메뉴 건너뛰기




Volumn 1778, Issue 3, 2008, Pages 646-659

Structural organization of the tight junctions

Author keywords

Adhesion; Cytoskeleton; Junction; Permeability; Polarity

Indexed keywords

ACTIN; AFADIN; CELL PROTEIN; CINGULIN; CLAUDIN; GUANINE NUCLEOTIDE BINDING PROTEIN; JUNCTIONAL ADHESION MOLECULE A; MEMBRANE ASSOCIATED GUANYLATE CYCLASE KINASE; MEMBRANE PROTEIN; OCCLUDIN; PROTEIN MAGI 1; PROTEIN ZO1; PROTEIN ZO2; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 39849102702     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.08.004     Document Type: Review
Times cited : (143)

References (107)
  • 1
    • 3042590902 scopus 로고    scopus 로고
    • Endothelial cell-to-cell junctions: molecular organization and role in vascular homeostasis
    • G. Bazzoni E. Dejana Endothelial cell-to-cell junctions: molecular organization and role in vascular homeostasis Physiol. Rev. 84 2004 869 901
    • (2004) Physiol. Rev. , vol.84 , pp. 869-901
    • Bazzoni, G.1    Dejana, E.2
  • 2
    • 3142744551 scopus 로고    scopus 로고
    • Cell adhesion, polarity, and epithelia in the dawn of metazoans
    • M. Cereijido R.G. Contreras L. Shoshani Cell adhesion, polarity, and epithelia in the dawn of metazoans Physiol. Rev. 84 2004 1229 1262
    • (2004) Physiol. Rev. , vol.84 , pp. 1229-1262
    • Cereijido, M.1    Contreras, R.G.2    Shoshani, L.3
  • 3
    • 0035991935 scopus 로고    scopus 로고
    • Molecular complexity of vertebrate tight junctions (Review)
    • F. D'Atri S. Citi Molecular complexity of vertebrate tight junctions (Review) Mol. Membr. Biol. 19 2002 103 112
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 103-112
    • D'Atri, F.1    Citi, S.2
  • 4
  • 5
    • 32544432516 scopus 로고    scopus 로고
    • Tight junctions: molecular architecture and function
    • S. Aijaz M.S. Balda K. Matter Tight junctions: molecular architecture and function Int. Rev. Cyt. 248 2006 261 298
    • (2006) Int. Rev. Cyt. , vol.248 , pp. 261-298
    • Aijaz, S.1    Balda, M.S.2    Matter, K.3
  • 6
    • 33645747414 scopus 로고    scopus 로고
    • Claudins in occluding junctions of humans and flies
    • M. Furuse S. Tsukita Claudins in occluding junctions of humans and flies Trends Cell Biol. 16 2006 181 188
    • (2006) Trends Cell Biol. , vol.16 , pp. 181-188
    • Furuse, M.1    Tsukita, S.2
  • 8
    • 39849108966 scopus 로고    scopus 로고
    • Transmembrane proteins of tight junctions
    • H. Chiba Transmembrane proteins of tight junctions Biochim. Biophys. Acta 1778 2008 588 600
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 588-600
    • Chiba, H.1
  • 9
    • 39849103311 scopus 로고    scopus 로고
    • The cytoplasmic plaque of tight junctions: a scaffolding and signalling center
    • L. Guillemot The cytoplasmic plaque of tight junctions: a scaffolding and signalling center Biochim. Biophys. Acta 1778 2008 601 613
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 601-613
    • Guillemot, L.1
  • 10
    • 33645553318 scopus 로고    scopus 로고
    • Endothelial tight junctions: permeable barriers of the vessel wall
    • G. Bazzoni Endothelial tight junctions: permeable barriers of the vessel wall Thromb. Haemost. 95 2006 36 42
    • (2006) Thromb. Haemost. , vol.95 , pp. 36-42
    • Bazzoni, G.1
  • 11
    • 85120143063 scopus 로고    scopus 로고
    • I. Blasig, Claudins: Structure and function of the extracellular domains, Biochim. Biophys. Acta, submitted for publication.
