메뉴 건너뛰기




Volumn 17, Issue 9, 2016, Pages 564-580

Tight junctions: From simple barriers to multifunctional molecular gates

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84976444297     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm.2016.80     Document Type: Review
Times cited : (1022)

References (180)
  • 1
    • 3142744551 scopus 로고    scopus 로고
    • Cell adhesion, polarity, and epithelia in the dawn of metazoans
    • Cereijido, M., Contreras, R. G. & Shoshani, L. Cell adhesion, polarity, and epithelia in the dawn of metazoans. Physiol. Rev. 84, 1229-1262 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 1229-1262
    • Cereijido, M.1    Contreras, R.G.2    Shoshani, L.3
  • 2
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M. G. & Palade, G. E. Junctional complexes in various epithelia. J. Cell Biol. 17, 375-412 (1963).
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 3
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia
    • Claude, P. & Goodenough, D. A. Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia. J. Cell Biol. 58, 390-400 (1973).
    • (1973) J. Cell Biol. , vol.58 , pp. 390-400
    • Claude, P.1    Goodenough, D.A.2
  • 4
    • 0014456576 scopus 로고
    • Freeze-etch appearance of the tight junctions in the epithelium of small and large intestine of mice
    • Staehelin, L. A., Mukherjee, T. M. & Williams, A. W. Freeze-etch appearance of the tight junctions in the epithelium of small and large intestine of mice. Protoplasma 67, 165-184 (1969).
    • (1969) Protoplasma , vol.67 , pp. 165-184
    • Staehelin, L.A.1    Mukherjee, T.M.2    Williams, A.W.3
  • 5
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures
    • Furuse, M. et al. Overexpression of occludin, a tight junction integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures. J. Cell Sci. 109, 429-435 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 429-435
    • Furuse, M.1
  • 6
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse, M., Sasaki, H., Fujimoto, K. & Tsukita, S. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143, 391-401 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 7
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita, K., Furuse, M., Fujimoto, K. & Tsukita, S. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc. Natl Acad. Sci. USA 96, 511-516 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 8
    • 0033598188 scopus 로고    scopus 로고
    • 2+-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions
    • 2+-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions. Curr. Biol. 9, 1035-1038 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1035-1038
    • Kubota, K.1
  • 9
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • Van Itallie, C. M. & Anderson, J. M. Occludin confers adhesiveness when expressed in fibroblasts. J. Cell Sci. 110, 1113-1121 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 10
    • 27844557346 scopus 로고    scopus 로고
    • Bves modulates epithelial integrity through an interaction at the tight junction
    • Osler, M. E., Chang, M. S. & Bader, D. M. Bves modulates epithelial integrity through an interaction at the tight junction. J. Cell Sci. 118, 4667-4678 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4667-4678
    • Osler, M.E.1    Chang, M.S.2    Bader, D.M.3
  • 11
    • 84899982143 scopus 로고    scopus 로고
    • JAM-related proteins in mucosal homeostasis and inflammation
    • Luissint, A. C., Nusrat, A. & Parkos, C. A. JAM-related proteins in mucosal homeostasis and inflammation. Semin. Immunopathol. 36, 211-226 (2014).
    • (2014) Semin. Immunopathol. , vol.36 , pp. 211-226
    • Luissint, A.C.1    Nusrat, A.2    Parkos, C.A.3
  • 12
    • 2642614521 scopus 로고    scopus 로고
    • Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration
    • Martin-Padura, I. et al. Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration. J. Cell Biol. 142, 117-127 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 117-127
    • Martin-Padura, I.1
  • 13
    • 0035910098 scopus 로고    scopus 로고
    • The coxsackievirus and adenovirus≈receptor is a transmembrane component of the tight junction
    • Cohen, C. J. et al. The coxsackievirus and adenovirus≈receptor is a transmembrane component of the tight junction. Proc. Natl Acad. Sci. USA 98, 15191-15196 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 15191-15196
    • Cohen, C.J.1
  • 14
    • 84883343773 scopus 로고    scopus 로고
    • Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2-tricellulin recruitment, epithelial barrier function and implication in deafness pathogenesis
    • Higashi, T. et al. Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2-tricellulin recruitment, epithelial barrier function and implication in deafness pathogenesis. J. Cell Sci. 126, 966-977 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 966-977
    • Higashi, T.1
  • 15
    • 79951830550 scopus 로고    scopus 로고
    • LSR defines cell corners for tricellular tight junction formation in epithelial cells
    • Masuda, S. et al. LSR defines cell corners for tricellular tight junction formation in epithelial cells. J. Cell Sci. 124, 548-555 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 548-555
    • Masuda, S.1
  • 16
    • 0037067320 scopus 로고    scopus 로고
    • HINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells
    • Lemmers, C. et al. hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells. J. Biol. Chem. 277, 25408-25415 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25408-25415
    • Lemmers, C.1
  • 17
    • 0037413672 scopus 로고    scopus 로고
    • Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1)
    • Makarova, O., Roh, M. H., Liu, C. J., Laurinec, S. & Margolis, B. Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1). Gene 302, 21-29 (2003).
    • (2003) Gene , vol.302 , pp. 21-29
    • Makarova, O.1    Roh, M.H.2    Liu, C.J.3    Laurinec, S.4    Margolis, B.5
  • 18
    • 84912092373 scopus 로고    scopus 로고
    • Architecture of tight junctions and principles of molecular composition
    • Van Itallie, C. M. & Anderson, J. M. Architecture of tight junctions and principles of molecular composition. Semin. Cell Dev. Biol. 36, 157-165 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 157-165
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 19
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson, B. R., Siliciano, J. D., Mooseker, M. S. & Goodenough, D. A. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103, 755-766 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 20
    • 84877944837 scopus 로고    scopus 로고
    • Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1
    • Rodgers, L. S., Beam, M. T., Anderson, J. M. & Fanning, A. S. Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1. J. Cell Sci. 126, 1565-1575 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 1565-1575
    • Rodgers, L.S.1    Beam, M.T.2    Anderson, J.M.3    Fanning, A.S.4
  • 21
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Balda, M. S. & Anderson, J. M. Two classes of tight junctions are revealed by ZO-1 isoforms. Am. J. Physiol. 264, C918-C924 (1993).
    • (1993) Am. J. Physiol. , vol.264 , pp. C918-C924
    • Balda, M.S.1    Anderson, J.M.2
  • 22
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning, A. S., Jameson, B. J., Jesaitis, L. A. & Anderson, J. M. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J. Biol. Chem. 273, 29745-29753 (1998).
