopus 로고
    • Molecular cloning of two CD7 (T-cell leukemia antigen) cDNAs by a COS cell expression system
    • Aruffo, A., and B. Seed. 1987. Molecular cloning of two CD7 (T-cell leukemia antigen) cDNAs by a COS cell expression system. EMBO (Eur. Mol. Biol. Organ.) J. 6:3313-6331.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 3313-6331
    • Aruffo, A.1    Seed, B.2
  • 4
    • 0027761007 scopus 로고
    • Impression of Wnt-1 in PC12 cells results in modulation of plakoglohin and E-cadherin and increased cellular adhesion
    • Bradley, R.S., P. Cowin, and A.M. Brown. 1993. Impression of Wnt-1 in PC12 cells results in modulation of plakoglohin and E-cadherin and increased cellular adhesion. J. Cell Biol. 123:1857-1865.
    • (1993) J. Cell Biol. , vol.123 , pp. 1857-1865
    • Bradley, R.S.1    Cowin, P.2    Brown, A.M.3
  • 5
    • 0029998613 scopus 로고    scopus 로고
    • Lateral dimerization is required for the homophilic binding activity of C-cadherin
    • Brieher, W.M., A.S. Yap, and B.M. Gumbiner. 1996. Lateral dimerization is required for the homophilic binding activity of C-cadherin J. Cell Biol. 135: 487-496.
    • (1996) J. Cell Biol. , vol.135 , pp. 487-496
    • Brieher, W.M.1    Yap, A.S.2    Gumbiner, B.M.3
  • 6
    • 1842332725 scopus 로고    scopus 로고
    • The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing
    • Briley, G.P., M.A. Hissong, M.L. Chiu, and D.C. Lee. 1997. The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing. Mol. Biol. Cell. 8:1619-1631.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1619-1631
    • Briley, G.P.1    Hissong, M.A.2    Chiu, M.L.3    Lee, D.C.4
  • 7
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affeets polarized expression of two proteins in MDCK cells
    • Brown, D.A., B. Crise, and J.K. Rose. 1989. Mechanism of membrane anchoring affeets polarized expression of two proteins in MDCK cells. Science. 245: 1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 8
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush, K.T., A.L. Goldberg, and S.K. Nigam. 1997. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272:9086-9092.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 9
    • 0031456158 scopus 로고    scopus 로고
    • Wnt signaling: A common theme in animal development
    • Cadigan, K.M., and K. Nusse. 1997. Wnt signaling: a common theme in animal development. Genes Dev. 11:3286-3305.
    • (1997) Genes Dev. , vol.11 , pp. 3286-3305
    • Cadigan, K.M.1    Nusse, K.2
  • 10
    • 0025766194 scopus 로고
    • An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor
    • Casanova, J.E., G. Apodaca, and K.E. Mostov. 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
  • 11
    • 0027182031 scopus 로고
    • Expression and localization of two low molecular weight GTP-binding proteins. Rab8 and Rab10, by epitope tag
    • Chen, Y.-T. C. Holcomb, and H.P. Moore. 1993. Expression and localization of two low molecular weight GTP-binding proteins. Rab8 and Rab10, by epitope tag. Proc. Natl. Acad. Sci. USA. 90:6508-6512.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6508-6512
    • Chen, Y.-T.1    Holcomb, C.2    Moore, H.P.3
  • 12
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A.L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 13
    • 0030960388 scopus 로고    scopus 로고
    • Uncoupling of XB/U-cadherin-catenin complex formation from its function in cell-cell adhesion
    • Finnemann, S., I. Mitrik, M. Hess, O. Otto, and D. Wedlich. 1997. Uncoupling of XB/U-cadherin-catenin complex formation from its function in cell-cell adhesion. J. Biol. Chem. 272:11856-11862.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11856-11862
    • Finnemann, S.1    Mitrik, I.2    Hess, M.3    Otto, O.4    Wedlich, D.5
  • 14
    • 0022021158 scopus 로고
    • An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments
    • Fuller, S.D., R. Bravo, and K. Simons. 1985. An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments. EMBO (Eur. Mol Biol. Or-gan.) J. 4:297-307.
    • (1985) EMBO (Eur. Mol Biol. Or-gan.) J. , vol.4 , pp. 297-307
    • Fuller, S.D.1    Bravo, R.2    Simons, K.3
  • 15
    • 0025037793 scopus 로고
    • Polarized expression of functional rat liver asialoglycoprotein receptor in transfected Madin-Darby canine kidney cells
    • Graeve, L., A. Patzak, K. Drickamer, and E. Rodriguez-Boulan. 1990. Polarized expression of functional rat liver asialoglycoprotein receptor in transfected Madin-Darby canine kidney cells. J Biol. Chem. 265:1216-1224.
