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Volumn 13, Issue 17, 2008, Pages 6520-6536

Regulation of epithelial and endothelial junctions by PAR proteins

Author keywords

Cell polarity; Cell Cell Contacts; Epithelial Cells; JAM; Membrane Asymmetry; PAR proteins; Review; Tight Junctions

Indexed keywords

VERTEBRATA;

EID: 52049125202     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3172     Document Type: Article
Times cited : (19)

References (153)
  • 1
    • 0037452071 scopus 로고    scopus 로고
    • Adaptation of core mechanisms to generate cell polarity
    • DOI 10.1038/nature01602
    • W. J. Nelson: Adaptation of core mechanisms to generate cell polarity. Nature 422, 766-774 (2003) (Pubitemid 36514120)
    • (2003) Nature , vol.422 , Issue.6933 , pp. 766-774
    • Nelson, W.J.1
  • 3
    • 0034599992 scopus 로고    scopus 로고
    • Pores in the wall: Claudins constitute tight junction strands containing aqueous pores
    • DOI 10.1083/jcb.149.1.13
    • S. Tsukita and M. Furuse: Pores in the wall: claudins constitute tight junction strands containing aqueous pores. J Cell Biol 149, 13-16 (2000) (Pubitemid 30196694)
    • (2000) Journal of Cell Biology , vol.149 , Issue.1 , pp. 13-16
    • Tsukita, S.1    Furuse, M.2
  • 4
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • C. M. Van Itallie and J. M. Anderson: Claudins and Epithelial Paracellular Transport. Annu Rev Physiol 68, 403-429 (2006)
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 5
    • 34249732713 scopus 로고    scopus 로고
    • Epithelial tight junctions, gene expression and nucleo-junctional interplay
    • DOI 10.1242/jcs.005975
    • K. Matter and M. S. Balda: Epithelial tight junctions, gene expression and nucleo-junctional interplay. J Cell Sci 120, 1505-1511 (2007) (Pubitemid 46831780)
    • (2007) Journal of Cell Science , vol.120 , Issue.9 , pp. 1505-1511
    • Matter, K.1    Balda, M.S.2
  • 6
    • 0031918158 scopus 로고    scopus 로고
    • Role of tight junctions in establishing and maintaining cell polarity
    • DOI 10.1146/annurev.physiol.60.1.161
    • M. Cereijido, J. Valdes, L. Shoshani and R. G. Contreras: Role of tight junctions in establishing and maintaining cell polarity. Annu Rev Physiol 60, 161-177 (1998) (Pubitemid 28157869)
    • (1998) Annual Review of Physiology , vol.60 , pp. 161-177
    • Cereijido, M.1    Valdes, J.2    Shoshani, L.3    Contreras, R.G.4
  • 7
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • DOI 10.1083/jcb.143.1.95
    • Y. Izumi, T. Hirose, Y. Tamai, S. Hirai, Y. Nagashima, T. Fujimoto, Y. Tabuse, K. J. Kemphues and S. Ohno: 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, 95-106 (1998) (Pubitemid 28480520)
    • (1998) Journal of Cell Biology , vol.143 , Issue.1 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.-I.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 8
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • G. Joberty, C. Petersen, L. Gao and I. G. Macara: The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol 2, 531-539 (2000)
    • (2000) Nat Cell Biol , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    MacAra, I.G.4
  • 9
    • 0030217996 scopus 로고    scopus 로고
    • Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo
    • DOI 10.1016/S0959-437X(96)80061-X
    • S. Guo and K. J. Kemphues: Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo. Curr Opin Genet Dev 6, 408-415 (1996) (Pubitemid 26280792)
    • (1996) Current Opinion in Genetics and Development , vol.6 , Issue.4 , pp. 408-415
    • Guo, S.1    Kemphues, K.J.2
  • 10
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: Lessons in polarity
    • A. Suzuki and S. Ohno: The PAR-aPKC system: lessons in polarity. J Cell Sci 119, 979-987 (2006)
    • (2006) J Cell Sci , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 11
    • 35549001736 scopus 로고    scopus 로고
    • The PAR proteins: Fundamental players in animal cell polarization
    • DOI 10.1016/j.devcel.2007.10.007, PII S1534580707003851
    • B. Goldstein and I. G. Macara: The par proteins: fundamental players in animal cell polarization. Dev Cell 13, 609-622 (2007) (Pubitemid 350011991)
    • (2007) Developmental Cell , vol.13 , Issue.5 , pp. 609-622
    • Goldstein, B.1    Macara, I.G.2
  • 12
    • 0032426346 scopus 로고    scopus 로고
    • Early patterning of the C. elegans embryo
    • DOI 10.1146/annurev.genet.32.1.521
    • L. S. Rose and K. J. Kemphues: Early patterning of the C. elegans embryo. Annu Rev Genet 32, 521-545 (1998) (Pubitemid 29045323)
    • (1998) Annual Review of Genetics , vol.32 , pp. 521-545
    • Rose, L.S.1    Kemphues, K.J.2
  • 13
    • 0031674842 scopus 로고    scopus 로고
    • Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans
    • Y. Tabuse, Y. Izumi, F. Piano, K. J. Kemphues, J. Miwa and S. Ohno: Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development 125, 3607-3614 (1998) (Pubitemid 28469961)
    • (1998) Development , vol.125 , Issue.18 , pp. 3607-3614
    • Tabuse, Y.1    Izumi, Y.2    Piano, F.3    Kemphues, K.J.4    Miwa, J.5    Ohno, S.6
  • 14
    • 0034640089 scopus 로고    scopus 로고
    • PARsing embryonic polarity
    • K. Kemphues: PARsing embryonic polarity. Cell 101, 345-348 (2000)
    • (2000) Cell , vol.101 , pp. 345-348
    • Kemphues, K.1
  • 15
    • 0035141038 scopus 로고    scopus 로고
    • Cell polarity: The PARty expands
    • C. Q. Doe: Cell polarity: the PARty expands. Nat Cell Biol 3, E7-9 (2001)
    • (2001) Nat Cell Biol , vol.3
    • Doe, C.Q.1
  • 16
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • DOI 10.1016/S0955-0674(00)00264-7
    • S. Ohno: Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr Opin Cell Biol 13, 641-648. (2001) (Pubitemid 32817025)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 641-648
    • Ohno, S.1
  • 17
    • 0037032804 scopus 로고    scopus 로고
    • Composition and formation of intercellular junctions in epithelial cells
    • DOI 10.1126/science.1072161
    • E. Knust and O. Bossinger: Composition and formation of intercellular junctions in epithelial cells. Science 298,1955-1959. (2002) (Pubitemid 35425244)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1955-1959
    • Knust, E.1    Bossinger, O.2
  • 18
    • 0037055254 scopus 로고    scopus 로고
    • Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties
    • DOI 10.1016/S0378-1119(02)00681-9, PII S0378111902006819
    • L. Gao, I. G. Macara and G. Joberty: Multiple splice variants of Par3 and of a novel related gene, Par3L,produce proteins with different binding properties. Gene 294, 99-107 (2002) (Pubitemid 35291017)
    • (2002) Gene , vol.294 , Issue.1-2 , pp. 99-107
    • Gao, L.1    Macara, I.G.2    Joberty, G.3
  • 20
    • 0037287298 scopus 로고    scopus 로고
    • Protein kinase C λ/ι (PKCλ/ι: A PKC isotype essential for the development of multicellular organisms
    • DOI 10.1093/jb/mvg018
    • A. Suzuki, K. Akimoto and S. Ohno: Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms. J Biochem(Tokyo) 133, 9-16 (2003) (Pubitemid 36240973)