    • (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
  • 23
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda, M. S. & Matter, K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19, 2024-2033 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 24
    • 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
    • Tsapara, A., Matter, K. & Balda, M. S. The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB. Mol. Biol. Cell 17, 1322-1330 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1322-1330
    • Tsapara, A.1    Matter, K.2    Balda, M.S.3
  • 25
    • 3042615519 scopus 로고    scopus 로고
    • Occludin binds to the SH3-hinge-GuK unit of zonula occludens protein 1: Potential mechanism of tight junction regulation
    • Schmidt, A. et al. Occludin binds to the SH3-hinge-GuK unit of zonula occludens protein 1: potential mechanism of tight junction regulation. Cell. Mol. Life Sci. 61, 1354-1365 (2004).
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1354-1365
    • Schmidt, A.1
  • 26
    • 77951613715 scopus 로고    scopus 로고
    • Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module
    • Lye, M. F., Fanning, A. S., Su, Y., Anderson, J. M. & Lavie, A. Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module. J. Biol. Chem. 285, 13907-13917 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 13907-13917
    • Lye, M.F.1    Fanning, A.S.2    Su, Y.3    Anderson, J.M.4    Lavie, A.5
  • 27
    • 33947133738 scopus 로고    scopus 로고
    • The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties
    • Fanning, A. S. et al. The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties. Mol. Biol. Cell 18, 721-731 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 721-731
    • Fanning, A.S.1
  • 28
    • 84905844113 scopus 로고    scopus 로고
    • ZO proteins redundantly regulate the transcription factor DbpA/ZONAB
    • Spadaro, D. et al. ZO proteins redundantly regulate the transcription factor DbpA/ZONAB. J. Biol. Chem. 289, 22500-22511 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 22500-22511
    • Spadaro, D.1
  • 29
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner, B., Lowenkopf, T. & Apatira, D. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl Acad. Sci. USA 88, 3460-3464 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 31
    • 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
    • Haskins, J., Gu, L., Wittchen, E. S., Hibbard, J. & Stevenson, B. R. 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, 199-208 (1998).
    • (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
  • 32
    • 0033576547 scopus 로고    scopus 로고
    • Localization of membrane-associated guanylate kinase (MAGI)-1/BAI-associated protein (BAP) 1 at tight junctions of epithelial cells
    • Ide, N. et al. Localization of membrane-associated guanylate kinase (MAGI)-1/BAI-associated protein (BAP) 1 at tight junctions of epithelial cells. Oncogene 18, 7810-7815 (1999).
    • (1999) Oncogene , vol.18 , pp. 7810-7815
    • Ide, N.1
  • 33
    • 0031440289 scopus 로고    scopus 로고
    • MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains
    • Dobrosotskaya, I., Guy, R. K. & James, G. L. MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains. J. Biol. Chem. 272, 31589-31597 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31589-31597
    • Dobrosotskaya, I.1    Guy, R.K.2    James, G.L.3
  • 34
    • 0037191066 scopus 로고    scopus 로고
    • Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
    • Poliak, S., Matlis, S., Ullmer, C., Scherrer, S. S. & Peles, E. 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    Scherrer, S.S.4    Peles, E.5
  • 35
    • 0036544563 scopus 로고    scopus 로고
    • The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of crumbs and discs lost
    • Roh, M. H. et al. The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost. J. Cell Biol. 157, 161-172 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 161-172
    • Roh, M.H.1
  • 36
    • 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
    • Hamazaki, Y., Itoh, M., Sasaki, H., Furuse, M. & Tsukita, S. 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, 455-461 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 37
    • 84861983882 scopus 로고    scopus 로고
    • Cingulin, paracingulin, and PLEKHA7: Signaling and cytoskeletal adaptors at the apical junctional complex
    • Citi, S., Pulimeno, P. & Paschoud, S. Cingulin, paracingulin, and PLEKHA7: signaling and cytoskeletal adaptors at the apical junctional complex. Ann. NY Acad. Sci. 1257, 125-132 (2012).
    • (2012) Ann. NY Acad. Sci. , vol.1257 , pp. 125-132
    • Citi, S.1    Pulimeno, P.2    Paschoud, S.3
  • 38
    • 84890243481 scopus 로고    scopus 로고
    • The association of microtubules with tight junctions is promoted by cingulin phosphorylation by AMPK
    • Yano, T., Matsui, T., Tamura, A., Uji, M. & Tsukita, S. The association of microtubules with tight junctions is promoted by cingulin phosphorylation by AMPK. J. Cell Biol. 203, 605-614 (2013).
    • (2013) J. Cell Biol. , vol.203 , pp. 605-614
    • Yano, T.1    Matsui, T.2    Tamura, A.3    Uji, M.4    Tsukita, S.5
  • 39
    • 0024456405 scopus 로고
    • ZO-1 and cingulin: Tight junction proteins with distinct identities and localizations
    • Stevenson, B. R., Heintzelman, M. B., Anderson, J. M., Citi, S. & Mooseker, M. S. ZO-1 and cingulin: tight junction proteins with distinct identities and localizations. Am. J. Physiol. 257, C621-C628 (1989).