  • 12
    • 39849102083 scopus 로고    scopus 로고
    • Stimulus-induced reorganization of tight junction structure: The role of membrane traffic
    • D. Yu J.R. Turner Stimulus-induced reorganization of tight junction structure: The role of membrane traffic Biochim. Biophys. Acta 1778 2008 709 716
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 709-716
    • Yu, D.1    Turner, J.R.2
  • 14
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • M. Furuse M. Itoh T. Hirase A. Nagafuchi S. Yonemura S. Tsukita Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions J. Cell Biol. 127 1994 1617 1626
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6
  • 15
    • 0033605347 scopus 로고    scopus 로고
    • Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin
    • M. Itoh K. Morita S. Tsukita Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin J. Biol. Chem. 274 1999 5981 5986
    • (1999) J. Biol. Chem. , vol.274 , pp. 5981-5986
    • Itoh, M.1    Morita, K.2    Tsukita, S.3
  • 16
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • J. Haskins L. Gu E.S. Wittchen J. Hibbard B.R. Stevenson ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin J. Cell Biol. 141 1998 199 208
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 17
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • A.S. Fanning B.J. Jameson L.A. Jesaitis J.M. Anderson The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton J. Biol. Chem. 273 1998 29745 29753
    • (1998) J. Biol. Chem. , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 18
    • 0033199904 scopus 로고    scopus 로고
    • Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin
    • M. Cordenonsi F. Turco F. D'Atri E. Hammar G. Martinucci F. Meggio S. Citi Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin Eur. J. Biochem. 264 1999 374 384
    • (1999) Eur. J. Biochem. , vol.264 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D'Atri, F.3    Hammar, E.4    Martinucci, G.5    Meggio, F.6    Citi, S.7
  • 19
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • E.S. Wittchen J. Haskins B.R. Stevenson Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3 J. Biol. Chem. 274 1999 35179 35185
    • (1999) J. Biol. Chem. , vol.274 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 20
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • A. Sakakibara M. Furuse M. Saitou Y. Ando-Akatsuka S. Tsukita Possible involvement of phosphorylation of occludin in tight junction formation J. Cell Biol. 137 1997 1393 1401
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 21
    • 0036226069 scopus 로고    scopus 로고
    • Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells
    • Y.H. Chen Q. Lu D.A. Goodenough B. Jeansonne Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells Mol. Biol. Cell 13 2002 1227 1237
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1227-1237
    • Chen, Y.H.1    Lu, Q.2    Goodenough, D.A.3    Jeansonne, B.4
  • 22
    • 0038201989 scopus 로고    scopus 로고
    • Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2
    • C. Smales M. Ellis R. Baumber N. Hussain H. Desmond J.M. Staddon Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2 FEBS Lett. 545 2003 161 166
    • (2003) FEBS Lett. , vol.545 , pp. 161-166
    • Smales, C.1    Ellis, M.2    Baumber, R.3    Hussain, N.4    Desmond, H.5    Staddon, J.M.6
  • 23
    • 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 D.I. Utepbergenov Protein kinase C regulates the phosphorylation and cellular localization of occludin J. Biol. Chem. 276 2001 38480 38486
    • (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
  • 24
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • A. Nusrat J.A. Chen C.S. Foley T.W. Liang J. Tom M. Cromwell C. Quan R.J. Mrsny The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction J. Biol. Chem. 275 2000 29816 29822
    • (2000) J. Biol. Chem. , vol.275 , pp. 29816-29822
    • Nusrat, A.1    Chen, J.A.2    Foley, C.S.3    Liang, T.W.4    Tom, J.5    Cromwell, M.6    Quan, C.7    Mrsny, R.J.8
  • 25
    • 0037009005 scopus 로고    scopus 로고
    • Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex
    • V. Nunbhakdi-Craig T. Machleidt E. Ogris D. Bellotto C.L. White III E. Sontag Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex J. Cell Biol. 158 2002 967 978
    • (2002) J. Cell Biol. , vol.158 , pp. 967-978
    • Nunbhakdi-Craig, V.1    Machleidt, T.2    Ogris, E.3    Bellotto, D.4    White, C.L.5    Sontag, E.6
  • 26
    • 1542677112 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions
    • P. Sheth S. Basuroy C. Li A.P. Naren R.K. Rao Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions J. Biol. Chem. 278 2003 49239 49245
    • (2003) J. Biol. Chem. , vol.278 , pp. 49239-49245
    • Sheth, P.1    Basuroy, S.2    Li, C.3    Naren, A.P.4    Rao, R.K.5
  • 29
    • 18244375541 scopus 로고    scopus 로고
    • cAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludin
    • W.Y. Lui W.M. Lee cAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludin J. Cell. Physiol. 203 2005 564 572
    • (2005) J. Cell. Physiol. , vol.203 , pp. 564-572
    • Lui, W.Y.1    Lee, W.M.2
  • 30
    • 1642312139 scopus 로고    scopus 로고
    • Diversity in protein-protein interactions of connexins: emerging roles
    • J.C. Herve N. Bourmeyster D. Sarrouilhe Diversity in protein-protein interactions of connexins: emerging roles Biochim. Biophys. Acta. 1662 2004 22 41
    • (2004) Biochim. Biophys. Acta. , vol.1662 , pp. 22-41
    • Herve, J.C.1    Bourmeyster, N.2    Sarrouilhe, D.3
  • 31
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • J. Ikenouchi M. Furuse K. Furuse H. Sasaki S. Tsukita Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells J. Cell Biol. 171 2005 939 945
    • (2005) J. Cell Biol. , vol.171 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5
  • 32
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • M. Furuse K. Fujita T. Hiiragi K. Fujimoto S. Tsukita Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin J. Cell Biol. 141 1998 1539 1550
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 33
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • M. Itoh M. Furuse K. Morita K. Kubota M. Saitou S. Tsukita Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins J. Cell Biol. 147 1999 1351 1363
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 34
    • 0037178864 scopus 로고    scopus 로고
    • The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • M.H. Roh C.J. Liu S. Laurinec B. Margolis The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions J. Biol. Chem. 277 2002 27501 27509
    • (2002) J. Biol. Chem. , vol.277 , pp. 27501-27509
    • Roh, M.H.1    Liu, C.J.2    Laurinec, S.3    Margolis, B.4
  • 35
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • Y. Hamazaki M. Itoh H. Sasaki M. Furuse S. Tsukita Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule J. Biol. Chem. 277 2002 455 461
    • (2002) J. Biol. Chem. , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 38
    • 0035958937 scopus 로고    scopus 로고
    • Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases
    • H. Miyamori T. Takino Y. Kobayashi H. Tokai Y. Itoh M. Seiki H. Sato Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases J. Biol. Chem. 276 2001 28204 28211
    • (2001) J. Biol. Chem. , vol.276 , pp. 28204-28211
    • Miyamori, H.1    Takino, T.2    Kobayashi, Y.3    Tokai, H.4    Itoh, Y.5    Seiki, M.6    Sato, H.7
  • 39
    • 0039027605 scopus 로고    scopus 로고
    • Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin
    • G. Bazzoni O.M. Martinez-Estrada F. Orsenigo M. Cordenonsi S. Citi E. Dejana Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin J. Biol. Chem. 275 2000 20520 20526
    • (2000) J. Biol. Chem. , vol.275 , pp. 20520-20526
    • Bazzoni, G.1    Martinez-Estrada, O.M.2    Orsenigo, F.3    Cordenonsi, M.4    Citi, S.5    Dejana, E.6
  • 40
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • K. Ebnet C.U. Schulz M.K. Meyer Zu Brickwedde G.G. Pendl D. Vestweber Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1 J. Biol. Chem. 275 2000 27979 27988
    • (2000) J. Biol. Chem. , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 41
    • 0035937810 scopus 로고    scopus 로고
    • Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells
    • O.M. Martinez-Estrada A. Villa F. Breviario F. Orsenigo E. Dejana G. Bazzoni Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells J. Biol. Chem. 276 2001 9291 9296
    • (2001) J. Biol. Chem. , vol.276 , pp. 9291-9296
    • Martinez-Estrada, O.M.1    Villa, A.2    Breviario, F.3    Orsenigo, F.4    Dejana, E.5    Bazzoni, G.6
  • 42
    • 16344374495 scopus 로고    scopus 로고
    • PICK-1: a scaffold protein that interacts with Nectins and JAMs at cell junctions
    • N. Reymond S. Garrido-Urbani J.P. Borg P. Dubreuil M. Lopez PICK-1: a scaffold protein that interacts with Nectins and JAMs at cell junctions FEBS Lett. 579 2005 2243 2249
    • (2005) FEBS Lett. , vol.579 , pp. 2243-2249
    • Reymond, N.1    Garrido-Urbani, S.2    Borg, J.P.3    Dubreuil, P.4    Lopez, M.5
  • 47
    • 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 I.G. Macara The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42 Nat. Cell Biol. 2 2000 531 539
    • (2000) Nat. Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 48
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • D. Lin A.S. Edwards J.P. Fawcett G. Mbamalu J.D. Scott T. Pawson A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity Nat. Cell Biol. 2 2000 540 547
    • (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
  • 49
    • 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
    • Y. Noda R. Takeya S. Ohno S. Naito T. Ito H. Sumimoto 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 Genes Cells 6 2001 107 119
    • (2001) Genes Cells , vol.6 , pp. 107-119
    • Noda, Y.1    Takeya, R.2    Ohno, S.3    Naito, S.4    Ito, T.5    Sumimoto, H.6
  • 51
    • 0033621957 scopus 로고    scopus 로고
    • Atypical protein kinases Clambda and -zeta associate with the GTP-binding protein Cdc42 and mediate stress fiber loss
    • M.P. Coghlan M.M. Chou C.L. Carpenter Atypical protein kinases Clambda and -zeta associate with the GTP-binding protein Cdc42 and mediate stress fiber loss Mol. Cell. Biol. 20 2000 2880 2889
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2880-2889
    • Coghlan, M.P.1    Chou, M.M.2    Carpenter, C.L.3
  • 52
    • 3242702211 scopus 로고    scopus 로고
    • Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity
    • X.F. Liu H. Ishida R. Raziuddin T. Miki Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity Mol. Cell. Biol. 24 2004 6665 6675
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6665-6675
    • Liu, X.F.1    Ishida, H.2    Raziuddin, R.3    Miki, T.4
  • 53
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions
    • M. Itoh H. Sasaki M. Furuse H. Ozaki T. Kita S. Tsukita Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions J. Cell Biol. 154 2001 491 497
    • (2001) J. Cell Biol. , vol.154 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 55
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • T.W. Hurd L. Gao M.H. Roh I.G. Macara B. Margolis Direct interaction of two polarity complexes implicated in epithelial tight junction assembly Nat. Cell Biol. 5 2003 137 142
    • (2003) Nat. Cell Biol. , vol.5 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    Macara, I.G.4    Margolis, B.5
  • 57
    • 0029112236 scopus 로고
    • A human homologue of the Drosophila tumour suppressor gene l(2)gl maps to 17p11.2-12 and codes for a cytoskeletal protein that associates with nonmuscle myosin II heavy chain
    • D. Strand S. Unger R. Corvi K. Hartenstein H. Schenkel A. Kalmes G. Merdes B. Neumann F. Krieg-Schneider J.F. Coy A human homologue of the Drosophila tumour suppressor gene l(2)gl maps to 17p11.2-12 and codes for a cytoskeletal protein that associates with nonmuscle myosin II heavy chain Oncogene 11 1995 291 301
    • (1995) Oncogene , vol.11 , pp. 291-301
    • Strand, D.1    Unger, S.2    Corvi, R.3    Hartenstein, K.4    Schenkel, H.5    Kalmes, A.6    Merdes, G.7    Neumann, B.8    Krieg-Schneider, F.9    Coy, J.F.10
  • 58
    • 0347596668 scopus 로고    scopus 로고
    • Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells
    • R. Benton D. St Johnston Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells Cell 115 2003 691 704
