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Volumn 9, Issue 4, 1998, Pages 901-915

Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPHORIN A; IMMUNOGLOBULIN A; IMMUNOGLOBULIN RECEPTOR; T LYMPHOCYTE RECEPTOR;

EID: 0031898776     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.4.901     Document Type: Article
Times cited : (44)

References (43)
  • 1
    • 0028359878 scopus 로고
    • Glycophorin A helical transmembrane domains dimerize in phorpholipid bilayers: A resonance energy transfer study
    • Adair, B.D., and Engelman, D.M. (1994). Glycophorin A helical transmembrane domains dimerize in phorpholipid bilayers: a resonance energy transfer study. Biochemistry 33, 5539-5544.
    • (1994) Biochemistry , vol.33 , pp. 5539-5544
    • Adair, B.D.1    Engelman, D.M.2
  • 2
    • 0028304457 scopus 로고
    • The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in MDCK cells
    • Apodaca, G., Enrich, C., and Mostov, K.E. (1994). The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in MDCK cells. J. Biol. Chem. 269, 19005-19013.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19005-19013
    • Apodaca, G.1    Enrich, C.2    Mostov, K.E.3
  • 3
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells via apical recycling endosomes
    • Apodaca, G., Katz, L.A., and Mostov, K.E. (1994). Receptor-mediated transcytosis of IgA in MDCK cells 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
  • 4
    • 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
  • 5
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann, B-J., William, J.K., and Marchesi, W.T. 1989. Synthetic peptides mimic the assembly of transmembrane glycoproteins. J. Biol. Chem. 264, 4033-4037.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4033-4037
    • Bormann, B.-J.1    William, J.K.2    Marchesi, W.T.3
  • 6
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer, C.B., and Roth, M.G. (1991). A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114, 413-421.
    • (1991) J. Cell Biol. , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 7
    • 0029954454 scopus 로고    scopus 로고
    • Signal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor transcytosis
    • Cardone, M.H., Smith, B.L., Mennitt, P.A., Mochly-Rosen, D., Silver, R.B., and Mostov, K.E. (1996). Signal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor transcytosis. J. Cell Biol. 133, 997-1005.
    • (1996) J. Cell Biol. , vol.133 , pp. 997-1005
    • Cardone, M.H.1    Smith, B.L.2    Mennitt, P.A.3    Mochly-Rosen, D.4    Silver, R.B.5    Mostov, K.E.6
  • 8
    • 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
  • 9
    • 0028355746 scopus 로고
    • Sequence and structure of the membrane-associated peptide of glycophorin A
    • Challou, N, Goormaghtigh, E., Cabiaux, V., Conrath, K., and Ruysschaert, J. (1994). Sequence and structure of the membrane-associated peptide of glycophorin A. Biochemistry 33, 6902-6910.
    • (1994) Biochemistry , vol.33 , pp. 6902-6910
    • Challou, N.1    Goormaghtigh, E.2    Cabiaux, V.3    Conrath, K.4    Ruysschaert, J.5
  • 10
    • 0030924771 scopus 로고    scopus 로고
    • Production of secretory immunoglobulin A by single mammalian cell
    • Chintalacharuvu, K.R., and Morrison, S. (1997). Production of secretory immunoglobulin A by single mammalian cell. Proc. Natl. Acad. Sci. USA 94, 6364-6368.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6364-6368
    • Chintalacharuvu, K.R.1    Morrison, S.2
  • 11
    • 0029952988 scopus 로고    scopus 로고
    • The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling
    • Chu, D.H., Spits, H., Peyron, J.F., Rowley, R.B., Bolen, J.B., and Weiss, A. (1996). The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling. EMBO J. 15, 6251-6261.
    • (1996) EMBO J. , vol.15 , pp. 6251-6261
    • Chu, D.H.1    Spits, H.2    Peyron, J.F.3    Rowley, R.B.4    Bolen, J.B.5    Weiss, A.6
  • 12
    • 0026601947 scopus 로고
    • Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases
    • Eiseman, E., and Bolen, J.B. (1992a). Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355, 78-80.
    • (1992) Nature , vol.355 , pp. 78-80
    • Eiseman, E.1    Bolen, J.B.2
  • 13
    • 0026730813 scopus 로고
    • Signal transduction by the cytoplasmic domains of Fc epsilon RI-gamma and TCR-zeta in rat basophilic leukemia cells
    • Eiseman, E., and Bolen, J.B. (1992b). Signal transduction by the cytoplasmic domains of Fc epsilon RI-gamma and TCR-zeta in rat basophilic leukemia cells. J. Biol. Chem. 267, 21027-21032.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21027-21032
    • Eiseman, E.1    Bolen, J.B.2
  • 14
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, Tw Jr, and Jovin, T.M. (1995). Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation, J. Cell Biol. 129, 1543-1558.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella Jr., Tw.1    Jovin, T.M.2
  • 15
    • 0029851704 scopus 로고    scopus 로고
    • Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
    • Gardina, P.J., and Manson, M.D. (1996). Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain [see comments]. Science 274, 425-426.