    • (1989) Am. J. Physiol. , vol.257 , pp. C621-C628
    • Stevenson, B.R.1    Heintzelman, M.B.2    Anderson, J.M.3    Citi, S.4    Mooseker, M.S.5
  • 40
    • 0033611142 scopus 로고    scopus 로고
    • Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin
    • Cordenonsi, M. et al. Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin. J. Cell Biol. 147, 1569-1582 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1569-1582
    • Cordenonsi, M.1
  • 41
    • 84895737640 scopus 로고    scopus 로고
    • MarvelD3 couples tight junctions to the MEKK1-JNK pathway to regulate cell behavior and survival
    • Steed, E. et al. MarvelD3 couples tight junctions to the MEKK1-JNK pathway to regulate cell behavior and survival. J. Cell Biol. 204, 821-838 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 821-838
    • Steed, E.1
  • 42
    • 84961288745 scopus 로고    scopus 로고
    • Proteomic analysis of proteins surrounding occludin and claudin-4 reveals their proximity to signaling and trafficking networks
    • Fredriksson, K. et al. Proteomic analysis of proteins surrounding occludin and claudin-4 reveals their proximity to signaling and trafficking networks. PLoS ONE 10, e0117074 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0117074
    • Fredriksson, K.1
  • 43
    • 84906057165 scopus 로고    scopus 로고
    • Signalling at tight junctions during epithelial differentiation and microbial pathogenesis
    • Zihni, C., Balda, M. S. & Matter, K. Signalling at tight junctions during epithelial differentiation and microbial pathogenesis. J. Cell Sci. 127, 3401-3413 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 3401-3413
    • Zihni, C.1    Balda, M.S.2    Matter, K.3
  • 44
    • 85027920932 scopus 로고    scopus 로고
    • Tight junctions and the regulation of gene expression
    • Gonzalez-Mariscal, L. et al. Tight junctions and the regulation of gene expression. Semin. Cell Dev. Biol. 36, 213-223 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 213-223
    • Gonzalez-Mariscal, L.1
  • 45
    • 84912059213 scopus 로고    scopus 로고
    • RhoGTPases, actomyosin signaling and regulation of the epithelial apical junctional complex
    • Quiros, M. & Nusrat, A. RhoGTPases, actomyosin signaling and regulation of the epithelial apical junctional complex. Semin. Cell Dev. Biol. 36, 194-203 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 194-203
    • Quiros, M.1    Nusrat, A.2
  • 46
    • 33845212422 scopus 로고    scopus 로고
    • Normal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK protein
    • Adachi, M. et al. Normal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK protein. Mol. Cell. Biol. 26, 9003-9015 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9003-9015
    • Adachi, M.1
  • 47
    • 84872227438 scopus 로고    scopus 로고
    • Cingulin is dispensable for epithelial barrier function and tight junction structure, and plays a role in the control of claudin-2 expression and response to duodenal mucosa injury
    • Guillemot, L. et al. Cingulin is dispensable for epithelial barrier function and tight junction structure, and plays a role in the control of claudin-2 expression and response to duodenal mucosa injury. J. Cell Sci. 125, 5005-5014 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 5005-5014
    • Guillemot, L.1
  • 48
    • 40749084863 scopus 로고    scopus 로고
    • Early embryonic lethality of mice lacking ZO-2, but Not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development
    • Xu, J. et al. Early embryonic lethality of mice lacking ZO-2, but Not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development. Mol. Cell. Biol. 28, 1669-1678 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1669-1678
    • Xu, J.1
  • 49
    • 48649096603 scopus 로고    scopus 로고
    • Deficiency of ZO-1 causes embryonic lethal phenotype associated with defected yolk sac angiogenesis and apoptosis of embryonic cells
    • Katsuno, T. et al. Deficiency of ZO-1 causes embryonic lethal phenotype associated with defected yolk sac angiogenesis and apoptosis of embryonic cells. Mol. Biol. Cell 19, 2465-2475 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2465-2475
    • Katsuno, T.1
  • 50
    • 84922223377 scopus 로고    scopus 로고
    • ZO-1 knockout by TALEN-mediated gene targeting in MDCK cells: Involvement of ZO-1 in the regulation of cytoskeleton and cell shape
    • Tokuda, S., Higashi, T. & Furuse, M. ZO-1 knockout by TALEN-mediated gene targeting in MDCK cells: involvement of ZO-1 in the regulation of cytoskeleton and cell shape. PLoS ONE 9, e104994 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e104994
    • Tokuda, S.1    Higashi, T.2    Furuse, M.3
  • 51
    • 40949111378 scopus 로고    scopus 로고
    • Tjp3/zo-3 is critical for epidermal barrier function in zebrafish embryos
    • Kiener, T. K., Selptsova-Friedrich, I. & Hunziker, W. Tjp3/zo-3 is critical for epidermal barrier function in zebrafish embryos. Dev. Biol. 316, 36-49 (2008).
    • (2008) Dev. Biol. , vol.316 , pp. 36-49
    • Kiener, T.K.1    Selptsova-Friedrich, I.2    Hunziker, W.3
  • 52
    • 84956906927 scopus 로고    scopus 로고
    • Occludin deficiency promotes ethanol-induced disruption of colonic epithelial junctions, gut barrier dysfunction and liver damage in mice
    • Mir, H. et al. Occludin deficiency promotes ethanol-induced disruption of colonic epithelial junctions, gut barrier dysfunction and liver damage in mice. Biochim. Biophys. Acta 1860, 765-774 (2016).
    • (2016) Biochim. Biophys. Acta , vol.1860 , pp. 765-774
    • Mir, H.1
  • 53
    • 84899490629 scopus 로고    scopus 로고
    • Crystal structure of a claudin provides insight into the architecture of tight junctions
    • Suzuki, H. et al. Crystal structure of a claudin provides insight into the architecture of tight junctions. Science 344, 304-307 (2014).
    • (2014) Science , vol.344 , pp. 304-307
    • Suzuki, H.1
  • 54
    • 84920861016 scopus 로고    scopus 로고
    • Model for the architecture of claudin-based paracellular ion channels through tight junctions
    • Suzuki, H., Tani, K., Tamura, A., Tsukita, S. & Fujiyoshi, Y. Model for the architecture of claudin-based paracellular ion channels through tight junctions. J. Mol. Biol. 427, 291-297 (2015).
    • (2015) J. Mol. Biol. , vol.427 , pp. 291-297
    • Suzuki, H.1    Tani, K.2    Tamura, A.3    Tsukita, S.4    Fujiyoshi, Y.5
  • 55
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse, M., Sasaki, H. & Tsukita, S. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J. Cell Biol. 147, 891-903 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 56
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight-junction strands: Leading or supporting players?
    • Tsukita, S. & Furuse, M. Occludin and claudins in tight-junction strands: leading or supporting players? Trends Cell Biol. 9, 268-273 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 57
    • 84928204290 scopus 로고    scopus 로고
    • Transmembrane proteins of the tight junctions at the blood-brain barrier: Structural and functional aspects
    • Haseloff, R. F., Dithmer, S., Winkler, L., Wolburg, H. & Blasig, I. E. Transmembrane proteins of the tight junctions at the blood-brain barrier: structural and functional aspects. Semin. Cell Dev. Biol. 38, 16-25 (2015).
    • (2015) Semin. Cell Dev. Biol. , vol.38 , pp. 16-25
    • Haseloff, R.F.1    Dithmer, S.2    Winkler, L.3    Wolburg, H.4    Blasig, I.E.5
  • 58
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • Shen, L., Weber, C. R. & Turner, J. R. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J. Cell Biol. 181, 683-695 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3
  • 59
    • 0020079785 scopus 로고
    • On tight junction structure
    • Pinto da Silva, P. & Kachar, B. On tight junction structure. Cell 28, 441-450 (1982).
    • (1982) Cell , vol.28 , pp. 441-450
    • Pinto Da-Silva, P.1    Kachar, B.2
  • 60
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V. & Kozlov, M. M. Membrane hemifusion: crossing a chasm in two leaps. Cell 123, 375-382 (2005).
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 61
    • 0020058236 scopus 로고
    • Evidence for the lipidic nature of tight junction strands
    • Kachar, B. & Reese, T. S. Evidence for the lipidic nature of tight junction strands. Nature 296, 464-466 (1982).
    • (1982) Nature , vol.296 , pp. 464-466
    • Kachar, B.1    Reese, T.S.2
  • 62
    • 0027417219 scopus 로고
    • Cytochemical evidence for the presence of phospholipids in epithelial tight junction strands
    • Kan, F. W. Cytochemical evidence for the presence of phospholipids in epithelial tight junction strands. J. Histochem. Cytochem. 41, 649-656 (1993).