    • (2003) Cell , vol.115 , pp. 691-704
    • Benton, R.1    St Johnston, D.2
  • 59
    • 0344663968 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia
    • T.W. Hurd S. Fan C.J. Liu H.K. Kweon K. Hakansson B. Margolis Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia Curr. Biol. 13 2003 2082 2090
    • (2003) Curr. Biol. , vol.13 , pp. 2082-2090
    • Hurd, T.W.1    Fan, S.2    Liu, C.J.3    Kweon, H.K.4    Hakansson, K.5    Margolis, B.6
  • 60
    • 1942540791 scopus 로고    scopus 로고
    • Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity
    • J.B. Hurov J.L. Watkins H. Piwnica-Worms Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity Curr. Biol. 14 2004 736 741
    • (2004) Curr. Biol. , vol.14 , pp. 736-741
    • Hurov, J.B.1    Watkins, J.L.2    Piwnica-Worms, H.3
  • 62
    • 33644530393 scopus 로고    scopus 로고
    • Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly
    • X. Chen I.G. Macara Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly J. Cell Biol. 172 2006 671 678
    • (2006) J. Cell Biol. , vol.172 , pp. 671-678
    • Chen, X.1    Macara, I.G.2
  • 63
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • E. Nishida S. Maekawa H. Sakai Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin Biochemistry 23 1984 5307 5313
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 64
    • 14744289370 scopus 로고    scopus 로고
    • Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
    • X. Chen I.G. Macara Par-3 controls tight junction assembly through the Rac exchange factor Tiam1 Nat. Cell Biol. 7 2005 262 269
    • (2005) Nat. Cell Biol. , vol.7 , pp. 262-269
    • Chen, X.1    Macara, I.G.2
  • 65
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • D.K. Worthylake K.L. Rossman J. Sondek Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1 Nature 408 2000 682 688
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 66
    • 14844364701 scopus 로고    scopus 로고
    • Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity
    • B. Ozdamar R. Bose M. Barrios-Rodiles H.R. Wang Y. Zhang J.L. Wrana Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity Science 307 2005 1603 1609
    • (2005) Science , vol.307 , pp. 1603-1609
    • Ozdamar, B.1    Bose, R.2    Barrios-Rodiles, M.3    Wang, H.R.4    Zhang, Y.5    Wrana, J.L.6
  • 68
    • 0036832157 scopus 로고    scopus 로고
    • Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1
    • A.S. Fanning T.Y. Ma J.M. Anderson Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1 FASEB J. 16 2002 1835 1837
    • (2002) FASEB J. , vol.16 , pp. 1835-1837
    • Fanning, A.S.1    Ma, T.Y.2    Anderson, J.M.3
  • 69
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • S.A. Weed A.V. Karginov D.A. Schafer A.M. Weaver A.W. Kinley J.A. Cooper J.T. Parsons Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex J. Cell Biol. 151 2000 29 40
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 70
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments
    • M. Itoh A. Nagafuchi S. Moroi S. Tsukita Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments J. Cell Biol. 138 1997 181 192
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 71
    • 0037166245 scopus 로고    scopus 로고
    • Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin
    • S. Pokutta F. Drees Y. Takai W.J. Nelson W.I. Weis Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin J. Biol. Chem. 277 2002 18868 18874
    • (2002) J. Biol. Chem. , vol.277 , pp. 18868-18874
    • Pokutta, S.1    Drees, F.2    Takai, Y.3    Nelson, W.J.4    Weis, W.I.5
  • 72
    • 0034730515 scopus 로고    scopus 로고
    • Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton
    • S.N. Mattagajasingh S.C. Huang J.S. Hartenstein E.J. Benz Jr. Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton J. Biol. Chem. 275 2000 30573 30585
    • (2000) J. Biol. Chem. , vol.275 , pp. 30573-30585
    • Mattagajasingh, S.N.1    Huang, S.C.2    Hartenstein, J.S.3    Benz, E.J.4
  • 73
    • 0037062586 scopus 로고    scopus 로고
    • Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins
    • J.A. Gimm X. An W. Nunomura N. Mohandas Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins Biochemistry 41 2002 7275 7282
    • (2002) Biochemistry , vol.41 , pp. 7275-7282
    • Gimm, J.A.1    An, X.2    Nunomura, W.3    Mohandas, N.4
  • 74
    • 0037008741 scopus 로고    scopus 로고
    • Evidence for a functional interaction between cingulin and ZO-1 in cultured cells
    • F. D'Atri F. Nadalutti S. Citi Evidence for a functional interaction between cingulin and ZO-1 in cultured cells J. Biol. Chem. 277 2002 27757 27764
    • (2002) J. Biol. Chem. , vol.277 , pp. 27757-27764
    • D'Atri, F.1    Nadalutti, F.2    Citi, S.3
  • 76
    • 0035914113 scopus 로고    scopus 로고
    • Cingulin interacts with F-actin in vitro
    • F. D'Atri S. Citi Cingulin interacts with F-actin in vitro FEBS Lett. 507 2001 21 24
    • (2001) FEBS Lett. , vol.507 , pp. 21-24
    • D'Atri, F.1    Citi, S.2
  • 78
    • 17844402719 scopus 로고    scopus 로고
    • Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition
    • S. Aijaz F. D'Atri S. Citi M.S. Balda K. Matter Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition Dev. Cell 8 2005 777 786
    • (2005) Dev. Cell , vol.8 , pp. 777-786
    • Aijaz, S.1    D'Atri, F.2    Citi, S.3    Balda, M.S.4    Matter, K.5
  • 80
    • 0038586530 scopus 로고    scopus 로고
    • NZO-3 expression causes global changes to actin cytoskeleton in Madin–Darby canine kidney cells: linking a tight junction protein to Rho GTPases
    • E.S. Wittchen J. Haskins B.R. Stevenson NZO-3 expression causes global changes to actin cytoskeleton in Madin–Darby canine kidney cells: linking a tight junction protein to Rho GTPases Mol. Biol. Cell 14 2003 1757 1768
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1757-1768
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 83
    • 24644496823 scopus 로고    scopus 로고
    • Mammalian tight junctions in the regulation of epithelial differentiation and proliferation
    • K. Matter S. Aijaz A. Tsapara M.S. Balda Mammalian tight junctions in the regulation of epithelial differentiation and proliferation Curr. Opin. Cell Biol. 17 2005 453 458
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 453-458
    • Matter, K.1    Aijaz, S.2    Tsapara, A.3    Balda, M.S.4
  • 84
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • M.S. Balda K. Matter The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression EMBO J. 19 2000 2024 2033
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 85
    • 0037415643 scopus 로고    scopus 로고
    • The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density
    • M.S. Balda M.D. Garrett K. Matter The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density J. Cell Biol. 160 2003 423 432
    • (2003) J. Cell Biol. , vol.160 , pp. 423-432
    • Balda, M.S.1    Garrett, M.D.2    Matter, K.3
  • 86
    • 13244260780 scopus 로고    scopus 로고
    • RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity
    • P. Frankel A. Aronheim E. Kavanagh M.S. Balda K. Matter T.D. Bunney C.J. Marshall RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity EMBO J. 24 2005 54 62
    • (2005) EMBO J. , vol.24 , pp. 54-62
    • Frankel, P.1    Aronheim, A.2    Kavanagh, E.3    Balda, M.S.4    Matter, K.5    Bunney, T.D.6    Marshall, C.J.7
  • 87
    • 33644861530 scopus 로고    scopus 로고
    • The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB
    • A. Tsapara K. Matter M.S. Balda The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB Mol. Biol. Cell 17 2006 1322 1330
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1322-1330
    • Tsapara, A.1    Matter, K.2    Balda, M.S.3
  • 89
    • 0037462794 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B
    • A. Traweger R. Fuchs I.A. Krizbai T.M. Weiger H.C. Bauer H. Bauer The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B J. Biol. Chem. 278 2003 2692 2700
    • (2003) J. Biol. Chem. , vol.278 , pp. 2692-2700
    • Traweger, A.1    Fuchs, R.2    Krizbai, I.A.3    Weiger, T.M.4    Bauer, H.C.5    Bauer, H.6
  • 90
    • 9444277252 scopus 로고    scopus 로고
    • Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell–cell adhesion regulate plasma membrane and nuclear localization of ARVCF