    • (2003) Journal of Biochemistry , vol.133 , Issue.1 , pp. 9-16
    • Suzuki, A.1    Akimoto, K.2    Ohno, S.3
  • 21
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Cζ (PKCζ): Activation mechanisms and cellular functions
    • DOI 10.1093/jb/mvg017
    • T. Hirai and K. Chida: Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions. J Biochem (Tokyo) 133, 1-7 (2003) (Pubitemid 36240972)
    • (2003) Journal of Biochemistry , vol.133 , Issue.1 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 22
    • 24944577909 scopus 로고    scopus 로고
    • Cdc42 and Par6-PKCη regulate the spatially localized association of Dlg1 and APC to control cell polarization
    • DOI 10.1083/jcb.200412172
    • S. Etienne-Manneville, J. B. Manneville, S. Nicholls, M. A. Ferenczi and A. Hall: Cdc42 and Par6-PKC{zeta} regulate the spatially localized association of Dlg1 and APC to control cell polarization. J Cell Biol 170, 895-901 (2005) (Pubitemid 41306289)
    • (2005) Journal of Cell Biology , vol.170 , Issue.6 , pp. 895-901
    • Etienne-Manneville, S.1    Manneville, J.-B.2    Nicholls, S.3    Ferenczi, M.A.4    Hall, A.5
  • 23
    • 0037385561 scopus 로고    scopus 로고
    • A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl
    • DOI 10.1038/ncb948
    • P. J. Plant, J. P. Fawcett, D. C. Lin, A. D. Holdorf, K. Binns, S. Kulkarni and T. Pawson: A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl. Nat Cell Biol 5, 301-308 (2003) (Pubitemid 36432294)
    • (2003) Nature Cell Biology , vol.5 , Issue.4 , pp. 301-308
    • Plant, P.J.1    Fawcett, J.P.2    Lin, D.C.C.3    Holdorf, A.D.4    Binns, K.5    Kulkarni, S.6    Pawson, T.7
  • 24
    • 0038032917 scopus 로고    scopus 로고
    • Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity
    • DOI 10.1016/S0960-9822(03)00244-6
    • T. Yamanaka, Y. Horikoshi, Y. Sugiyama, C. Ishiyama, A. Suzuki, T. Hirose, A. Iwamatsu, A. Shinohara and S. Ohno: Mammalian Lgl Forms a Protein Complex with PAR-6 and aPKC Independently of PAR-3 to Regulate Epithelial Cell Polarity. Curr Biol 13, 734-743. (2003) (Pubitemid 36531020)
    • (2003) Current Biology , vol.13 , Issue.9 , pp. 734-743
    • Yamanaka, T.1    Horikoshi, Y.2    Sugiyama, Y.3    Ishiyama, C.4    Suzuki, A.5    Hirose, T.6    Iwamatsu, A.7    Shinohara, A.8    Ohno, S.9
  • 25
    • 33750505436 scopus 로고    scopus 로고
    • Par6-aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control
    • DOI 10.1038/ncb1485, PII NCB1485
    • V. Aranda, T. Haire, M. E. Nolan, J. P. Calarco, A. Z. Rosenberg, J. P. Fawcett, T. Pawson and S. K.Muthuswamy: Par6-aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control. Nat Cell Biol 8, 1235-1245 (2006) (Pubitemid 44660588)
    • (2006) Nature Cell Biology , vol.8 , Issue.11 , pp. 1235-1245
    • Aranda, V.1    Haire, T.2    Nolan, M.E.3    Calarco, J.P.4    Rosenberg, A.Z.5    Fawcett, J.P.6    Pawson, T.7    Muthuswamy, S.K.8
  • 26
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signaling and cell polarity
    • D. Lin, A. S. Edwards, J. P. Fawcett, G. Mbamalu, J. D. Scott and T. Pawson: A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signaling and cell polarity. Nat Cell Biol 2, 540-547 (2000)
    • (2000) Nat Cell Biol , vol.2 , pp. 540-547
    • Lin, D.1    Edwards, A.S.2    Fawcett, J.P.3    Mbamalu, G.4    Scott, J.D.5    Pawson, T.6
  • 27
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved PAR protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • DOI 10.1083/jcb.152.6.1183
    • A. Suzuki, T. Yamanaka, T. Hirose, N. Manabe, K. Mizuno, M. Shimizu, K. Akimoto, Y. Izumi, T. Ohnishi and S. Ohno: Atypical protein kinase C is involved in the evolutionary conserved PAR protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol 152, 1183-1196 (2001) (Pubitemid 34280176)
    • (2001) Journal of Cell Biology , vol.152 , Issue.6 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 28
  • 29
    • 0037106581 scopus 로고    scopus 로고
    • APKC kinase activity is required for theasymmetric differentiation of the premature junctional complex during epithelial cell polarization
    • A. Suzuki, C. Ishiyama, K. Hashiba, M. Shimizu, K. Ebnet and S. Ohno: aPKC kinase activity is required for theasymmetric differentiation of the premature junctional complex during epithelial cell polarization. J Cell Sci 115, 3565-3573. (2002)
    • (2002) J Cell Sci , vol.115 , pp. 3565-3573
    • Suzuki, A.1    Ishiyama, C.2    Hashiba, K.3    Shimizu, M.4    Ebnet, K.5    Ohno, S.6
  • 30
    • 0036828968 scopus 로고    scopus 로고
    • Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells
    • DOI 10.1046/j.1365-2443.2002.00590.x
    • Y. Nagai-Tamai, K. Mizuno, T. Hirose, A. Suzuki and S. Ohno: Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells. Genes Cells 7, 1161-1171. (2002) (Pubitemid 35256337)
    • (2002) Genes to Cells , vol.7 , Issue.11 , pp. 1161-1171
    • Nagai-Tamai, Y.1    Mizuno, K.2    Hirose, T.3    Suzuki, A.4    Ohno, S.5
  • 32
    • 33747155076 scopus 로고    scopus 로고
    • ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation
    • DOI 10.1016/j.cell.2006.06.043, PII S0092867406009603
    • K. Umeda, J. Ikenouchi, S. Katahira-Tayama, K. Furuse, H. Sasaki, M. Nakayama, T. Matsui, S. Tsukita andM. Furuse: ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126, 741-754 (2006) (Pubitemid 44233624)
    • (2006) Cell , vol.126 , Issue.4 , pp. 741-754
    • Umeda, K.1    Ikenouchi, J.2    Katahira-Tayama, S.3    Furuse, K.4    Sasaki, H.5    Nakayama, M.6    Matsui, T.7    Tsukita, S.8    Furuse, M.9    Tsukita, S.10
  • 33
    • 23744440058 scopus 로고    scopus 로고
    • Multiple regions of Crumbs3 are required for tight junction formation in MCF10A cells
    • DOI 10.1242/jcs.02412
    • V. C. Fogg, C. J. Liu and B. Margolis: Multiple regions of Crumbs3 are required for tight junction formation in MCF10A cells. J Cell Sci 118, 2859-2869 (2005) (Pubitemid 41136363)
    • (2005) Journal of Cell Science , vol.118 , Issue.13 , pp. 2859-2869
    • Fogg, V.C.1    Liu, C.-J.2    Margolis, B.3
  • 34
    • 0037067320 scopus 로고    scopus 로고
    • HINAd1/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells
    • DOI 10.1074/jbc.M202196200
    • C. Lemmers, E. Medina, M. H. Delgrossi, D. Michel, J. P. Arsanto and A. Le Bivic: hINADl/PATJ, a homolog ofdiscs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells. J Biol Chem 277, 25408-25415. (2002) (Pubitemid 34951853)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25408-25415
    • Lemmers, C.1    Medina, E.2    Delgrossi, M.-H.3    Michel, D.4    Arsanto, J.-P.5    Le Bivic, A.6
  • 36
    • 26244441572 scopus 로고    scopus 로고
    • PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells
    • DOI 10.1242/jcs.02528
    • D. Michel, J. P. Arsanto, D. Massey-Harroche, C. Beclin, J. Wijnholds and A. Le Bivic: PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells. J Cell Sci 118, 4049-4057 (2005) (Pubitemid 41410286)