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 649-656
    • Kan, F.W.1
  • 63
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of intergral membrane proteins: Aplication to the immunogold labeling of intercellular junctional complex
    • Fujimoto, K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of intergral membrane proteins: aplication to the immunogold labeling of intercellular junctional complex. J. Cell Sci. 108, 3443-3449 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 64
    • 84876075035 scopus 로고    scopus 로고
    • In tight junctions, claudins regulate the interactions between occludin, tricellulin and marvelD3, which, inversely, modulate claudin oligomerization
    • Cording, J. et al. In tight junctions, claudins regulate the interactions between occludin, tricellulin and marvelD3, which, inversely, modulate claudin oligomerization. J. Cell Sci. 126, 554-564 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 554-564
    • Cording, J.1
  • 65
    • 0022516245 scopus 로고
    • The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next
    • van Meer, G., Gumbiner, B. & Simons, K. The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next. Nature 322, 639-641 (1986).
    • (1986) Nature , vol.322 , pp. 639-641
    • Van Meer, G.1    Gumbiner, B.2    Simons, K.3
  • 66
    • 0028235916 scopus 로고
    • Translational diffusion measurements of a fluorescent phospholipid between MDCK-I cells support the lipid model of the tight junctions
    • Grebenkamper, K. & Galla, H. J. Translational diffusion measurements of a fluorescent phospholipid between MDCK-I cells support the lipid model of the tight junctions. Chem. Phys. Lipids 71, 133-143 (1994).
    • (1994) Chem. Phys. Lipids , vol.71 , pp. 133-143
    • Grebenkamper, K.1    Galla, H.J.2
  • 67
    • 0034068866 scopus 로고    scopus 로고
    • Tight junctions are membrane microdomains
    • Nusrat, A. et al. Tight junctions are membrane microdomains. J. Cell Sci. 113, 1771-1781 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1771-1781
    • Nusrat, A.1
  • 68
    • 17644421069 scopus 로고    scopus 로고
    • Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins
    • Lambert, D., O'Neill, C. A. & Padfield, P. J. Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins. Biochem. J. 387, 553-560 (2005).
    • (2005) Biochem. J. , vol.387 , pp. 553-560
    • Lambert, D.1    O'Neill, C.A.2    Padfield, P.J.3
  • 69
    • 34250800879 scopus 로고    scopus 로고
    • Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin
    • Lynch, R. D. et al. Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin. Exp. Cell Res. 313, 2597-2610 (2007).
    • (2007) Exp. Cell Res. , vol.313 , pp. 2597-2610
    • Lynch, R.D.1
  • 70
    • 0032126082 scopus 로고    scopus 로고
    • Tight junctions and the experimental modifications of lipid content
    • Calderon, V. et al. Tight junctions and the experimental modifications of lipid content. J. Membr. Biol. 164, 59-69 (1998).
    • (1998) J. Membr. Biol. , vol.164 , pp. 59-69
    • Calderon, V.1
  • 71
    • 0032840311 scopus 로고    scopus 로고
    • Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance
    • Francis, S. A. et al. Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance. Eur. J. Cell Biol. 78, 473-484 (1999).
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 473-484
    • Francis, S.A.1
  • 72
    • 84912101029 scopus 로고    scopus 로고
    • The emergence of the concept of tight junctions and physiological regulation by ouabain
    • Larre, I., Ponce, A., Franco, M. & Cereijido, M. The emergence of the concept of tight junctions and physiological regulation by ouabain. Semin. Cell Dev. Biol. 36, 149-156 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 149-156
    • Larre, I.1    Ponce, A.2    Franco, M.3    Cereijido, M.4
  • 73
    • 84924120436 scopus 로고    scopus 로고
    • Claudins and the kidney
    • Yu, A. S. Claudins and the kidney. J. Am. Soc. Nephrol. 26, 11-19 (2015).
    • (2015) J. Am. Soc. Nephrol. , vol.26 , pp. 11-19
    • Yu, A.S.1
  • 74
    • 60549090106 scopus 로고    scopus 로고
    • Molecular basis for cation selectivity in claudin-2-based paracellular pores: Identification of an electrostatic interaction site
    • Yu, A. S. et al. Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site. J. Gen. Physiol. 133, 111-127 (2009).
    • (2009) J. Gen. Physiol. , vol.133 , pp. 111-127
    • Yu, A.S.1
  • 75
    • 84940894920 scopus 로고    scopus 로고
    • Conceptual barriers to understanding physical barriers
    • Lingaraju, A. et al. Conceptual barriers to understanding physical barriers. Semin. Cell Dev. Biol. 42, 13-21 (2015).
    • (2015) Semin. Cell Dev. Biol. , vol.42 , pp. 13-21
    • Lingaraju, A.1
  • 76
    • 77249110786 scopus 로고    scopus 로고
    • Dynamics and functions of tight junctions
    • Steed, E., Balda, M. S. & Matter, K. Dynamics and functions of tight junctions. Trends Cell Biol. 20, 142-149 (2010).
    • (2010) Trends Cell Biol. , vol.20 , pp. 142-149
    • Steed, E.1    Balda, M.S.2    Matter, K.3
  • 77
    • 0033516683 scopus 로고    scopus 로고
    • 2+ resorption
    • 2+ resorption. Science 285, 103-106 (1999).
    • (1999) Science , vol.285 , pp. 103-106
    • Simon, D.B.1
  • 78
    • 0033766722 scopus 로고    scopus 로고
    • Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells
    • McCarthy, K. M. et al. Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells. J. Cell Sci. 113, 3387-3398 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3387-3398
    • McCarthy, K.M.1
  • 79
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice
    • Furuse, M. et al. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J. Cell Biol. 156, 1099-1111 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 1099-1111
    • Furuse, M.1
  • 80
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • Amasheh, S. et al. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J. Cell Sci. 115, 4969-4976 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 4969-4976
    • Amasheh, S.1
  • 81
    • 0035897412 scopus 로고    scopus 로고
    • Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney i cells
    • Furuse, M., Furuse, K., Sasaki, H. & Tsukita, S. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J. Cell Biol. 153, 263-272 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 82
    • 33845370795 scopus 로고    scopus 로고
    • Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities
    • Van Itallie, C. M. et al. Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities. Am. J. Physiol. Renal Physiol. 291, F1288-F1299 (2006).