    • (1990) J Biol. Chem. , vol.265 , pp. 1216-1224
    • Graeve, L.1    Patzak, A.2    Drickamer, K.3    Rodriguez-Boulan, E.4
  • 16
    • 0026322157 scopus 로고
    • Mechanism for regulating cell surface distribution of Na(+)K(+)-ATPase in polarized epithelial cells
    • Hammerton, R.W., K.A. Krzeminski, R.W. Mays, T.A. Ryan, D.A. Wollner, and W.J. Nelson. 1991. Mechanism for regulating cell surface distribution of Na(+)K(+)-ATPase in polarized epithelial cells. Science. 254:847-850.
    • (1991) Science , vol.254 , pp. 847-850
    • Hammerton, R.W.1    Krzeminski, K.A.2    Mays, R.W.3    Ryan, T.A.4    Wollner, D.A.5    Nelson, W.J.6
  • 17
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex assembly
    • Hinck, L., I.S. Nathke, J. Papkoff, and W.J. Nelson. 1994a. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell. 125:1327-1340.
    • (1994) J. Cell. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Nathke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 18
    • 0028258445 scopus 로고
    • Wnt-1 modulates cell-cell adhesion in mammalian cells by stabilizing beta-catenin binding to the cell adhesion protein cadherin
    • Hinck, L., W.J. Nelson, and J. Papkoff. 1994b. Wnt-1 modulates cell-cell adhesion in mammalian cells by stabilizing beta-catenin binding to the cell adhesion protein cadherin. J. Cell Biol. 124:729-741.
    • (1994) J. Cell Biol. , vol.124 , pp. 729-741
    • Hinck, L.1    Nelson, W.J.2    Papkoff, J.3
  • 19
    • 0025909610 scopus 로고
    • Isolation of the cDNA encoding glycoprotein-2 (Gp-2). The major zymogen granule membrane protein. Homology to uromodulin/Tamm-Horsfall protein
    • Hoops, T.C., and M.J. Rindler, 1991. Isolation of the cDNA encoding glycoprotein-2 (GP-2). the major zymogen granule membrane protein. Homology to uromodulin/Tamm-Horsfall protein. J. Biol. Chem. 266:4257-4263.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4257-4263
    • Hoops, T.C.1    Rindler, M.J.2
  • 20
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber, A.H., W.J. Nelson, and W.I. Weis. 1997. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell. 90:871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 21
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton
    • Hulsken, J., W. Birchmeier, and J. Behrens. 1994. E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton. J. Cell Biol. 127:2061-2069.
    • (1994) J. Cell Biol. , vol.127 , pp. 2061-2069
    • Hulsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 22
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fe receptors in MDCK cells
    • Hunziker, W., and C. Fumey, 1994. A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fe receptors in MDCK cells. EMBO (Eur. Mol. Biol. Organ.) J. 13:2963-2967.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2963-2967
    • Hunziker, W.1    Fumey, C.2
  • 23
    • 0029040123 scopus 로고
    • Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex
    • Jou, T.S., D.B. Stewart, J. Stappert. W.J. Nelson, and J.A. Marrs. 1995. Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc. Natl. Acad. Sci. USA. 92:5067-5071.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5067-5071
    • Jou, T.S.1    Stewart, D.B.2    Stappert, J.3    Nelson, W.J.4    Marrs, J.A.5
  • 24
    • 0026877444 scopus 로고
    • Classical cadherins
    • Kemler, R. 1992. Classical cadherins. Semin. Cell Biol. 3:149-155.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 149-155
    • Kemler, R.1
  • 25
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • Knudsen, K.A., A.P. Soler, K.R. Johnson, and M.J. Wheelock. 1995. Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. J. Cell Biol. 130:67-77.
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 26
    • 0025297214 scopus 로고
    • Vectorial targeting of an endogenous apical membrane asialoglycoprotein and uvomorulin in MDCK cells
    • Le Bivic, A., Y. Sambuy, K. Mostov, and E. Rodriguez-Boulan. 1990. Vectorial targeting of an endogenous apical membrane asialoglycoprotein and uvomorulin in MDCK cells. J. Cell Biol. 110:1533-1539.
    • (1990) J. Cell Biol. , vol.110 , pp. 1533-1539
    • Le Bivic, A.1    Sambuy, Y.2    Mostov, K.3    Rodriguez-Boulan, E.4
  • 27
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti, M.P., I.W. Caras, M.A. Davitz, and E., Rodriguez-Boulan. 1989. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109:2145-2156.