    • (2005) Journal of Cell Science , vol.118 , Issue.17 , pp. 4049-4057
    • Michel, D.1    Arsanto, J.-P.2    Massey-Harroche, D.3    Beclin, C.4    Wijnholds, J.5    Le Bivic, A.6
  • 37
    • 0041669430 scopus 로고    scopus 로고
    • The Crumbs3-Pals1 complex participates in the establishment of polarity in mammalian epithelial cells
    • DOI 10.1242/jcs.00500
    • M. H. Roh, S. Fan, C. J. Liu and B. Margolis: The Crumbs3-Pals1 complex participates in the establishment of polarity in mammalian epithelial cells. J Cell Sci 116, 2895-2906 (2003) (Pubitemid 36926979)
    • (2003) Journal of Cell Science , vol.116 , Issue.14 , pp. 2895-2906
    • Roh, M.H.1    Fan, S.2    Liu, C.-J.3    Margolis, B.4
  • 38
    • 14744275517 scopus 로고    scopus 로고
    • PATJ regulates tight junction formation and polarity in mammalian epithelial cells
    • DOI 10.1083/jcb.200408064
    • K. Shin, S. Straight and B. Margolis: PATJ regulates tight junction formation and polarity in mammalian epithelial cells. J Cell Biol 168, 705-711 (2005) (Pubitemid 40328155)
    • (2005) Journal of Cell Biology , vol.168 , Issue.5 , pp. 705-711
    • Shin, K.1    Straight, S.2    Margolis, B.3
  • 40
    • 0029045343 scopus 로고
    • Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila
    • A. Wodarz, U. Hinz, M. Engelbert and E. Knust: Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila. Cell 82, 67-76 (1995)
    • (1995) Cell , vol.82 , pp. 67-76
    • Wodarz, A.1    Hinz, U.2    Engelbert, M.3    Knust, E.4
  • 41
    • 0022569860 scopus 로고
    • A functional assay for proteins involved in establishing and epithelial occluding barrier: Identification of a uvomorulin-like polypeptide
    • B. Gumbiner and K. Simons: A functional assay for proteins involved in establishing an epithelial occluding barrier: identification of a uvomorulin-like polypeptide. J Cell Biol 102, 457-468 (1986) (Pubitemid 16140806)
    • (1986) Journal of Cell Biology , vol.102 , Issue.2 , pp. 457-468
    • Gumbiner, B.1    Simons, K.2
  • 42
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight junctions is negatively regulated by Par6
    • DOI 10.1016/S0960-9822(01)00663-7, PII S0960982201006637
    • L. Gao, G. Joberty and I. G. Macara: Assembly of epithelial tight junctions is negatively regulated by Par6.Curr Biol 12, 221-225. (2002) (Pubitemid 34122378)
    • (2002) Current Biology , vol.12 , Issue.3 , pp. 221-225
    • Gao, L.1    Joberty, G.2    Macara, I.G.3
  • 43
    • 14744289370 scopus 로고    scopus 로고
    • Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
    • DOI 10.1038/ncb1226
    • X. Chen and I. G. Macara: Par-3 controls tight junction assembly through the Rac exchange factor Tiam1. Nat Cell Biol 7, 262-269 (2005) (Pubitemid 40331127)
    • (2005) Nature Cell Biology , vol.7 , Issue.3 , pp. 262-269
    • Chen, X.1    Macara, I.G.2
  • 44
    • 33644530393 scopus 로고    scopus 로고
    • Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly
    • X. Chen and I. G. Macara: Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly. J Cell Biol 172, 671-678 (2006)
    • (2006) J Cell Biol , vol.172 , pp. 671-678
    • Chen, X.1    MacAra, I.G.2
  • 46
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • DOI 10.1083/jcb.135.6.1899
    • C. L. Adams, W. J. Nelson and S. J. Smith: Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J Cell Biol 135, 1899-1911. (1996) (Pubitemid 27036450)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 47
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between nonpolarized fibroblasts and polarized epithelial cells
    • S. Yonemura, M. Itoh, A. Nagafuchi and S. Tsukita: Cell-to-cell adherens junction formation and actin filament organization: similarities and differences between nonpolarized fibroblasts and polarized epithelial cells. J Cell Sci 108, 127-142 (1995)
    • (1995) J Cell Sci , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 48
    • 0032941962 scopus 로고    scopus 로고
    • Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity
    • DOI 10.1002/(SICI)1097-4652(199905)179:2<115::AID-JCP1>3.0.CO;2-T
    • Y. Ando-Akatsuka, S. Yonemura, M. Itoh, M. Furuse and S. Tsukita: Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity. J Cell Physiol 179, 115-125 (1999) (Pubitemid 29165139)
    • (1999) Journal of Cellular Physiology , vol.179 , Issue.2 , pp. 115-125
    • Ando-Akatsuka, Y.1    Yonemura, S.2    Itoh, M.3    Furuse, M.4    Tsukita, S.5
  • 49
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • H. McNeill, T. A. Ryan, S. J. Smith and W. J. Nelson: Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J Cell Biol 120, 1217-1226 (1993) (Pubitemid 23064176)
    • (1993) Journal of Cell Biology , vol.120 , Issue.5 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 50
    • 0032753450 scopus 로고    scopus 로고
    • Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells
    • T. Asakura, H. Nakanishi, T. Sakisaka, K. Takahashi, K. Mandai, M. Nishimura, T. Sasaki and Y. Takai: Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells. Genes Cells 4, 573-581. (1999)
    • (1999) Genes Cells , vol.4 , pp. 573-581
    • Asakura, T.1    Nakanishi, H.2    Sakisaka, T.3    Takahashi, K.4    Mandai, K.5    Nishimura, M.6    Sasaki, T.7    Takai, Y.8
  • 51
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • DOI 10.1093/emboj/20.14.3738
    • K. Ebnet, A. Suzuki, Y. Horikoshi, T. Hirose, M. K. Meyer Zu Brickwedde, S. Ohno and D. Vestweber: Thecell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). Embo J 20, 3738-3748 (2001) (Pubitemid 32691785)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3738-3748
    • Ebnet, K.1    Suzuki, A.2    Horikoshi, Y.3    Hirose, T.4    Meyer Zu Brickwedde, M.-K.5    Ohno, S.6    Vestweber, D.7
  • 52
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • C. Yeaman, K. K. Grindstaff and W. J. Nelson: New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol Rev 79, 73-98 (1999) (Pubitemid 29056949)
    • (1999) Physiological Reviews , vol.79 , Issue.1 , pp. 73-98
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 54
    • 0037458707 scopus 로고    scopus 로고
    • Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse
    • DOI 10.1074/jbc.C200707200
    • K. Takekuni, W. Ikeda, T. Fujito, K. Morimoto, M. Takeuchi, M. Monden and Y. Takai: Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. J Biol Chem 278, 5497-5500 (2003) (Pubitemid 36800787)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5497-5500
    • Takekuni, K.1    Ikeda, W.2    Fujito, T.3    Morimoto, K.4    Takeuchi, M.5    Monden, M.6    Takai, Y.7
  • 55
    • 33748592841 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A participates in the formation of apico-basal polarity through different domains
    • DOI 10.1016/j.yexcr.2006.07.004, PII S0014482706002825
