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Adaptation of core mechanisms to generate cell polarity
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Nelson W.J. Adaptation of core mechanisms to generate cell polarity. Nature. 422:2003;766-774.
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Nelson, W.J.1
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Composition and formation of intercellular junctions in epithelial cells
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Knust E., Bossinger O. Composition and formation of intercellular junctions in epithelial cells. Science. 298:2002;1955-1959.
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Knust, E.1
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Tsukita S., Furuse M. Claudin-based barrier in simple and stratified cellular sheets. Curr. Opin. Cell Biol. 14:2002;531-536.
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Tsukita, S.1
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6
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0031740862
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Drosophila coracle, a member of the protein 4.1 superfamily, has essential structural functions in the septate junctions and developmental functions in embryonic and adult epithelial cells
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Lamb R.S., Ward R.E., Schweizer L., Fehon R.G. Drosophila coracle, a member of the protein 4.1 superfamily, has essential structural functions in the septate junctions and developmental functions in embryonic and adult epithelial cells. Mol. Biol. Cell. 9:1998;3505-3519.
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7
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0038457822
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+ ATPase are essential for septate junction function in Drosophila
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A genetic screen is employed to identify genes required for paracellular barrier formation in the Drosophila salivary gland. Mutations disrupting the paracellular barrier are shown to correlate with ultrastructural defects in epidermal septate junctions. Interactions among several newly described components of the SJ are considered in detail.
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+ ATPase are essential for septate junction function in Drosophila. J. Cell Biol. 161:2003;979-989 A genetic screen is employed to identify genes required for paracellular barrier formation in the Drosophila salivary gland. Mutations disrupting the paracellular barrier are shown to correlate with ultrastructural defects in epidermal septate junctions. Interactions among several newly described components of the SJ are considered in detail.
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Genova, J.L.1
Fehon, R.G.2
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8
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0037228253
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Integrated activity of PDZ protein complexes regulates epithelial polarity
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••], establishes a genetic hierarchy by which three protein complexes interact to establish apicobasal polarity in the Drosophila epidermis. A central finding is that opposing activities of basolateral Scrib and apical Crb complxes define distinct plasma membrane domains and thus set the position of cell-cell junctions.
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••], establishes a genetic hierarchy by which three protein complexes interact to establish apicobasal polarity in the Drosophila epidermis. A central finding is that opposing activities of basolateral Scrib and apical Crb complxes define distinct plasma membrane domains and thus set the position of cell-cell junctions.
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Bilder, D.1
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9
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0037225708
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Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization
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•], establish that the Crb complex and Lgl group competitively function to define apical and basolateral membrane domains, respectively.
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•], establish that the Crb complex and Lgl group competitively function to define apical and basolateral membrane domains, respectively.
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Tanentzapf, G.1
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10
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0037319350
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Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
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This article links vertebrate epithelial cell polarity and TJ morphogenesis by establishing a direct biochemical interaction between vertebrate Par6 and PALS1 through the PDZ domain of Par6 in MDCK cell cultures. Misexpression experiments strongly suggest a functional interaction between these protein groups during tight-junction morphogenesis.
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Hurd T.W., Gao L., Roh M.H., Macara I.G., Margolis B. Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat. Cell Biol. 5:2003;137-142 This article links vertebrate epithelial cell polarity and TJ morphogenesis by establishing a direct biochemical interaction between vertebrate Par6 and PALS1 through the PDZ domain of Par6 in MDCK cell cultures. Misexpression experiments strongly suggest a functional interaction between these protein groups during tight-junction morphogenesis.
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Nat. Cell Biol.
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Hurd, T.W.1
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Margolis, B.5
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11
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0038032917
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Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity
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The authors demonstrate that mLgl and Par3 form mutually exclusive protein complexes with Par6β/aPKCλ during cell polarization. Immunolocalization experiments indicate that a transient co-localization between mLgl-2 and Par6/aPKC occurs during the initial phases of MDCK cell polarization. The authors suggest a model wherein mLgl binding to Par6β/aPKCλ inhibits TJ formation. MLgl dissociates from this complex upon phosphorylation by aPKCλ, thus permitting formation of a TK-promoting Par3/Par6β/aPKCλ complex.
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Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A., Hirose T., Iwamatsu A., Shinohara A., Ohno S. Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Curr. Biol. 13:2003;734-743 The authors demonstrate that mLgl and Par3 form mutually exclusive protein complexes with Par6β/aPKCλ during cell polarization. Immunolocalization experiments indicate that a transient co-localization between mLgl-2 and Par6/aPKC occurs during the initial phases of MDCK cell polarization. The authors suggest a model wherein mLgl binding to Par6β/aPKCλ inhibits TJ formation. MLgl dissociates from this complex upon phosphorylation by aPKCλ, thus permitting formation of a TK-promoting Par3/Par6β/aPKCλ complex.