    • (1989) J. Cell Biol. , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 28
    • 0021683127 scopus 로고
    • Monoclonal antibodies specific for the carboxy terminus of simian virus 40 large T antigen
    • MacArthur, H., and G. Walter. 1984. Monoclonal antibodies specific for the carboxy terminus of simian virus 40 large T antigen. J. Virol. 52:483-491.
    • (1984) J. Virol. , vol.52 , pp. 483-491
    • MacArthur, H.1    Walter, G.2
  • 29
    • 0027515201 scopus 로고
    • Distinguishing roles of the membrane-cytoskeleton and cadherin mediated cell-cell adhesion in generating different Na(+)K(+)-ATPase distributions in polarized epithelia
    • Marrs, J.A., E.W. Napolitano, C. Murphy-Erdosh, R.W. Mays, L.F. Reichardt, and W.J. Nelson. 1993. Distinguishing roles of the membrane-cytoskeleton and cadherin mediated cell-cell adhesion in generating different Na(+)K(+)-ATPase distributions in polarized epithelia. J. Cell. Biol. 123: 149-164.
    • (1993) J. Cell. Biol. , vol.123 , pp. 149-164
    • Marrs, J.A.1    Napolitano, E.W.2    Murphy-Erdosh, C.3    Mays, R.W.4    Reichardt, L.F.5    Nelson, W.J.6
  • 30
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • Matter, K., W. Hunziker, and I. Mellman. 1992. Basolateral sorting of LDL receptor in MDCK cells: the cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell. 71:741-753.
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 31
    • 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
  • 32
    • 0027989516 scopus 로고
    • Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells
    • Matter, K., E.M. Yamamoto, and I. Mellman. 1994. Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells. J. Cell Biol. 126:991-1004.
    • (1994) J. Cell Biol. , vol.126 , pp. 991-1004
    • Matter, K.1    Yamamoto, E.M.2    Mellman, I.3
  • 33
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays, R.W., K.A. Siemens, B.A. Fritz, A.W. Lowe, G. van Meer, and W.J. Nelson. 1995. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol. 130:1105-1115.
    • (1995) J. Cell Biol. , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemens, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 34
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi, A., and M. Takeichi. 1988. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 7:3679-3684.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 35
    • 0023225108 scopus 로고
    • Transformation of cell adhesion properties by exocenously introduced E-cadherin cDNA
    • Nagafuchi, A., Y. Shirayoshi, K. Okazaki, K. Yasuda, and M. Takeichi. 1987. Transformation of cell adhesion properties by exocenously introduced E-cadherin cDNA. Nature. 329:341-343.
    • (1987) Nature , vol.329 , pp. 341-343
    • Nagafuchi, A.1    Shirayoshi, Y.2    Okazaki, K.3    Yasuda, K.4    Takeichi, M.5
  • 36
    • 0029980542 scopus 로고    scopus 로고
    • Structural basis of calcium-induced E-cadherin rigidification and dimerization
    • Nagar, B., M. Overduin, M. Ikura, and J.M. Rini. 1996. Structural basis of calcium-induced E-cadherin rigidification and dimerization. Nature. 380:360-364.
    • (1996) Nature , vol.380 , pp. 360-364
    • Nagar, B.1    Overduin, M.2    Ikura, M.3    Rini, J.M.4
  • 37
    • 0026446341 scopus 로고
    • Regulation of cell surface polarity from bacteria to mammals
    • Nelson, W.J. 1992. Regulation of cell surface polarity from bacteria to mammals. Science. 258:948-955.
    • (1992) Science , vol.258 , pp. 948-955
    • Nelson, W.J.1
  • 38
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N., and W.E. Balch. 1997. A di-acidic signal required for selective export from the endoplasmic reticulum. Science. 277:556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 39
    • 0030885251 scopus 로고    scopus 로고
    • Mammalian GPI proteins: Sorting, membrane residence and functions
    • Nosjean, O., A. Briolay, and B. Roux. 1997. Mammalian GPI proteins: sorting, membrane residence and functions. Biochim. Biophys. Acta. 1331:153-186.
    • (1997) Biochim. Biophys. Acta. , vol.1331 , pp. 153-186
    • Nosjean, O.1    Briolay, A.2    Roux, B.3
  • 40
    • 0025064957 scopus 로고
    • Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin
    • Ozawa, M., and R. Kemler. 1990. Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin. J. Cell Biol. 111:1645-1650.