    • (1996) Science , vol.274 , pp. 425-426
    • Gardina, P.J.1    Manson, M.D.2
  • 17
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low density lipoprotein in cultured cells
    • Goldstein, J.L., Basu, S.K., and Brown, M.S. (1983). Receptor-mediated endocytosis of low density lipoprotein in cultured cells. Methods Enzymol. 96, 241-259.
    • (1983) Methods Enzymol. , vol.96 , pp. 241-259
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 19
    • 0026064305 scopus 로고
    • The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways
    • Irving, B.A., and Weiss, A. (1991). The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways. Cell 64, 891-901.
    • (1991) Cell , vol.64 , pp. 891-901
    • Irving, B.A.1    Weiss, A.2
  • 20
    • 0026521943 scopus 로고
    • Transepithelial transport and mucosal defence II: Secretion of IgA
    • Kraehenbuhl, J.-P., and Neutra, M.R. (1992). Transepithelial transport and mucosal defence II: secretion of IgA. Trends Cell Biol. 2, 170-174.
    • (1992) Trends Cell Biol. , vol.2 , pp. 170-174
    • Kraehenbuhl, J.-P.1    Neutra, M.R.2
  • 21
    • 0040658234 scopus 로고
    • The sacrificial receptor-translocation of polymeric IgA across epithelia
    • Kuhn, L.C., and Kraehenbuhl, J.-P. (1982). The sacrificial receptor-translocation of polymeric IgA across epithelia. Trends Biochem. 7, 299-302.
    • (1982) Trends Biochem. , vol.7 , pp. 299-302
    • Kuhn, L.C.1    Kraehenbuhl, J.-P.2
  • 22
    • 0026761298 scopus 로고
    • Functional dissection of structural domains in the receptor for colony-stimulating factor-1
    • Lee, A.W., and Nienhuis, A.W. (1992). Functional dissection of structural domains in the receptor for colony-stimulating factor-1. J. Biol. Chem. 267, 16472-16483.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16472-16483
    • Lee, A.W.1    Nienhuis, A.W.2
  • 23
    • 0026592483 scopus 로고
    • Recognition of liposomes by cells: In vitro binding and endocytosis mediated by specific lipid head groups and surface charge density
    • Lee, K., Hong, K., and Papahadjopoulos, D. (1992). Recognition of liposomes by cells: in vitro binding and endocytosis mediated by specific lipid head groups and surface charge density. Biochim. Biophys. Acta, 1103, 185-197.
    • (1992) Biochim. Biophys. Acta , vol.1103 , pp. 185-197
    • Lee, K.1    Hong, K.2    Papahadjopoulos, D.3
  • 25
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane α-helices
    • Lemmon, M.A., Glanagan, J.M., Treutlein, R., Zhang, J., and Engelman, D.M. (1992a). Sequence specificity in the dimerization of transmembrane α-helices. Biochemistry 31, 12719-12725.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Glanagan, J.M.2    Treutlein, R.3    Zhang, J.4    Engelman, D.M.5
  • 27
    • 0025998529 scopus 로고
    • T-cell and basophil activation through the cytopasmic tail of T-cell-receptor ζ family proteins
    • Letourneur, F., and Klausner, R.D. 1991.T-cell and basophil activation through the cytopasmic tail of T-cell-receptor ζ family proteins. Proc. Natl. Acad. Sci. USA 88, 8905-8909.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8905-8909
    • Letourneur, F.1    Klausner, R.D.2
  • 28
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K.R., Prestegard, J.H., and Engelman, D.M. (1997). A transmembrane helix dimer: structure and implications. Science 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 29
    • 0028202474 scopus 로고
    • Transepithelial transport of immunoglobulins
    • Mostov, K.E. (1994). Transepithelial transport of immunoglobulins. Annu. Rev. Immunol. 12, 63-84.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 63-84
    • Mostov, K.E.1
  • 30
    • 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
  • 31
    • 0026667712 scopus 로고
    • The cytoplasmic domain of the polymeric immunoglobulin receptor contains two internalization signals that are distinct from its basolateral sorting signal
    • Okamoto, C.T., S.-Shia, P., Bird, C., Mostov, K.E., and Roth, M.G. (1992). The cytoplasmic domain of the polymeric immunoglobulin receptor contains two internalization signals that are distinct from its basolateral sorting signal. J. Biol. Chem. 267, 9925-9932.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9925-9932
    • Okamoto, C.T.1    S-Shia, P.2    Bird, C.3    Mostov, K.E.4    Roth, M.G.5
  • 32
    • 0029043177 scopus 로고
    • Production of human secretory component with dimeric IgA binding capacity using viral expression systems