    • D. Rehder, S. Iden, I. Nasdala, J. Wegener, M. K. Brickwedde, D. Vestweber and K. Ebnet: Junctional adhesion molecule-A participates in the formation of apicobasal polarity through different domains. Exp Cell Res 312, 3389-3403 (2006) (Pubitemid 44380238)
    • (2006) Experimental Cell Research , vol.312 , Issue.17 , pp. 3389-3403
    • Rehder, D.1    Iden, S.2    Nasdala, I.3    Wegener, J.4    Brickwedde, M.-K.M.Z.5    Vestweber, D.6    Ebnet, K.7
  • 56
    • 0033790539 scopus 로고    scopus 로고
    • The mammalian homologue of the caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases cdc42 and rac1
    • A. Johansson, M. Driessens and P. Aspenstrom: The mammalian homologue of the caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases cdc42 and rac1. J Cell Sci 113, 3267-3275 (2000)
    • (2000) J Cell Sci , vol.113 , pp. 3267-3275
    • Johansson, A.1    Driessens, M.2    Aspenstrom, P.3
  • 57
    • 0035070099 scopus 로고    scopus 로고
    • Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C
    • DOI 10.1046/j.1365-2443.2001.00404.x
    • Y. Noda, R. Takeya, S. Ohno, S. Naito, T. Ito and H. Sumimoto: Human homologues of the Caenorhabditiselegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells 6, 107-119. (2001) (Pubitemid 32266488)
    • (2001) Genes to Cells , vol.6 , Issue.2 , pp. 107-119
    • Noda, Y.1    Takeya, R.2    Ohno, S.3    Naito, S.4    Ito, T.5    Sumimoto, H.6
  • 58
    • 0034659420 scopus 로고    scopus 로고
    • A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCζ signaling and cell transformation
    • DOI 10.1016/S0960-9822(00)00535-2
    • R. G. Qiu, A. Abo and G. S. Martin: A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation. Curr Biol 10, 697-707 (2000) (Pubitemid 30437942)
    • (2000) Current Biology , vol.10 , Issue.12 , pp. 697-707
    • Qiu, R.-G.1    Abo, A.2    Martin, G.S.3
  • 59
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
    • DOI 10.1093/emboj/cdg110
    • S. M. Garrard, C. T. Capaldo, L. Gao, M. K. Rosen, I. G. Macara and D. R. Tomchick: Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. Embo J 22, 1125-1133 (2003) (Pubitemid 36313596)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1125-1133
    • Garrard, S.M.1    Capaldo, C.T.2    Gao, L.3    Rosen, M.K.4    Macara, I.G.5    Tomchick, D.R.6
  • 60
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • DOI 10.1016/S1097-2765(04)00086-3, PII S1097276504000863
    • F. C. Peterson, R. R. Penkert, B. F. Volkman and K. E. Prehoda: Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Mol Cell 13, 665-676 (2004) (Pubitemid 38368124)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4
  • 61
    • 0037020084 scopus 로고    scopus 로고
    • Rac activation upon cell-cell contact formation is dependent on signaling from the epidermal growth factor receptor
    • M. Betson, E. Lozano, J. Zhang and V. M. Braga: Rac activation upon cell-cell contact formation is dependent on signaling from the epidermal growth factor receptor. J Biol Chem 277, 36962-36969 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 36962-36969
    • Betson, M.1    Lozano, E.2    Zhang, J.3    Braga, V.M.4
  • 62
    • 0037155159 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts
    • DOI 10.1074/jbc.M109640200
    • E. M. Kovacs, R. G. Ali, A. J. McCormack and A. S. Yap: E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts. J Biol Chem 277, 6708-6718 (2002) (Pubitemid 34968474)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6708-6718
    • Kovacs, E.M.1    Ali, R.G.2    McCormack, A.J.3    Yap, A.S.4
  • 63
    • 0034994490 scopus 로고    scopus 로고
    • Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites
    • M. Nakagawa, M. Fukata, M. Yamaga, N. Itoh and K. Kaibuchi: Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites. J Cell Sci 114, 1829-1838 (2001) (Pubitemid 32530038)
    • (2001) Journal of Cell Science , vol.114 , Issue.10 , pp. 1829-1838
    • Nakagawa, M.1    Fukata, M.2    Yamaga, M.3    Itoh, N.4    Kaibuchi, K.5
  • 64
  • 65
    • 0036696823 scopus 로고    scopus 로고
    • Spatiotemporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion
    • J. S. Ehrlich, M. D. Hansen and W. J. Nelson: Spatiotemporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion. Dev Cell 3, 259-270 (2002)
    • (2002) Dev Cell , vol.3 , pp. 259-270
    • Ehrlich, J.S.1    Hansen, M.D.2    Nelson, W.J.3
  • 66
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • DOI 10.1083/jcb.200701058
    • S. Yamada and W. J. Nelson: Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J Cell Biol 178, 517-527 (2007) (Pubitemid 47196158)
    • (2007) Journal of Cell Biology , vol.178 , Issue.3 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 67
    • 25444486668 scopus 로고    scopus 로고
    • The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
    • DOI 10.1083/jcb.200502129
    • A. E. Mertens, T. P. Rygiel, C. Olivo, R. van der Kammen and J. G. Collard: The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. J Cell Biol 170, 1029-1037 (2005) (Pubitemid 41362635)
    • (2005) Journal of Cell Biology , vol.170 , Issue.7 , pp. 1029-1037
    • Mertens, A.E.E.1    Rygiel, T.P.2    Olivo, C.3    Van Der Kammen, R.4    Collard, J.G.5
  • 68
    • 0012229963 scopus 로고    scopus 로고
    • Trans-interactions of nectins induce formation of Filopodia and Lamellipodia through the respective activation of Cdc42 and Rac small G proteins
    • T. Kawakatsu, K. Shimizu, T. Honda, T. Fukuhara, T. Hoshino and Y. Takai: Trans-interactions of nectins induce formation of Filopodia and Lamellipodia through the respective activation of Cdc42 and Rac small G proteins. J Biol Chem 11, 11 (2002)
    • (2002) J Biol Chem , vol.11 , pp. 11
    • Kawakatsu, T.1    Shimizu, K.2    Honda, T.3    Fukuhara, T.4    Hoshino, T.5    Takai, Y.6
  • 69
    • 0345967824 scopus 로고    scopus 로고
    • Involvement of nectin-activated Cdc42 small G protein in organization of adherens and tight junctions in madin-darby canine kidney cells
    • DOI 10.1074/jbc.M308015200
    • A. Fukuhara, K. Shimizu, T. Kawakatsu, T. Fukuhara and Y. Takai: Involvement of nectin-activated Cdc42 small G protein in organization of adherens and tight junctions in Madin-Darby canine kidney cells. J Biol Chem 278, 51885-51893 (2003) (Pubitemid 38020435)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51885-51893
    • Fukuhara, A.1    Shimizu, K.2    Kawakatsu, T.3    Fukuhara, T.4    Takai, Y.5
  • 72
    • 14044273991 scopus 로고    scopus 로고
    • Vav2 as a Rac-GDP/GTP exchange factor responsible for the nectin-induced, c-Src- and Cdc42-mediated activation of Rac
    • DOI 10.1074/jbc.M408710200
    • T. Kawakatsu, H. Ogita, T. Fukuhara, T. Fukuyama, Y. Minami, K. Shimizu and Y. Takai: Vav2 as a Rac- GDP/GTP exchange factor responsible for the nectininduced, c-Src- and Cdc42-mediated activation of Rac. J Biol Chem 280, 4940-4947 (2005) (Pubitemid 40288669)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4940-4947
    • Kawakatsu, T.1    Ogita, H.2    Fukuhara, T.3    Fukuyama, T.4    Minami, Y.5    Shimizu, K.6    Takai, Y.7