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Yamanaka, T.1
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Hirose, T.6
Iwamatsu, A.7
Shinohara, A.8
Ohno, S.9
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12
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0029903396
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Armadillo, bazooka, and stardust are critical for early stages in formation of the zonula adherens and maintenance of the polarized blastoderm epithelium in Drosophila
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Muller H.A., Wieschaus E. armadillo, bazooka, and stardust are critical for early stages in formation of the zonula adherens and maintenance of the polarized blastoderm epithelium in Drosophila. J. Cell Biol. 134:1996;149-163.
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Muller, H.A.1
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13
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Drosophila atypical protein kinase C associates with bazooka and controls polarity of epithelia and neuroblasts
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Wodarz A., Ramrath A., Grimm A., Knust E. Drosophila atypical protein kinase C associates with bazooka and controls polarity of epithelia and neuroblasts. J. Cell Biol. 150:2000;1361-1374.
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Wodarz, A.1
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Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
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Bilder D., Li M., Perrimon N. Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science. 289:2000;113-116.
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Bilder, D.1
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15
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0034628471
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Localization of apical epithelial determinants by the basolateral PDZ protein Scribble
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Bilder D., Perrimon N. Localization of apical epithelial determinants by the basolateral PDZ protein Scribble. Nature. 403:2000;676-680.
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Bilder, D.1
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Drosophila stardust is a partner of crumbs in the control of epithelial cell polarity
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Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E. Drosophila stardust is a partner of crumbs in the control of epithelial cell polarity. Nature. 414:2001;638-643.
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Bachmann, A.1
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17
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0035819005
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Drosophila stardust interacts with crumbs to control polarity of epithelia but not neuroblasts
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Hong Y., Stronach B., Perrimon N., Jan L.Y., Jan Y.N. Drosophila stardust interacts with crumbs to control polarity of epithelia but not neuroblasts. Nature. 414:2001;634-638.
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Hong, Y.1
Stronach, B.2
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Jan, L.Y.4
Jan, Y.N.5
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18
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0030578406
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Crumbs, a component of the apical membrane, is required for zonula adherens formation in primary epithelia of Drosophila
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Tepass U. Crumbs, a component of the apical membrane, is required for zonula adherens formation in primary epithelia of Drosophila. Dev. Biol. 177:1996;217-225.
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Tepass, U.1
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Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila
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Wodarz A., Hinz U., Engelbert M., Knust E. Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila. Cell. 82:1995;67-76.
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Wodarz, A.1
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0037456795
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The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl
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Betschinger J., Mechtler K., Knoblich J.A. The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl. Nature. 422:2003;326-330.
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Nature
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Betschinger, J.1
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Knoblich, J.A.3
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22
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0037385561
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A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl
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Plant P.J., Fawcett J.P., Lin D.C., Holdorf A.D., Binns K., Kulkarni S., Pawson T. A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl. Nat. Cell Biol. 5:2003;301-308.
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Plant, P.J.1
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Lin, D.C.3
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Binns, K.5
Kulkarni, S.6
Pawson, T.7
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23
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Polarized insertion of new membrane from a cytoplasmic reservoir during cleavage of the Drosophila embryo
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Lecuit T., Wieschaus E. Polarized insertion of new membrane from a cytoplasmic reservoir during cleavage of the Drosophila embryo. J. Cell Biol. 150:2000;849-860.
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Lecuit, T.1
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How one becomes many: Blastoderm cellularization in Drosophila melanogaster
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Mazumdar A., Mazumdar M. How one becomes many: blastoderm cellularization in Drosophila melanogaster. Bioessays. 24:2002;1012-1022.
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Mazumdar, A.1
Mazumdar, M.2
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25
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0036228689
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Slam encodes a developmental regulator of polarized membrane growth during cleavage of the Drosophila embryo
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In syncitial Drosophila embryos, a process termed 'cellularization' precedes formation of the blastoderm epithelium. This article demonstrates that the novel locus slam is required for stage-specific polarized membrane growth during cellularization, thus identifying one of the earliest known players in the establishment of apicobasal polarity. Slam is further shown to regulate the localization of junctional components like Arm/β-catenin and Dlt.
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Lecuit T., Samanta R., Wieschaus E. slam encodes a developmental regulator of polarized membrane growth during cleavage of the Drosophila embryo. Dev. Cell. 2:2002;425-436 In syncitial Drosophila embryos, a process termed 'cellularization' precedes formation of the blastoderm epithelium. This article demonstrates that the novel locus slam is required for stage-specific polarized membrane growth during cellularization, thus identifying one of the earliest known players in the establishment of apicobasal polarity. Slam is further shown to regulate the localization of junctional components like Arm/β-catenin and Dlt.