    • Rindisbacher, L., Cottet, S., Wittek, R., Kraehenbuhl, J.P., and Corthesy, B. (1995). Production of human secretory component with dimeric IgA binding capacity using viral expression systems. J. Biol. Chem. 270, 14220-14228.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14220-14228
    • Rindisbacher, L.1    Cottet, S.2    Wittek, R.3    Kraehenbuhl, J.P.4    Corthesy, B.5
  • 33
    • 0028814024 scopus 로고
    • Determination of helix-helix interactions in membranes by rotational resonance NMR
    • Smith, S.O., and Bormann, B.J. (1995). Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc. Natl. Acad. Sci. USA 92, 488-491.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 488-491
    • Smith, S.O.1    Bormann, B.J.2
  • 34
    • 0027998280 scopus 로고
    • Transcytosis of the polymeric immunoglobulin receptor is regulated in multiple intracellular compartments
    • Song, W., Apodaca, G., and Mostov, K. (1994a). Transcytosis of the polymeric immunoglobulin receptor is regulated in multiple intracellular compartments. J. Biol. Chem. 269, 29474-29480.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29474-29480
    • Song, W.1    Apodaca, G.2    Mostov, K.3
  • 35
    • 0028082426 scopus 로고
    • Stimulation of transcytosis of the polymeric immunoglobulin receptor by dimeric IgA
    • Song, W., Bomsel, M., Casanova, J., Vaerman, J.-P., and Mostov, K.E. (1994b). Stimulation of transcytosis of the polymeric immunoglobulin receptor by dimeric IgA. Proc. Natl. Acad. Sci. USA 91, 163-166.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 163-166
    • Song, W.1    Bomsel, M.2    Casanova, J.3    Vaerman, J.-P.4    Mostov, K.E.5
  • 36
    • 0028999160 scopus 로고
    • Dimeric and tetrameric IgA are transcytosed equally by the polymeric immunoglobulin receptor
    • Song, W., Vaerman, J.-P., and Mostov, K.E. (1995). Dimeric and tetrameric IgA are transcytosed equally by the polymeric immunoglobulin receptor. J. Immunol. 155, 715-721.
    • (1995) J. Immunol. , vol.155 , pp. 715-721
    • Song, W.1    Vaerman, J.-P.2    Mostov, K.E.3
  • 37
    • 0028307058 scopus 로고
    • Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond
    • Sorokin, A., Lemmon, M.A., Ullrich, A., and Schlessinger, J. (1994). Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond. J. Biol. Chem. 269, 9752-9759.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9752-9759
    • Sorokin, A.1    Lemmon, M.A.2    Ullrich, A.3    Schlessinger, J.4
  • 38
    • 0025274249 scopus 로고
    • A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization
    • Sternberg, M.J.E., and Gullick, W.J. (1990). A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization. Protein Eng. 3, 245-248.
    • (1990) Protein Eng. , vol.3 , pp. 245-248
    • Sternberg, M.J.E.1    Gullick, W.J.2
  • 39
    • 0030198866 scopus 로고    scopus 로고
    • Receptor signaling: Dimerization and beyond
    • Stock, J. (1996). Receptor signaling: dimerization and beyond. Curr. Biol. 6, 825-827.
    • (1996) Curr. Biol. , vol.6 , pp. 825-827
    • Stock, J.1
  • 40
    • 0029803848 scopus 로고    scopus 로고
    • Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer
    • Tatsuno, I., Homma, M., Oosawa, K., and Kawagishi, I. (1996). Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer [see comments]. Science 274, 423-425.
    • (1996) Science , vol.274 , pp. 423-425
    • Tatsuno, I.1    Homma, M.2    Oosawa, K.3    Kawagishi, I.4
  • 41
    • 0027092981 scopus 로고
    • The glycophorin A transmembrane domain dimer: Sequence-specific propensity
    • Treutlein, H.R., Lemmon, M.A., Engelman, D.M., and Brunger, A.T. 1992. The glycophorin A transmembrane domain dimer: sequence-specific propensity. Biochemistry 31, 12726-12733.
    • (1992) Biochemistry , vol.31 , pp. 12726-12733
    • Treutlein, H.R.1    Lemmon, M.A.2    Engelman, D.M.3    Brunger, A.T.4
  • 42
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A.V., Lamaze, C., and Schmid, S.L. (1996). Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 43
    • 0021678703 scopus 로고
    • Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line
    • Weiss, A., and Stobo, J.D. (1984). Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line. J. Exp. Med. 160, 1284-1299.
    • (1984) J. Exp. Med. , vol.160 , pp. 1284-1299
    • Weiss, A.1    Stobo, J.D.2


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