  • 74
    • 33645747414 scopus 로고    scopus 로고
    • Claudins in occluding junctions of humans and flies
    • M. Furuse and S. Tsukita: Claudins in occluding junctions of humans and flies. Trends Cell Biol 16, 181-188 (2006)
    • (2006) Trends Cell Biol , vol.16 , pp. 181-188
    • Furuse, M.1    Tsukita, S.2
  • 75
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • DOI 10.1083/jcb.137.6.1393
    • A. Sakakibara, M. Furuse, M. Saitou, Y. Ando- Akatsuka and S. Tsukita: Possible involvement of phosphorylation of occludin in tight junction formation. J Cell Biol 137, 1393-1401 (1997) (Pubitemid 27265950)
    • (1997) Journal of Cell Biology , vol.137 , Issue.6 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 76
    • 0035914359 scopus 로고    scopus 로고
    • Protein kinase C regulates the phosphorylation and cellular localization of occludin
    • A. Y. Andreeva, E. Krause, E. C. Muller, I. E. Blasig and D. I. Utepbergenov: Protein kinase C regulates the phosphorylation and cellular localization of occludin. J Biol Chem 276, 38480-38486 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 38480-38486
    • Andreeva, A.Y.1    Krause, E.2    Muller, E.C.3    Blasig, I.E.4    Utepbergenov, D.I.5
  • 77
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • DOI 10.1074/jbc.M610597200
    • A. Seth, P. Sheth, B. C. Elias and R. Rao: Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J Biol Chem 282, 11487-11498 (2007) (Pubitemid 47100808)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3    Rao, R.4
  • 78
    • 33744544786 scopus 로고    scopus 로고
    • Phosphorylation of paracellin-1 at Ser217 by protein kinase A is essential for localization in tight junctions
    • DOI 10.1242/jcs.02901
    • A. Ikari, S. Matsumoto, H. Harada, K. Takagi, H. Hayashi, Y. Suzuki, M. Degawa and M. Miwa: Phosphorylation of paracellin-1 at Ser217 by protein kinase A is essential for localization in tight junctions. J Cell Sci 119, 1781-1789 (2006) (Pubitemid 43811004)
    • (2006) Journal of Cell Science , vol.119 , Issue.9 , pp. 1781-1789
    • Ikari, A.1    Matsumoto, S.2    Harada, H.3    Takagi, K.4    Hayashi, H.5    Suzuki, Y.6    Degawa, M.7    Miwa, M.8
  • 79
    • 34548023972 scopus 로고    scopus 로고
    • Phosphorylation of claudin-4 by PKCε regulates tight junction barrier function in ovarian cancer cells
    • DOI 10.1016/j.yexcr.2007.06.026, PII S0014482707003163
    • T. D'Souza, F. E. Indig and P. J. Morin: Phosphorylation of claudin-4 by PKCepsilon regulates tight junction barrier function in ovarian cancer cells. Exp Cell Res 313, 3364-3375 (2007) (Pubitemid 47284066)
    • (2007) Experimental Cell Research , vol.313 , Issue.15 , pp. 3364-3375
    • D'Souza, T.1    Indig, F.E.2    Morin, P.J.3
  • 80
    • 33746637520 scopus 로고    scopus 로고
    • Cingulin regulates claudin-2 expression and cell proliferation through the small GTPase RhoA
    • DOI 10.1091/mbc.E06-02-0122
    • L. Guillemot and S. Citi: Cingulin regulates claudin-2 expression and cell proliferation through the small GTPase RhoA. Mol Biol Cell 17, 3569-3577 (2006) (Pubitemid 44156449)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.8 , pp. 3569-3577
    • Guillemot, L.1    Citi, S.2
  • 81
    • 9444239778 scopus 로고    scopus 로고
    • Disruption of the cingulin gene does not prevent tight junction formation but alters gene expression
    • DOI 10.1242/jcs.01399
    • L. Guillemot, E. Hammar, C. Kaister, J. Ritz, D. Caille, L. Jond, C. Bauer, P. Meda and S. Citi: Disruption of the cingulin gene does not prevent tight junction formation but alters gene expression. J Cell Sci 117, 5245-5256 (2004) (Pubitemid 39562487)
    • (2004) Journal of Cell Science , vol.117 , Issue.22 , pp. 5245-5256
    • Guillemot, L.1    Hammar, E.2    Kaister, C.3    Ritz, J.4    Caille, D.5    Jond, L.6    Bauer, C.7    Meda, P.8    Citi, S.9
  • 82
    • 0036774217 scopus 로고    scopus 로고
    • Cell-cell adhesion and signaling
    • V. M. Braga: Cell-cell adhesion and signaling. Curr Opin Cell Biol 14, 546-556 (2002)
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 546-556
    • Braga, V.M.1
  • 83
    • 33750459738 scopus 로고    scopus 로고
    • Catenins: Keeping cells from getting their signals crossed
    • DOI 10.1016/j.devcel.2006.10.010, PII S153458070600462X
    • M. Perez-Moreno and E. Fuchs: Catenins: keeping cells from getting their signals crossed. Dev Cell 11, 601-612 (2006) (Pubitemid 44644972)
    • (2006) Developmental Cell , vol.11 , Issue.5 , pp. 601-612
    • Perez-Moreno, M.1    Fuchs, E.2
  • 84
    • 0037416129 scopus 로고    scopus 로고
    • Identification of a tight junction-associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability
    • DOI 10.1083/jcb.200211047
    • G. Benais-Pont, A. Punn, C. Flores-Maldonado, J. Eckert, G. Raposo, T. P. Fleming, M. Cereijido, M. S. Balda and K. Matter: Identification of a tight junctionassociated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability. J Cell Biol 160, 729-740 (2003) (Pubitemid 36298268)
    • (2003) Journal of Cell Biology , vol.160 , Issue.5 , pp. 729-740
    • Benais-Pont, G.1    Punn, A.2    Flores-Maldonado, C.3    Eckert, J.4    Raposo, G.5    Fleming, T.P.6    Cereijido, M.7    Balda, M.S.8    Matter, K.9
  • 85
    • 24644480749 scopus 로고    scopus 로고
    • Molecular requirements for epithelial-mesenchymal transition during tumor progression
    • DOI 10.1016/j.ceb.2005.08.001, PII S0955067405001043
    • M. A. Huber, N. Kraut and H. Beug: Molecular requirements for epithelial-mesenchymal transitionduring tumor progression. Curr Opin Cell Biol 17, 548-558 (2005) (Pubitemid 41267170)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.5 , pp. 548-558
    • Huber, M.A.1    Kraut, N.2    Beug, H.3
  • 87
    • 14844364701 scopus 로고    scopus 로고
    • Regulation of the polarity protein Par6 by TGFβ receptors controls epithelial cell plasticity
    • DOI 10.1126/science.1105718
    • B. Ozdamar, R. Bose, M. Barrios-Rodiles, H. R. Wang, Y. Zhang and J. L. Wrana: Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity. Science 307, 1603-1609 (2005) (Pubitemid 40354739)
    • (2005) Science , vol.307 , Issue.5715 , pp. 1603-1609
    • Ozdamar, B.1    Bose, R.2    Barrios-Rodiles, M.3    Wang, H.-R.4    Zhang, Y.5    Wrana, J.L.6
  • 88
    • 34447102014 scopus 로고    scopus 로고
    • Polarity regulators and the control of epithelial architecture, cell migration, and tumorigenesis
    • DOI 10.1016/S0074-7696(07)62006-3, PII S0074769607620063, A Survey of Cell Biology
    • L. E. Dow and P. O. Humbert: Polarity regulators and the control of epithelial architecture, cell migration, and tumorigenesis. Int Rev Cytol 262, 253-302 (2007) (Pubitemid 47031311)
    • (2007) International Review of Cytology , vol.262 , pp. 253-302
    • Dow, L.E.1    Humbert, P.O.2
  • 89
    • 33751347857 scopus 로고    scopus 로고
    • The Scribble and Par complexes in polarity and migration: Friends or foes?