    • (2006) Am. J. Physiol. Renal Physiol. , vol.291 , pp. F1288-F1299
    • Van Itallie, C.M.1
  • 83
    • 67249117191 scopus 로고    scopus 로고
    • Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function
    • Gunzel, D. et al. Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function. J. Cell Sci. 122, 1507-1517 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1507-1517
    • Gunzel, D.1
  • 84
    • 84864277469 scopus 로고    scopus 로고
    • Claudin-17 forms tight junction channels with distinct anion selectivity
    • Krug, S. M. et al. Claudin-17 forms tight junction channels with distinct anion selectivity. Cell. Mol. Life Sci. 69, 2765-2778 (2012).
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 2765-2778
    • Krug, S.M.1
  • 85
    • 84912105184 scopus 로고    scopus 로고
    • Tight junction, selective permeability, and related diseases
    • Krug, S. M., Schulzke, J. D. & Fromm, M. Tight junction, selective permeability, and related diseases. Semin. Cell Dev. Biol. 36, 166-176 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 166-176
    • Krug, S.M.1    Schulzke, J.D.2    Fromm, M.3
  • 87
    • 70350399482 scopus 로고    scopus 로고
    • Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis
    • Angelow, S. & Yu, A. S. Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis. J. Biol. Chem. 284, 29205-29217 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 29205-29217
    • Angelow, S.1    Yu, A.S.2
  • 88
    • 84878506887 scopus 로고    scopus 로고
    • Claudins and the modulation of tight junction permeability
    • Gunzel, D. & Yu, A. S. Claudins and the modulation of tight junction permeability. Physiol. Rev. 93, 525-569 (2013).
    • (2013) Physiol. Rev. , vol.93 , pp. 525-569
    • Gunzel, D.1    Yu, A.S.2
  • 89
    • 84957922490 scopus 로고    scopus 로고
    • Claudin-2-dependent paracellular channels are dynamically gated
    • Weber, C. R. et al. Claudin-2-dependent paracellular channels are dynamically gated. eLife 4, e09906 (2015).
    • (2015) ELife , vol.4 , pp. e09906
    • Weber, C.R.1
  • 90
    • 79952286129 scopus 로고    scopus 로고
    • + deficiency and glucose malabsorption in mouse small intestine
    • + deficiency and glucose malabsorption in mouse small intestine. Gastroenterology 140, 913-923 (2011).
    • (2011) Gastroenterology , vol.140 , pp. 913-923
    • Tamura, A.1
  • 91
  • 92
    • 17744380785 scopus 로고    scopus 로고
    • Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29
    • Wilcox, E. R. et al. Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29. Cell 104, 165-172 (2001).
    • (2001) Cell , vol.104 , pp. 165-172
    • Wilcox, E.R.1
  • 93
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: Role of the first extracellular domain of claudin-5
    • Wen, H., Watry, D. D., Marcondes, M. C. & Fox, H. S. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 24, 8408-8417 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8408-8417
    • Wen, H.1    Watry, D.D.2    Marcondes, M.C.3    Fox, H.S.4
  • 94
    • 84940889137 scopus 로고    scopus 로고
    • Assembly and function of claudins: Structure-function relationships based on homology models and crystal structures
    • Krause, G., Protze, J. & Piontek, J. Assembly and function of claudins: Structure-function relationships based on homology models and crystal structures. Semin. Cell Dev. Biol. 42, 3-12 (2015).
    • (2015) Semin. Cell Dev. Biol. , vol.42 , pp. 3-12
    • Krause, G.1    Protze, J.2    Piontek, J.3
  • 95
    • 6944227814 scopus 로고    scopus 로고
    • - permeability is regulated by WNK4 kinase: Insight into normal physiology and hypertension
    • - permeability is regulated by WNK4 kinase: insight into normal physiology and hypertension. Proc. Natl Acad. Sci. USA 101, 14877-14882 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14877-14882
    • Kahle, K.T.1
  • 96
    • 17944373014 scopus 로고    scopus 로고
    • Human hypertension caused by mutations in WNK kinases
    • Wilson, F. H. et al. Human hypertension caused by mutations in WNK kinases. Science 293, 1107-1112 (2001).
    • (2001) Science , vol.293 , pp. 1107-1112
    • Wilson, F.H.1
  • 97
    • 11144354175 scopus 로고    scopus 로고
    • Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins
    • Yamauchi, K. et al. Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins. Proc. Natl Acad. Sci. USA 101, 4690-4694 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4690-4694
    • Yamauchi, K.1
  • 98
    • 33748430618 scopus 로고    scopus 로고
    • Overexpression of human WNK1 increases paracellular chloride permeability and phosphorylation of claudin-4 in MDCKII cells
    • Ohta, A. et al. Overexpression of human WNK1 increases paracellular chloride permeability and phosphorylation of claudin-4 in MDCKII cells. Biochem. Biophys. Res. Commun. 349, 804-808 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 804-808
    • Ohta, A.1
  • 99
    • 34547112045 scopus 로고    scopus 로고
    • WNK4 phosphorylates ser(206) of claudin-7 and promotes paracellular Cl(-) permeability
    • Tatum, R. et al. WNK4 phosphorylates ser(206) of claudin-7 and promotes paracellular Cl(-) permeability. FEBS Lett. 581, 3887-3891 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 3887-3891
    • Tatum, R.1
  • 100
    • 0019806209 scopus 로고
    • Membrane asymmetry in epithelia: Is the tight junction a barrier to diffusion in the plasma membrane?
    • Dragsen, P. R., Blumenthal, R. & Handler, J. S. Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane? Nature 294, 718-722 (1981).
    • (1981) Nature , vol.294 , pp. 718-722
    • Dragsen, P.R.1    Blumenthal, R.2    Handler, J.S.3
  • 101
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells
    • van Meer, G. & Simons, K. The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J. 5, 1455-1464 (1986).
    • (1986) EMBO J. , vol.5 , pp. 1455-1464
    • Van Meer, G.1    Simons, K.2
  • 102
    • 0027339375 scopus 로고
    • Uncoupling of the molecular 'fence' and paracellular 'gate' functions in epithelial tight junctions
    • Mandel, L. J., Bacallao, R. & Zampighi, G. Uncoupling of the molecular 'fence' and paracellular 'gate' functions in epithelial tight junctions. Nature 361, 552-555 (1993).
    • (1993) Nature , vol.361 , pp. 552-555
    • Mandel, L.J.1    Bacallao, R.2    Zampighi, G.3
  • 103
    • 10944228240 scopus 로고    scopus 로고
    • The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells
    • Nava, P., Lopez, S., Arias, C. F., Islas, S. & Gonzalez-Mariscal, L. The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells. J. Cell Sci. 117, 5509-5519 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 5509-5519
    • Nava, P.1    Lopez, S.2    Arias, C.F.3    Islas, S.4    Gonzalez-Mariscal, L.5
  • 104
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda, M. S. et al. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J. Cell Biol. 134, 1031-1049 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1
  • 105
    • 33747155076 scopus 로고    scopus 로고
    • ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation
    • Umeda, K. et al. ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126, 741-754 (2006).