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Dev. Cell
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Lecuit, T.1
Samanta, R.2
Wieschaus, E.3
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0036671017
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Slow as molasses is required for polarized membrane growth and germ cell migration in Drosophila
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Stein J.A., Broihier H.T., Moore L.A., Lehmann R. Slow as molasses is required for polarized membrane growth and germ cell migration in Drosophila. Development. 129:2002;3925-3934.
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Stein, J.A.1
Broihier, H.T.2
Moore, L.A.3
Lehmann, R.4
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0033582916
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Discs lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity
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Bhat M.A., Izaddoost S., Lu Y., Cho K.O., Choi K.W., Bellen H.J. Discs lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity. Cell. 96:1999;833-845.
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Bhat, M.A.1
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Lu, Y.3
Cho, K.O.4
Choi, K.W.5
Bellen, H.J.6
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28
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0032487494
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An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
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Izumi Y., Hirose T., Tamai Y., Hirai S., Nagashima Y., Fujimoto T., Tabuse Y., Kemphues K.J., Ohno S. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143:1998;95-106.
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Izumi, Y.1
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Nagashima, Y.5
Fujimoto, T.6
Tabuse, Y.7
Kemphues, K.J.8
Ohno, S.9
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29
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0034253536
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The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
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Joberty G., Petersen C., Gao L., Macara I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2:2000;531-539.
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Joberty, G.1
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30
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0036156362
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Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
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Musch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E., Brennwald P.J. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol. Biol. Cell. 13:2002;158-168.
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Musch, A.1
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Nelson, W.J.4
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Brennwald, P.J.6
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31
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0037456847
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Links between signal transduction, transcription and adhesion in epithelial bud development
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Jamora C., DasGupta R., Kocieniewski P., Fuchs E. Links between signal transduction, transcription and adhesion in epithelial bud development. Nature. 422:2003;317-322.
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Nature
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Jamora, C.1
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0029993728
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LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
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33
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0032544565
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The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
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Kaech S.M., Whitfield C.W., Kim S.K. The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell. 94:1998;761-771.
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Amsler K., Kuwada S.K. Membrane receptor location defines receptor interaction with signaling proteins in a polarized epithelium. Am. J. Physiol. 276:1999;C91-C101.
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Localization and modulation of ErbB receptor tyrosine kinases
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Carraway K.L. III, Sweeney C. Localization and modulation of ErbB receptor tyrosine kinases. Curr. Opin. Cell Biol. 13:2001;125-130.
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36
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0037456842
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Segregation of receptor and ligand regulates activation of epithelial growth factor receptor
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In this study of differentiated airway epithelia, the authors show that the ligand heregulin-a is secreted into the apical extracellular space while its (inactive) receptors are confined to the basolateral membrane below the TJ. When the epithelium is mechanically disrupted or the paracellular permeability increased, apical ligands can access and activate the basolateral receptors. These experiments demonstrate that segregation of ligand and receptor to opposite sides of the TJ-mediated paracellular diffusion barrier can regulate cell-cell signalling events.
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Vermeer P.D., Einwalter L.A., Moninger T.O., Rokhlina T., Kern J.A., Zabner J., Welsh M.J. Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. Nature. 422:2003;322-326 In this study of differentiated airway epithelia, the authors show that the ligand heregulin-a is secreted into the apical extracellular space while its (inactive) receptors are confined to the basolateral membrane below the TJ. When the epithelium is mechanically disrupted or the paracellular permeability increased, apical ligands can access and activate the basolateral receptors. These experiments demonstrate that segregation of ligand and receptor to opposite sides of the TJ-mediated paracellular diffusion barrier can regulate cell-cell signalling events.
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(2003)
Nature
, vol.422
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Vermeer, P.D.1
Einwalter, L.A.2
Moninger, T.O.3
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Kern, J.A.5
Zabner, J.6
Welsh, M.J.7
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37
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0038780624
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Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA
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This report demonstrates that the Helicobacter pylori Cag A protein recruits the junctional proteins ZO-1 and JAM to sites of bacterial attachment in polarized MDCK cell cultures. Among other findings, H. pylori infection of MDCK epithelia is shown to increase paracellular permeability and cause dysplastic cell shapes in a CagA-dependent manner.
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Amieva M.R., Vogelmann R., Covacci A., Tompkins L.S., Nelson W.J., Falkow S. Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA. Science. 300:2003;1430-1434 This report demonstrates that the Helicobacter pylori Cag A protein recruits the junctional proteins ZO-1 and JAM to sites of bacterial attachment in polarized MDCK cell cultures. Among other findings, H. pylori infection of MDCK epithelia is shown to increase paracellular permeability and cause dysplastic cell shapes in a CagA-dependent manner.
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(2003)
Science
, vol.300
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Amieva, M.R.1
Vogelmann, R.2
Covacci, A.3
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38
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Tumor suppressors: Linking cell polarity and growth control
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Wodarz A. Tumor suppressors: linking cell polarity and growth control. Curr. Biol. 10:2000;R624-R626.
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Wodarz, A.1
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