    • DOI 10.1016/j.tcb.2006.10.005, PII S0962892406002753
    • P. O. Humbert, L. E. Dow and S. M. Russell: The Scribble and Par complexes in polarity and migration: friends or foes? Trends Cell Biol 16, 622-630 (2006) (Pubitemid 44809887)
    • (2006) Trends in Cell Biology , vol.16 , Issue.12 , pp. 622-630
    • Humbert, P.O.1    Dow, L.E.2    Russell, S.M.3
  • 90
    • 33748923940 scopus 로고    scopus 로고
    • Scribble associates with two polarity proteins, Lgl2 and Vangl2, via distinct molecular domains
    • DOI 10.1002/jcb.20992
    • L. M. Kallay, A. McNickle, P. J. Brennwald, A. L. Hubbard and L. T. Braiterman: Scribble associates with two polarity proteins, Lgl2 and Vangl2, via distinct molecular domains. J Cell Biochem 99, 647-664 (2006) (Pubitemid 44435580)
    • (2006) Journal of Cellular Biochemistry , vol.99 , Issue.2 , pp. 647-664
    • Kallay, L.M.1    McNickle, A.2    Brennwald, P.J.3    Hubbard, A.L.4    Braiterman, L.T.5
  • 91
    • 4043170088 scopus 로고    scopus 로고
    • Epithelial polarity and proliferation control: Links from the Drosophila neoplastictumor suppressors
    • DOI 10.1101/gad.1211604
    • D. Bilder: Epithelial polarity and proliferation control: links from the Drosophila neoplastic tumor suppressors. Genes Dev 18, 1909-1925 (2004) (Pubitemid 39071572)
    • (2004) Genes and Development , vol.18 , Issue.16 , pp. 1909-1925
    • Bilder, D.1
  • 92
    • 29144469472 scopus 로고    scopus 로고
    • The mammalian Scribble polarity protein regulates epithelial cell adhesion and migration through E-cadherin
    • DOI 10.1083/jcb.200506094
    • Y. Qin, C. Capaldo, B. M. Gumbiner and I. G. Macara: The mammalian Scribble polarity protein regulates epithelial cell adhesion and migration through E-cadherin. J Cell Biol 171, 1061-1071 (2005) (Pubitemid 41815837)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 1061-1071
    • Qin, Y.1    Capaldo, C.2    Gumbiner, B.M.3    Macara, I.G.4
  • 93
    • 34248143390 scopus 로고    scopus 로고
    • The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation
    • DOI 10.1091/mbc.E06-11-0980
    • V. M. Stucke, E. Timmerman, J. Vandekerckhove, K. Gevaert and A. Hall: The MAGUK protein MPP7 binds tothe polarity protein hDlg1 and facilitates epithelial tight junction formation. Mol Biol Cell 18, 1744-1755 (2007) (Pubitemid 46717556)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1744-1755
    • Stucke, V.M.1    Timmerman, E.2    Vandekerckhove, J.3    Gevaert, K.4    Hall, A.5
  • 94
    • 0037434790 scopus 로고    scopus 로고
    • Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity
    • DOI 10.1038/nature01423
    • S. Etienne-Manneville and A. Hall: Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature 421, 753-756 (2003) (Pubitemid 36227627)
    • (2003) Nature , vol.421 , Issue.6924 , pp. 753-756
    • Etienne-Manneville, S.1    Hall, A.2
  • 95
    • 7044245710 scopus 로고    scopus 로고
    • Par6α signaling controls glial-guided neuronal migration
    • DOI 10.1038/nn1332
    • D. J. Solecki, L. Model, J. Gaetz, T. M. Kapoor and M. E. Hatten: Par6alpha signaling controls glial-guided neuronal migration. Nat Neurosci 7, 1195-1203 (2004) (Pubitemid 39426239)
    • (2004) Nature Neuroscience , vol.7 , Issue.11 , pp. 1195-1203
    • Solecki, D.J.1    Model, L.2    Gaetz, J.3    Kapoor, T.M.4    Hatten, M.E.5
  • 96
    • 34547811037 scopus 로고    scopus 로고
    • Polarity proteins PAR6 and aPKC regulate cell death through GSK-3β in 3D epithelial morphogenesis
    • DOI 10.1242/jcs.007443
    • M. Kim, A. Datta, P. Brakeman, W. Yu and K. E. Mostov: Polarity proteins PAR6 and aPKC regulate cell death through GSK-3beta in 3D epithelial morphogenesis. J Cell Sci 120, 2309-2317 (2007) (Pubitemid 47225934)
    • (2007) Journal of Cell Science , vol.120 , Issue.14 , pp. 2309-2317
    • Kim, M.1    Datta, A.2    Brakeman, P.3    Yu, W.4    Mostov, K.E.5
  • 97
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epthelial tight junction assembly
    • DOI 10.1038/ncb923
    • T. W. Hurd, L. Gao, M. H. Roh, I. G. Macara and B. Margolis: Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat Cell Biol 5, 137-142 (2003) (Pubitemid 36210848)
    • (2003) Nature Cell Biology , vol.5 , Issue.2 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    Macara, I.G.4    Margolis, B.5
  • 98
    • 7544232779 scopus 로고    scopus 로고
    • Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex
    • DOI 10.1038/nsmb839
    • R. R. Penkert, H. M. DiVittorio and K. E. Prehoda: Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex. Nat Struct Mol Biol 11, 1122-1127 (2004) (Pubitemid 39453342)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.11 , pp. 1122-1127
    • Penkert, R.R.1    DiVittorio, H.M.2    Prehoda, K.E.3
  • 99
    • 3142757182 scopus 로고    scopus 로고
    • Tight junction protein Par6 interacts with an evolutionarily conserved region in the amino terminus of PALS1/stardust
    • DOI 10.1074/jbc.M401930200
    • Q. Wang, T. W. Hurd and B. Margolis: Tight Junction Protein Par6 Interacts with an Evolutionarily Conserved Region in the Amino Terminus of PALS1/Stardust. J Biol Chem 279, 30715-30721 (2004) (Pubitemid 38938004)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30715-30721
    • Wang, Q.1    Hurd, T.W.2    Margolis, B.3
  • 100
    • 4143119015 scopus 로고    scopus 로고
    • DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila
    • S. Sotillos, M. T. Diaz-Meco, E. Caminero, J. Moscat and S. Campuzano: DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila. J Cell Biol (2004)
    • (2004) J Cell Biol
    • Sotillos, S.1    Diaz-Meco, M.T.2    Caminero, E.3    Moscat, J.4    Campuzano, S.5
  • 101
    • 33745217610 scopus 로고    scopus 로고
    • Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity
    • DOI 10.1242/jcs.02938
    • T. Yamanaka, Y. Horikoshi, N. Izumi, A. Suzuki, K. Mizuno and S. Ohno: Lgl mediates apical domaindisassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity. J Cell Sci 119, 2107-2118 (2006) (Pubitemid 43904965)
    • (2006) Journal of Cell Science , vol.119 , Issue.10 , pp. 2107-2118
    • Yamanaka, T.1    Horikoshi, Y.2    Izumi, N.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 102
    • 0347596668 scopus 로고    scopus 로고
    • Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells
    • DOI 10.1016/S0092-8674(03)00938-3
    • R. Benton and D. St Johnston: Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells. Cell 115, 691-704 (2003) (Pubitemid 38030298)
    • (2003) Cell , vol.115 , Issue.6 , pp. 691-704
    • Benton, R.1    St Johnston, D.2
  • 103
    • 0344663968 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia
    • DOI 10.1016/j.cub.2003.11.020
    • T. W. Hurd, S. Fan, C. J. Liu, H. K. Kweon, K. Hakansson and B. Margolis: Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia. Curr Biol 13, 2082-2090 (2003) (Pubitemid 37502525)
    • (2003) Current Biology , vol.13 , Issue.23 , pp. 2082-2090
    • Hurd, T.W.1    Fan, S.2    Liu, C.-J.3    Kweon, H.K.4    Hakansson, K.5    Margolis, B.6
  • 104
    • 0041700114 scopus 로고    scopus 로고
    • A conserved oligomerization domain in Drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity
    • DOI 10.1016/S0960-9822(03)00508-6
    • R. Benton and D. St Johnston: A conserved oligomerization domain in drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity. Curr Biol 13, 1330-1334 (2003) (Pubitemid 36953307)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1330-1334
    • Benton, R.1    St. Johnston, D.2
  • 105
    • 0042232080 scopus 로고    scopus 로고
    • Self-association of PAR-3-mediated by the conserved N-terminal domain contributes to the development of epithelial tight junctions
    • DOI 10.1074/jbc.M303593200
    • K. Mizuno, A. Suzuki, T. Hirose, K. Kitamura, Y. Kutsuzawa, M. Futaki, Y. Amano and S. Ohno: Selfassociation of PAR-3 mediated by the conserved Nterminal domain contributes to the development of epithelial tight junctionsr. J Biol Chem 278, 31240-31250 (2003) (Pubitemid 36994641)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31240-31250