    • (2006) Cell , vol.126 , pp. 741-754
    • Umeda, K.1
  • 106
    • 84863353883 scopus 로고    scopus 로고
    • Lipid polarity is maintained in absence of tight junctions
    • Ikenouchi, J. et al. Lipid polarity is maintained in absence of tight junctions. J. Biol. Chem. 287, 9525-9533 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 9525-9533
    • Ikenouchi, J.1
  • 107
    • 0017891781 scopus 로고
    • Polarized monolayers formed by epithelial cells on a permeable and translucent support
    • Cereijido, M., Robbins, E. S., Dolan, W. J., Rotunno, C. A. & Sabatini, D. D. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J. Cell Biol. 77, 853-880 (1978).
    • (1978) J. Cell Biol. , vol.77 , pp. 853-880
    • Cereijido, M.1    Robbins, E.S.2    Dolan, W.J.3    Rotunno, C.A.4    Sabatini, D.D.5
  • 108
    • 0025911428 scopus 로고
    • Assembly and sealing of tight junctions: Possible participation of G-proteins, phospholipase C, protein kinase C and calmodulin
    • Balda, M. S. et al. Assembly and sealing of tight junctions: possible participation of G-proteins, phospholipase C, protein kinase C and calmodulin. J. Mem. Biol. 122, 193-202 (1991).
    • (1991) J. Mem. Biol. , vol.122 , pp. 193-202
    • Balda, M.S.1
  • 109
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran, A. K., Hojo, M., Huima, T. & Rodriguez-Boulan, E. Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J. Cell Biol. 132, 451-463 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 110
    • 84883301688 scopus 로고    scopus 로고
    • ZO-1 recruitment to α-catenin - A novel mechanism for coupling the assembly of tight junctions to adherens junctions
    • Maiers, J. L., Peng, X., Fanning, A. S. & DeMali, K. A. ZO-1 recruitment to α-catenin - a novel mechanism for coupling the assembly of tight junctions to adherens junctions. J. Cell Sci. 126, 3904-3915 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 3904-3915
    • Maiers, J.L.1    Peng, X.2    Fanning, A.S.3    DeMali, K.A.4
  • 111
    • 0037206934 scopus 로고    scopus 로고
    • Involvement of nectin in the localization of junctional adhesion molecule at tight junctions
    • Fukuhara, A. et al. Involvement of nectin in the localization of junctional adhesion molecule at tight junctions. Oncogene 21, 7642-7655 (2002).
    • (2002) Oncogene , vol.21 , pp. 7642-7655
    • Fukuhara, A.1
  • 112
    • 84899432057 scopus 로고    scopus 로고
    • Tight junction dynamics: The role of junctional adhesion molecules (JAMs)
    • Garrido-Urbani, S., Bradfield, P. F. & Imhof, B. A. Tight junction dynamics: the role of junctional adhesion molecules (JAMs). Cell Tissue Res. 355, 701-715 (2014).
    • (2014) Cell Tissue Res. , vol.355 , pp. 701-715
    • Garrido-Urbani, S.1    Bradfield, P.F.2    Imhof, B.A.3
  • 113
    • 84983628438 scopus 로고    scopus 로고
    • Beyond Ussing's chambers: Contemporary thoughts on integration of transepithelial transport
    • Herrmann, J. R. & Turner, J. R. Beyond Ussing's chambers: contemporary thoughts on integration of transepithelial transport. Am. J. Physiol. Cell Physiol. 310, C423-C431 (2016).
    • (2016) Am. J. Physiol. Cell Physiol. , vol.310 , pp. C423-C431
    • Herrmann, J.R.1    Turner, J.R.2
  • 114
    • 79551612886 scopus 로고    scopus 로고
    • Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis
    • Terry, S. J. et al. Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis. Nat. Cell Biol. 13, 159-166 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 159-166
    • Terry, S.J.1
  • 115
    • 84862535878 scopus 로고    scopus 로고
    • Rho GTP exchange factor ARHGEF11 regulates the integrity of epithelial junctions by connecting ZO-1 and RhoA-myosin II signaling
    • Itoh, M., Tsukita, S., Yamazaki, Y. & Sugimoto, H. Rho GTP exchange factor ARHGEF11 regulates the integrity of epithelial junctions by connecting ZO-1 and RhoA-myosin II signaling. Proc. Natl Acad. Sci. USA 109, 9905-9910 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9905-9910
    • Itoh, M.1    Tsukita, S.2    Yamazaki, Y.3    Sugimoto, H.4
  • 116
    • 84925358255 scopus 로고    scopus 로고
    • ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation
    • Tornavaca, O. et al. ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation. J. Cell Biol. 208, 821-838 (2015).
    • (2015) J. Cell Biol. , vol.208 , pp. 821-838
    • Tornavaca, O.1
  • 117
    • 33749548025 scopus 로고    scopus 로고
    • Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells
    • Otani, T., Ichii, T., Aono, S. & Takeichi, M. Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells. J. Cell Biol. 175, 135-146 (2006).
    • (2006) J. Cell Biol. , vol.175 , pp. 135-146
    • Otani, T.1    Ichii, T.2    Aono, S.3    Takeichi, M.4
  • 118
    • 84910023987 scopus 로고    scopus 로고
    • Tricellulin regulates junctional tension of epithelial cells at tricellular contacts through Cdc42
    • Oda, Y., Otani, T., Ikenouchi, J. & Furuse, M. Tricellulin regulates junctional tension of epithelial cells at tricellular contacts through Cdc42. J. Cell Sci. 127, 4201-4212 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 4201-4212
    • Oda, Y.1    Otani, T.2    Ikenouchi, J.3    Furuse, M.4
  • 119
    • 84859827184 scopus 로고    scopus 로고
    • Apicobasal polarity in the kidney
    • Schluter, M. A. & Margolis, B. Apicobasal polarity in the kidney. Exp. Cell Res. 318, 1033-1039 (2012).
    • (2012) Exp. Cell Res. , vol.318 , pp. 1033-1039
    • Schluter, M.A.1    Margolis, B.2
  • 120
    • 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
    • Itoh, M. et al. Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J. Cell Biol. 154, 491-497 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 491-497
    • Itoh, M.1
  • 121
    • 52049125202 scopus 로고    scopus 로고
    • Regulation of epithelial and endothelial junctions by PAR proteins
    • Ebnet, K., Iden, S., Gerke, V. & Suzuki, A. Regulation of epithelial and endothelial junctions by PAR proteins. Front. Biosci. 13, 6520-6536 (2008).