    • P.J. Kausalya D.C. Phua W. Hunziker Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell–cell adhesion regulate plasma membrane and nuclear localization of ARVCF Mol. Biol. Cell 15 2004 5503 5515
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5503-5515
    • Kausalya, P.J.1    Phua, D.C.2    Hunziker, W.3
  • 91
    • 0030590868 scopus 로고    scopus 로고
    • The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain
    • M.S. Balda J.M. Anderson K. Matter The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain FEBS Lett. 399 1996 326 332
    • (1996) FEBS Lett. , vol.399 , pp. 326-332
    • Balda, M.S.1    Anderson, J.M.2    Matter, K.3
  • 92
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein
    • B.N. Giepmans W.H. Moolenaar The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein Curr. Biol. 8 1998 931 934
    • (1998) Curr. Biol. , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 93
    • 0035823043 scopus 로고    scopus 로고
    • Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells
    • P.J. Kausalya M. Reichert W. Hunziker Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells FEBS Lett. 505 2001 92 96
    • (2001) FEBS Lett. , vol.505 , pp. 92-96
    • Kausalya, P.J.1    Reichert, M.2    Hunziker, W.3
  • 94
    • 0037641234 scopus 로고    scopus 로고
    • JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1
    • S. Hirabayashi M. Tajima I. Yao W. Nishimura H. Mori Y. Hata JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1 Mol. Cell. Biol. 23 2003 4267 4282
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4267-4282
    • Hirabayashi, S.1    Tajima, M.2    Yao, I.3    Nishimura, W.4    Mori, H.5    Hata, Y.6
  • 95
    • 0034805643 scopus 로고    scopus 로고
    • Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1
    • I.Y. Dobrosotskaya Identification of mNET1 as a candidate ligand for the first PDZ domain of MAGI-1 Biochem. Biophys. Res. Commun. 283 2001 969 975
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 969-975
    • Dobrosotskaya, I.Y.1
  • 96
    • 4644245292 scopus 로고    scopus 로고
    • Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts
    • F. Wegmann K. Ebnet L. Du Pasquier D. Vestweber S. Butz Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts Exp. Cell Res. 300 2004 121 133
    • (2004) Exp. Cell Res. , vol.300 , pp. 121-133
    • Wegmann, F.1    Ebnet, K.2    Du Pasquier, L.3    Vestweber, D.4    Butz, S.5
  • 97
    • 5444236915 scopus 로고    scopus 로고
    • A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth
    • K.J. Excoffon A. Hruska-Hageman M. Klotz G.L. Traver J. Zabner A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth J. Cell Sci. 117 2004 4401 4409
    • (2004) J. Cell Sci. , vol.117 , pp. 4401-4409
    • Excoffon, K.J.1    Hruska-Hageman, A.2    Klotz, M.3    Traver, G.L.4    Zabner, J.5
  • 98
    • 0037119361 scopus 로고    scopus 로고
    • Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1
    • K.M. Patrie A.J. Drescher A. Welihinda P. Mundel B. Margolis Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1 J. Biol. Chem. 277 2002 30183 30190
    • (2002) J. Biol. Chem. , vol.277 , pp. 30183-30190
    • Patrie, K.M.1    Drescher, A.J.2    Welihinda, A.3    Mundel, P.4    Margolis, B.5
  • 101
    • 11244250646 scopus 로고    scopus 로고
    • Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness
    • L. Kotelevets J. van Hengel E. Bruyneel M. Mareel F. van Roy E. Chastre Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness FASEB J. 19 2005 115 117
    • (2005) FASEB J. , vol.19 , pp. 115-117
    • Kotelevets, L.1    van Hengel, J.2    Bruyneel, E.3    Mareel, M.4    van Roy, F.5    Chastre, E.6
  • 103
    • 0037385217 scopus 로고    scopus 로고
    • Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins
    • K. Adamsky K. Arnold H. Sabanay E. Peles Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins J. Cell Sci. 116 2003 1279 1289
    • (2003) J. Cell Sci. , vol.116 , pp. 1279-1289
    • Adamsky, K.1    Arnold, K.2    Sabanay, H.3    Peles, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.