    • Mizuno, K.1    Suzuki, A.2    Hirose, T.3    Kitamura, K.4    Kutsuzawa, K.5    Futaki, M.6    Amano, Y.7    Ohno, S.8
  • 106
    • 1942540791 scopus 로고    scopus 로고
    • Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity
    • DOI 10.1016/j.cub.2004.04.007, PII S0960982204002581
    • J. B. Hurov, J. L. Watkins and H. Piwnica-Worms: Atypical PKC Phosphorylates PAR-1 Kinases to Regulate Localization and Activity. Curr Biol 14, 736-741 (2004) (Pubitemid 38503613)
    • (2004) Current Biology , vol.14 , Issue.8 , pp. 736-741
    • Hurov, J.B.1    Watkins, J.L.2    Piwnica-Worms, H.3
  • 108
    • 31744439314 scopus 로고    scopus 로고
    • Stabilization of cell polarity by the C. elegans RING protein PAR-2
    • DOI 10.1016/j.devcel.2005.12.015, PII S1534580706000074
    • Y. Hao, L. Boyd and G. Seydoux: Stabilization of Cell Polarity by the C. elegans RING Protein PAR- 2. Dev Cell 10, 199-208 (2006) (Pubitemid 43174953)
    • (2006) Developmental Cell , vol.10 , Issue.2 , pp. 199-208
    • Hao, Y.1    Boyd, L.2    Seydoux, G.3
  • 109
    • 33746615950 scopus 로고    scopus 로고
    • PAR1b promotes cell-cell adhesion and inhibits dishevelled-mediated transformation of Madin-Darby canine kidney cells
    • DOI 10.1091/mbc.E06-03-0193
    • M. Elbert, D. Cohen and A. Musch: PAR1b promotes cell-cell adhesion and inhibits dishevelledmediated transformation of Madin-Darby canine kidney cells. Mol Biol Cell 17, 3345-3355 (2006) (Pubitemid 44156430)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.8 , pp. 3345-3355
    • Elbert, M.1    Cohen, D.2    Musch, A.3
  • 110
    • 1442358790 scopus 로고    scopus 로고
    • Mammalian PAR-1 determines epithelial lumen polarity by organizing the microtubule cytoskeleton
    • DOI 10.1083/jcb.200308104
    • D. Cohen, P. J. Brennwald, E. Rodriguez-Boulan and A. Musch: Mammalian PAR-1 determines epithelial lumen polarity by organizing the microtubule cytoskeleton. J Cell Biol 164, 717-727 (2004) (Pubitemid 38282955)
    • (2004) Journal of Cell Biology , vol.164 , Issue.5 , pp. 717-727
    • Cohen, D.1    Brennwald, P.J.2    Rodriguez-Boulan, E.3    Musch, A.4
  • 112
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD
    • DOI 10.1016/S0092-8674(04)00114-X, PII S009286740400114X
    • A. F. Baas, J. Kuipers, N. N. van der Wel, E. Batlle, H. K. Koerten, P. J. Peters and H. C. Clevers: Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell 116, 457-466 (2004) (Pubitemid 38366321)
    • (2004) Cell , vol.116 , Issue.3 , pp. 457-466
    • Baas, A.F.1    Kuipers, J.2    Van Der Wel, N.N.3    Batlle, E.4    Koerten, H.K.5    Peters, P.J.6    Clevers, H.C.7
  • 116
    • 0034090975 scopus 로고    scopus 로고
    • The C. elegans par-4 gene encodes a putative serine-threonine kinase required for establishing embryonic asymmetry
    • J. L. Watts, D. G. Morton, J. Bestman and K. J. Kemphues: The C. elegans par-4 gene encodes a putativeserine-threonine kinase required for establishing embryonic asymmetry. Development 127, 1467-1475 (2000) (Pubitemid 30232597)
    • (2000) Development , vol.127 , Issue.7 , pp. 1467-1475
    • Watts, J.L.1    Morton, D.G.2    Bestman, J.3    Kemphuesf, K.J.4
  • 117
    • 0036147620 scopus 로고    scopus 로고
    • The Caenorhabditis elegans par-5 Gene encodes a 14-3-3 protein required for cellular asymmetry in the early embryo
    • DOI 10.1006/dbio.2001.0489
    • D. G. Morton, D. C. Shakes, S. Nugent, D. Dichoso, W. Wang, A. Golden and K. J. Kemphues: The Caenorhabditis elegans par-5 gene encodes a 14-3-3 protein required for cellular asymmetry in the early embryo. Dev Biol 241, 47-58 (2002) (Pubitemid 34066761)
    • (2002) Developmental Biology , vol.241 , Issue.1 , pp. 47-58
    • Morton, D.G.1    Shakes, D.C.2    Nugent, S.3    Dichoso, D.4    Wang, W.5    Golden, A.6    Kemphues, K.J.7
  • 118
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • DOI 10.1242/jcs.01171
    • M. K. Dougherty and D. K. Morrison: Unlocking the code of 14-3-3. J Cell Sci 117, 1875-1884 (2004) (Pubitemid 38745122)
    • (2004) Journal of Cell Science , vol.117 , Issue.10 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 119
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: Happy together
    • DOI 10.1038/nrm1357
    • E. Dejana: Endothelial cell-cell junctions: happy together. Nat Rev Mol Cell Biol 5, 261-270 (2004) (Pubitemid 38480607)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.4 , pp. 261-270
    • Dejana, E.1
  • 120
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: Novel organizers of intracellular junctions
    • DOI 10.1242/jcs.00167
    • Y. Takai and H. Nakanishi: Nectin and afadin: novel organizers of intercellular junctions. J Cell Sci 116, 17-27. (2003) (Pubitemid 36113961)
    • (2003) Journal of Cell Science , vol.116 , Issue.1 , pp. 17-27
    • Takai, Y.1    Nakanishi, H.2
  • 121
    • 0016724876 scopus 로고
    • Segmental differentiations of cell junctions in the vascularendothelium. The microvasculature
    • M. Simionescu, N. Simionescu and G. E. Palade: Segmental differentiations of cell junctions in the vascularendothelium. The microvasculature. J Cell Biol 67, 863-885 (1975)
    • (1975) J Cell Biol , vol.67 , pp. 863-885
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 122
    • 0017229099 scopus 로고
    • Segmental differentiations of cell junctions in the vascular endothelium. Arteries and veins
    • M. Simionescu, N. Simionescu and G. E. Palade: Segmental differentiations of cell junctions in the vascular endothelium. Arteries and veins. J Cell Biol 68, 705-723 (1976)
    • (1976) J Cell Biol , vol.68 , pp. 705-723
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 123
    • 2442631580 scopus 로고    scopus 로고
    • Cell-cell junctions of dermal microvascular endothelial cells contain tight and adherens junction proteins in spatial proximity
    • DOI 10.1021/bi035517c
    • C. Ruffer, A. Strey, A. Janning, K. S. Kim and V. Gerke: Cell-cell junctions of dermal microvascular endothelial cells contain tight and adherens junction proteins in spatial proximity. Biochemistry 43, 5360-5369 (2004) (Pubitemid 38620928)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5360-5369
    • Ruffer, C.1    Strey, A.2    Janning, A.3    Kim, K.S.4    Gerke, V.5
  • 124
    • 2642563866 scopus 로고    scopus 로고
    • Molecular anatomy of interendothelial junctions in human blood-brain barrier microvessels
    • A. W. Vorbrodt and D. H. Dobrogowska: Molecular anatomy of interendothelial junctions in human blood-brain barrier microvessels. Folia Histochem Cytobiol 42, 67-75 (2004) (Pubitemid 38714693)
    • (2004) Folia Histochemica et Cytobiologica , vol.42 , Issue.2 , pp. 67-75
    • Vorbrodt, A.W.1    Dobrogowska, D.H.2
  • 125
    • 12444336848 scopus 로고    scopus 로고
    • The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: A possible role for JAMs in endothelial cell polarity
    • DOI 10.1242/jcs.00704
    • K. Ebnet, M. Aurrand-Lions, A. Kuhn, F. Kiefer, S. Butz, K. Zander, M. K. Meyer Zu Brickwedde, A. Suzuki, B.A. Imhof and D. Vestweber: The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: A possible role for JAMs in endothelial cell polarity. J Cell Sci 116, 3879-3891 (2003) (Pubitemid 37279304)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 3879-3891
    • Ebnet, K.1    Aurrand-Lions, M.2    Kuhn, A.3    Kiefer, F.4    Butz, S.5    Zander, K.6    Meyer Zu Brickwedde, M.-K.7    Suzuki, A.8    Imhof, B.A.9    Vestweber, D.10
  • 128
    • 33846626054 scopus 로고    scopus 로고
    • Regulation of T-cell activation by the cytoskeleton
    • DOI 10.1038/nri2021, PII NRI2021
    • D. D. Billadeau, J. C. Nolz and T. S. Gomez: Regulation of T-cell activation by the cytoskeleton. Nat Rev Immunol 7, 131-143 (2007) (Pubitemid 46174860)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.2 , pp. 131-143
    • Billadeau, D.D.1    Nolz, J.C.2    Gomez, T.S.3
  • 129