    • (2008) Front. Biosci. , vol.13 , pp. 6520-6536
    • Ebnet, K.1    Iden, S.2    Gerke, V.3    Suzuki, A.4
  • 122
    • 3242702211 scopus 로고    scopus 로고
    • Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Cζ (PKCζ) and regulates PKCζ activity
    • Liu, X. F., Ishida, H., Raziuddin, R. & Miki, T. Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Cζ (PKCζ) and regulates PKCζ activity. Mol. Cell. Biol. 24, 6665-6675 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6665-6675
    • Liu, X.F.1    Ishida, H.2    Raziuddin, R.3    Miki, T.4
  • 123
    • 33646136870 scopus 로고    scopus 로고
    • A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells
    • Wells, C. D. et al. A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells. Cell 125, 535-548 (2006).
    • (2006) Cell , vol.125 , pp. 535-548
    • Wells, C.D.1
  • 124
    • 84866385977 scopus 로고    scopus 로고
    • Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex
    • Elbediwy, A. et al. Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex. J. Cell Biol. 198, 677-693 (2012).
    • (2012) J. Cell Biol. , vol.198 , pp. 677-693
    • Elbediwy, A.1
  • 125
    • 84891896382 scopus 로고    scopus 로고
    • Dbl3 drives Cdc42 signaling at the apical margin to regulate junction position and apical differentiation
    • Zihni, C. et al. Dbl3 drives Cdc42 signaling at the apical margin to regulate junction position and apical differentiation. J. Cell Biol. 204, 111-127 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 111-127
    • Zihni, C.1
  • 126
    • 77951911203 scopus 로고    scopus 로고
    • APKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells
    • Morais-de-Sa, E., Mirouse, V. & St Johnston, D. aPKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells. Cell 141, 509-523 (2010).
    • (2010) Cell , vol.141 , pp. 509-523
    • Morais-De-Sa, E.1    Mirouse, V.2    St Johnston, D.3
  • 127
    • 77955714079 scopus 로고    scopus 로고
    • Crumbs/DaPKC-dependent apical exclusion of Bazooka promotes photoreceptor polarity remodeling
    • Walther, R. F. & Pichaud, F. Crumbs/DaPKC-dependent apical exclusion of Bazooka promotes photoreceptor polarity remodeling. Curr. Biol. 20, 1065-1074 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 1065-1074
    • Walther, R.F.1    Pichaud, F.2
  • 128
    • 26244441572 scopus 로고    scopus 로고
    • PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells
    • Michel, D. et al. PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells. J. Cell Sci. 118, 4049-4057 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4049-4057
    • Michel, D.1
  • 129
    • 65449170864 scopus 로고    scopus 로고
    • Similar and distinct properties of MUPP1 and Patj, two homologous PDZ domain-containing tight-junction proteins
    • Adachi, M. et al. Similar and distinct properties of MUPP1 and Patj, two homologous PDZ domain-containing tight-junction proteins. Mol. Cell. Biol. 29, 2372-2389 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2372-2389
    • Adachi, M.1
  • 130
    • 0037178864 scopus 로고    scopus 로고
    • The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • Roh, M. H., Liu, C. J., Laurinec, S. & Margolis, B. The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J. Biol. Chem. 277, 27501-27509 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 27501-27509
    • Roh, M.H.1    Liu, C.J.2    Laurinec, S.3    Margolis, B.4
  • 131
    • 1542283794 scopus 로고    scopus 로고
    • CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells
    • Lemmers, C. et al. CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells. Mol. Biol. Cell 15, 1324-1333 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1324-1333
    • Lemmers, C.1
  • 133
    • 78650895035 scopus 로고    scopus 로고
    • Angiomotin is a novel Hippo pathway component that inhibits YAP oncoprotein
    • Zhao, B. et al. Angiomotin is a novel Hippo pathway component that inhibits YAP oncoprotein. Genes Dev. 25, 51-63 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 51-63
    • Zhao, B.1
  • 134
    • 78649892579 scopus 로고    scopus 로고
    • Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling
    • Oka, T. et al. Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling. Biochem. J. 432, 461-472 (2010).
    • (2010) Biochem. J. , vol.432 , pp. 461-472
    • Oka, T.1
  • 135
    • 84981240003 scopus 로고    scopus 로고
    • Hippo pathway elements co-localize with occludin: A possible sensor system in pancreatic epithelial cells
    • Cravo, A. S. et al. Hippo pathway elements co-localize with occludin: a possible sensor system in pancreatic epithelial cells. Tissue Barriers 3, e1037948 (2015).
    • (2015) Tissue Barriers , vol.3 , pp. e1037948
    • Cravo, A.S.1
  • 136
    • 84938744596 scopus 로고    scopus 로고
    • PARD3 induces TAZ activation and cell growth by promoting LATS1 and PP1 interaction
    • Lv, X. B. et al. PARD3 induces TAZ activation and cell growth by promoting LATS1 and PP1 interaction. EMBO Rep. 16, 975-985 (2015).
    • (2015) EMBO Rep. , vol.16 , pp. 975-985
    • Lv, X.B.1
  • 137
    • 79953753962 scopus 로고    scopus 로고
    • A tight junction-associated Merlin-angiomotin complex mediates Merlin's regulation of mitogenic signaling and tumor suppressive functions
    • Yi, C. et al. A tight junction-associated Merlin-angiomotin complex mediates Merlin's regulation of mitogenic signaling and tumor suppressive functions. Cancer Cell 19, 527-540 (2011).
    • (2011) Cancer Cell , vol.19 , pp. 527-540
    • Yi, C.1
  • 138
    • 77954945373 scopus 로고    scopus 로고
    • The Merlin/NF2 tumor suppressor functions through the YAP oncoprotein to regulate tissue homeostasis in mammals
    • Zhang, N. et al. The Merlin/NF2 tumor suppressor functions through the YAP oncoprotein to regulate tissue homeostasis in mammals. Dev. Cell 19, 27-38 (2010).
    • (2010) Dev. Cell , vol.19 , pp. 27-38
    • Zhang, N.1
  • 139
    • 0037415643 scopus 로고    scopus 로고
    • The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density
    • Balda, M. S., Garrett, M. D. & Matter, K. The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J. Cell Biol. 160, 423-432 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 423-432
    • Balda, M.S.1    Garrett, M.D.2    Matter, K.3
  • 140
    • 70449699678 scopus 로고    scopus 로고
    • The Y-box factor ZONAB/DbpA associates with GEF-H1/Lfc and mediates Rho-stimulated transcription
    • Nie, M., Aijaz, S., Leefa Chong San, I. V., Balda, M. S. & Matter, K. The Y-box factor ZONAB/DbpA associates with GEF-H1/Lfc and mediates Rho-stimulated transcription. EMBO Rep. 10, 1125-1131 (2009).