    • (1990) J. Cell Biol. , vol.111 , pp. 1645-1650
    • Ozawa, M.1    Kemler, R.2
  • 41
    • 0026518504 scopus 로고
    • Molecular organization of the uvomorulin-catenin complex
    • Ozawa, M., and R. Kemler. 1992. Molecular organization of the uvomorulin-catenin complex. J. Cell Biol. 116:989-996.
    • (1992) J. Cell Biol. , vol.116 , pp. 989-996
    • Ozawa, M.1    Kemler, R.2
  • 42
    • 0025374899 scopus 로고
    • Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule
    • Ozawa, M., M. Ringwald, and R. Kemler. 1990. Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule. Proc. Natl. Acad. Sci. USA. 87:4246-4250.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4246-4250
    • Ozawa, M.1    Ringwald, M.2    Kemler, R.3
  • 43
    • 0024470450 scopus 로고
    • Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: Interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy
    • Pagano, R.E., M.A. Sepanski, and O.C. Martin. 1989. Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy. J. Cell Biol. 109:2067-2079.
    • (1989) J. Cell Biol. , vol.109 , pp. 2067-2079
    • Pagano, R.E.1    Sepanski, M.A.2    Martin, O.C.3
  • 44
    • 0026069460 scopus 로고
    • Acridine orange as a probe for measuring pH gradients across membranes: Mechanism and limitations
    • Palmgren, M.G. 1991. Acridine orange as a probe for measuring pH gradients across membranes: mechanism and limitations. Anal Biochem. 192:316-321.
    • (1991) Anal Biochem. , vol.192 , pp. 316-321
    • Palmgren, M.G.1
  • 45
    • 0028981208 scopus 로고
    • Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D.L., E.R. Koslov, P. Kebriaei, C.D. Cianci, and J.S. Morrow. 1995. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. USA. 92:8813-8817.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 46
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, E., and W.J. Nelson. 1989. Morphogenesis of the polarized epithelial cell phenotype. Science. 245:718-725.
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 49
    • 0025933683 scopus 로고
    • Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells
    • Shore, E.M., and W.J. Nelson. 1991. Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells. J. Biol. Chem. 266:19672-19680.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19672-19680
    • Shore, E.M.1    Nelson, W.J.2
  • 50
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and N.A. Wandinger. 1990. Polarized sorting in epithelia. Cell. 62: 207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger, N.A.2
  • 51
    • 0019989719 scopus 로고
    • Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter
    • Southern, P.J., and P. Berg. 1982. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J. Mol. Appl. Genet. 1:327-341.
    • (1982) J. Mol. Appl. Genet. , vol.1 , pp. 327-341
    • Southern, P.J.1    Berg, P.2
  • 52
    • 0027938682 scopus 로고
    • A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated
    • Stappert, J., and R. Kemler. 1994. A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated. Cell Adhes. Commun. 2:319-327.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 319-327
    • Stappert, J.1    Kemler, R.2
  • 53
    • 0030701838 scopus 로고    scopus 로고
    • Identification of four distinct pools of catenins in mammalian cells and transformation-dependent changes in catenin distributions between these pools
    • Stewart, D.B., and W.J. Nelson. 1997. Identification of four distinct pools of catenins in mammalian cells and transformation-dependent changes in catenin distributions between these pools. J. Biol. Chem. 272:29652-29662.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29652-29662
    • Stewart, D.B.1    Nelson, W.J.2
  • 54
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas, D.C. C.B. Brewer, and M.G. Roth. 1993. Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J. Biol. Chem. 268:3313-3320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 56
    • 0030771851 scopus 로고    scopus 로고
    • Accumulation of Armadillo induced by Wingless. Dishevelled, and dominant-negative Zeste-White 3 leads to elevated DE-cadherin in Drosophila clone 8 wing disc cells
    • Yanagawa, S.i., J.S. Lee, T. Haruna, U. Oda, T. Uemura, M. Takeichi, and A. Ishimoto. 1997. Accumulation of Armadillo induced by Wingless. Dishevelled, and dominant-negative Zeste-White 3 leads to elevated DE-cadherin in Drosophila clone 8 wing disc cells. J. Biol. Chem. 272:25243-25251.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25243-25251
    • Yanagawa, S.I.1    Lee, J.S.2    Haruna, T.3    Oda, U.4    Uemura, T.5    Takeichi, M.6    Ishimoto, A.7
  • 57
    • 0032482201 scopus 로고    scopus 로고
    • The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn
    • Yap, A.S., C.M. Niessen, and B.M. Gumbiner. 1998. The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn. J. Cell Biol. 141:779-789.
    • (1998) J. Cell Biol. , vol.141 , pp. 779-789
    • Yap, A.S.1    Niessen, C.M.2    Gumbiner, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.