    • 27844473354 scopus 로고    scopus 로고
    • A dynamic view of the immunological synapse
    • DOI 10.1016/j.smim.2005.09.002, PII S104453230500076X, Imaging Dynamic Interactions in Immune Responses
    • M. L. Dustin: A dynamic view of the immunological synapse. Semin Immunol 17, 400-410 (2005) (Pubitemid 41654692)
    • (2005) Seminars in Immunology , vol.17 , Issue.6 , pp. 400-410
    • Dustin, M.L.1
  • 130
    • 0034666131 scopus 로고    scopus 로고
    • GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes
    • T. Hanada, L. Lin, E. V. Tibaldi, E. L. Reinherz and A. H. Chishti: GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes. J Biol Chem 275, 28774-28784 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 28774-28784
    • Hanada, T.1    Lin, L.2    Tibaldi, E.V.3    Reinherz, E.L.4    Chishti, A.H.5
  • 132
    • 13644268540 scopus 로고    scopus 로고
    • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells
    • DOI 10.1084/jem.20041428
    • J. L. Round, T. Tomassian, M. Zhang, V. Patel, S. P. Schoenberger and M. C. Miceli: Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. J Exp Med 201, 419-430 (2005) (Pubitemid 40229416)
    • (2005) Journal of Experimental Medicine , vol.201 , Issue.3 , pp. 419-430
    • Round, J.L.1    Tomassian, T.2    Zhang, M.3    Patel, V.4    Schoenberger, S.P.5    Miceli, M.C.6
  • 134
    • 0034065232 scopus 로고    scopus 로고
    • On the molecular architecture of myelinated fibers
    • E. J. Arroyo and S. S. Scherer: On the molecular architecture of myelinated fibers. Histochem Cell Biol 113, 1-18 (2000) (Pubitemid 30164404)
    • (2000) Histochemistry and Cell Biology , vol.113 , Issue.1 , pp. 1-18
    • Arroyo, E.J.1    Scherer, S.S.2
  • 135
    • 25144469422 scopus 로고    scopus 로고
    • Mechanisms of axon ensheathment and myelin growth
    • DOI 10.1038/nrn1743, PII NRN1743
    • D. L. Sherman and P. J. Brophy: Mechanisms of axon ensheathment and myelin growth. Nat Rev Neurosci 6, 683-690 (2005) (Pubitemid 43160317)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.9 , pp. 683-690
    • Sherman, D.L.1    Brophy, P.J.2
  • 136
    • 0035991912 scopus 로고    scopus 로고
    • Cellular junctions of myelinated nerves (review)
    • DOI 10.1080/09687680210130009
    • I. Spiegel and E. Peles: Cellular junctions of myelinated nerves (Review). Mol Membr Biol 19, 95-101 (2002) (Pubitemid 34753313)
    • (2002) Molecular Membrane Biology , vol.19 , Issue.2 , pp. 95-101
    • Spiegel, I.1    Peles, E.2
  • 137
    • 0037191066 scopus 로고    scopus 로고
    • Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
    • S. Poliak, S. Matlis, C. Ullmer, S. S. Scherer and E. Peles: Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells. J Cell Biol 159, 361-372. (2002)
    • (2002) J Cell Biol , vol.159 , pp. 361-372
    • Poliak, S.1    Matlis, S.2    Ullmer, C.3    Scherer, S.S.4    Peles, E.5
  • 138
  • 139
    • 0036788073 scopus 로고    scopus 로고
    • Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development
    • C. Y. Cheng and D. D. Mruk: Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development. Physiol Rev 82, 825-874 (2002)
    • (2002) Physiol Rev , vol.82 , pp. 825-874
    • Cheng, C.Y.1    Mruk, D.D.2
  • 140
    • 33846586935 scopus 로고    scopus 로고
    • Ectoplasmic specialization: A friend or a foe of spermatogenesis?
    • DOI 10.1002/bies.20513
    • H. H. Yan, D. D. Mruk, W. M. Lee and C. Y. Cheng: Ectoplasmic specialization: a friend or a foe of spermatogenesis? Bioessays 29, 36-48 (2007) (Pubitemid 46181803)
    • (2007) BioEssays , vol.29 , Issue.1 , pp. 36-48
    • Yan, H.H.N.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 141
    • 4644307425 scopus 로고    scopus 로고
    • Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C
    • DOI 10.1038/nature02877
    • G. Gliki, K. Ebnet, M. Aurrand-Lions, B. A. Imhof and R. H. Adams: Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C. Nature 431, 320-324 (2004) (Pubitemid 39265668)
    • (2004) Nature , vol.431 , Issue.7006 , pp. 320-324
    • Gliki, G.1    Ebnet, K.2    Aurrand-Lions, M.3    Imhof, B.A.4    Adams, R.H.5
  • 142
    • 33644895026 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis
    • M. Mirza, J. Hreinsson, M. L. Strand, O. Hovatta, O. Soder, L. Philipson, R. F. Pettersson and K. Sollerbrant: Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis. Exp Cell Res 312, 817-830 (2006)
    • (2006) Exp Cell Res , vol.312 , pp. 817-830
    • Mirza, M.1    Hreinsson, J.2    Strand, M.L.3    Hovatta, O.4    Soder, O.5    Philipson, L.6    Pettersson, R.F.7    Sollerbrant, K.8
  • 143
    • 33751012712 scopus 로고    scopus 로고
    • A CTX family cell adhesion molecule, JAM4, is expressed in stem cell and progenitor cell populations of both male germ cell and hematopoietic cell lineages
    • DOI 10.1128/MCB.01502-06
    • G. Nagamatsu, M. Ohmura, T. Mizukami, I. Hamaguchi, S. Hirabayashi, S. Yoshida, Y. Hata, T. Suda and K. Ohbo: A CTX family cell adhesion molecule, JAM4, is expressed in stem cell and progenitor cell populations of both male germ cell and hematopoietic cell lineages. Mol Cell Biol 26, 8498-8506 (2006) (Pubitemid 44748582)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8498-8506
    • Nagamatsu, G.1    Ohmura, M.2    Mizukami, T.3    Hamaguchi, I.4    Hirabayashi, S.5    Yoshida, S.6    Hata, Y.7    Suda, T.8    Ohbo, K.9
  • 144
    • 0037228268 scopus 로고    scopus 로고
    • A genetic hierarchy controlling cell polarity
    • K. Johnson and A. Wodarz: A genetic hierarchy controlling cell polarity. Nat Cell Biol 5, 12-14 (2003)
    • (2003) Nat Cell Biol , vol.5 , pp. 12-14
    • Johnson, K.1    Wodarz, A.2
  • 146
    • 34548295877 scopus 로고    scopus 로고
    • Cell polarity in development and cancer
    • DOI 10.1038/ncb433, PII NCB433
    • A. Wodarz and I. Nathke: Cell polarity in development and cancer. Nat Cell Biol 9, 1016-1024 (2007) (Pubitemid 47342312)
    • (2007) Nature Cell Biology , vol.9 , Issue.9 , pp. 1016-1024
    • Wodarz, A.1    Nathke, I.2
  • 147
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • DOI 10.1016/j.molcel.2006.08.002, PII S1097276506005375
    • J. Moscat, M. T. Diaz-Meco, A. Albert and S. Campuzano: Cell signaling and function organized by PB1 domain interactions. Mol Cell 23, 631-640 (2006) (Pubitemid 44292560)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 148
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • P. D. Burbelo, D. Drechsel and A. Hall: A conserved binding motif defines
    • (1995) J Biol Chem , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 149
    • 0034740693 scopus 로고    scopus 로고
    • Mechanisma and role of PDZ domains in signaling complex assembly
    • B. Z. Harris and W. A. Lim: Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 114, 3219-3231. (2001) (Pubitemid 32998900)
    • (2001) Journal of Cell Science , vol.114 , Issue.18 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 150
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • DOI 10.1016/0968-0004(96)30015-7, PII S0968000496300157
    • K. Hofmann and P. Bucher: The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21, 172-173 (1996) (Pubitemid 126335285)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.5 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 152
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • C. Mackintosh: Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 381, 329-342 (2004)
    • (2004) Biochem J , vol.381 , pp. 329-342
    • MacKintosh, C.1
  • 153
    • 2942729619 scopus 로고    scopus 로고
    • LKB1 tumor suppressor protein: PARtaker in cell polarity
    • DOI 10.1016/j.tcb.2004.04.001, PII S096289240400100X
    • A. F. Baas, L. Smit and H. Clevers: LKB1 tumor suppressor protein: PARtaker in cell polarity. Trends Cell Biol 14, 312-319 (2004) (Pubitemid 38798180)
    • (2004) Trends in Cell Biology , vol.14 , Issue.6 , pp. 312-319
    • Baas, A.F.1    Smit, L.2    Clevers, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.