    • (2009) EMBO Rep. , vol.10 , pp. 1125-1131
    • Nie, M.1    Aijaz, S.2    Leefa Chong-San, I.V.3    Balda, M.S.4    Matter, K.5
  • 141
    • 33846136942 scopus 로고    scopus 로고
    • Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin
    • Kavanagh, E. et al. Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin. J. Cell Sci. 119, 5098-5105 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 5098-5105
    • Kavanagh, E.1
  • 142
    • 13244260780 scopus 로고    scopus 로고
    • RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity
    • Frankel, P. et al. RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. EMBO J. 24, 54-62 (2005).
    • (2005) EMBO J. , vol.24 , pp. 54-62
    • Frankel, P.1
  • 143
    • 84902477424 scopus 로고    scopus 로고
    • Nuclear distribution of claudin-2 increases cell proliferation in human lung adenocarcinoma cells
    • Ikari, A. et al. Nuclear distribution of claudin-2 increases cell proliferation in human lung adenocarcinoma cells. Biochim. Biophys. Acta 1843, 2079-2088 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 2079-2088
    • Ikari, A.1
  • 144
    • 36249011285 scopus 로고    scopus 로고
    • Phosphatidylethanol accumulation promotes intestinal hyperplasia by inducing ZONAB-mediated cell density increase in response to chronic ethanol exposure
    • Pannequin, J. et al. Phosphatidylethanol accumulation promotes intestinal hyperplasia by inducing ZONAB-mediated cell density increase in response to chronic ethanol exposure. Mol. Cancer Res. 5, 1147-1157 (2007).
    • (2007) Mol. Cancer Res. , vol.5 , pp. 1147-1157
    • Pannequin, J.1
  • 145
    • 77249166583 scopus 로고    scopus 로고
    • Symplekin promotes tumorigenicity by up-regulating claudin-2 expression
    • Buchert, M. et al. Symplekin promotes tumorigenicity by up-regulating claudin-2 expression. Proc. Natl Acad. Sci. USA 107, 2628-2633 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2628-2633
    • Buchert, M.1
  • 146
    • 33644773928 scopus 로고    scopus 로고
    • Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the ZO-1-regulated transcription factor ZONAB/DbpA
    • Sourisseau, T. et al. Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the ZO-1-regulated transcription factor ZONAB/DbpA. Mol. Cell. Biol. 26, 2387-2398 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2387-2398
    • Sourisseau, T.1
  • 147
    • 84918582197 scopus 로고    scopus 로고
    • CFTR interacts with ZO-1 to regulate tight junction assembly and epithelial differentiation through the ZONAB pathway
    • Ruan, Y. C. et al. CFTR interacts with ZO-1 to regulate tight junction assembly and epithelial differentiation through the ZONAB pathway. J. Cell Sci. 127, 4396-4408 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 4396-4408
    • Ruan, Y.C.1
  • 148
    • 79251617967 scopus 로고    scopus 로고
    • Bves modulates tight junction associated signaling
    • Russ, P. K. et al. Bves modulates tight junction associated signaling. PLoS ONE 6, e14563 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e14563
    • Russ, P.K.1
  • 149
    • 84937641208 scopus 로고    scopus 로고
    • Bradykinin increased the permeability of BTB via NOS/NO/ZONAB-mediating down-regulation of claudin-5 and occludin
    • Liu, L. B. et al. Bradykinin increased the permeability of BTB via NOS/NO/ZONAB-mediating down-regulation of claudin-5 and occludin. Biochem. Biophys. Res. Commun. 464, 118-125 (2015).
    • (2015) Biochem. Biophys. Res. Commun. , vol.464 , pp. 118-125
    • Liu, L.B.1
  • 150
    • 84968615883 scopus 로고    scopus 로고
    • ZO-2 silencing induces renal hypertrophy through a cell cycle mechanism and the activation of YAP and the mTOR pathway
    • Dominguez-Calderon, A. et al. ZO-2 silencing induces renal hypertrophy through a cell cycle mechanism and the activation of YAP and the mTOR pathway. Mol. Biol. Cell 27, 1581-1595 (2016).
    • (2016) Mol. Biol. Cell , vol.27 , pp. 1581-1595
    • Dominguez-Calderon, A.1
  • 151
    • 0034695923 scopus 로고    scopus 로고
    • Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin
    • Li, D. & Mrsny, R. J. Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin. J. Cell Biol. 148, 791-800 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 791-800
    • Li, D.1    Mrsny, R.J.2
  • 152
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • Nusrat, A. et al. The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction. J. Biol. Chem. 275, 29816-29822 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29816-29822
    • Nusrat, A.1
  • 153
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodiles, M. et al. High-throughput mapping of a dynamic signaling network in mammalian cells. Science 307, 1621-1625 (2005).
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodiles, M.1
  • 154
    • 50849091289 scopus 로고    scopus 로고
    • The C. Elegans zonula occludens ortholog cooperates with the cadherin complex to recruit actin during morphogenesis
    • Lockwood, C., Zaidel-Bar, R. & Hardin, J. The C. elegans zonula occludens ortholog cooperates with the cadherin complex to recruit actin during morphogenesis. Curr. Biol. 18, 1333-1337 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1333-1337
    • Lockwood, C.1    Zaidel-Bar, R.2    Hardin, J.3
  • 155
    • 84863577279 scopus 로고    scopus 로고
    • Stress- and Rho-activated ZO-1-associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival
    • Nie, M., Balda, M. S. & Matter, K. Stress- and Rho-activated ZO-1-associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival. Proc. Natl Acad. Sci. USA 109, 10897-10902 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 10897-10902
    • Nie, M.1    Balda, M.S.2    Matter, K.3
  • 156
    • 84901191613 scopus 로고    scopus 로고
    • Trans-dimerization of JAM-A regulates Rap2 and is mediated by a domain that is distinct from the cis-dimerization interface
    • Monteiro, A. C. et al. Trans-dimerization of JAM-A regulates Rap2 and is mediated by a domain that is distinct from the cis-dimerization interface. Mol. Biol. Cell 25, 1574-1585 (2014).
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1574-1585
    • Monteiro, A.C.1
  • 157
    • 65249125248 scopus 로고    scopus 로고
    • Junctional adhesion molecule A interacts with Afadin and PDZ-GEF2 to activate Rap1A, regulate β1 integrin levels, and enhance cell migration
    • Severson, E. A., Lee, W. Y., Capaldo, C. T., Nusrat, A. & Parkos, C. A. Junctional adhesion molecule A interacts with Afadin and PDZ-GEF2 to activate Rap1A, regulate β1 integrin levels, and enhance cell migration. Mol. Biol. Cell 20, 1916-1925 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1916-1925
    • Severson, E.A.1    Lee, W.Y.2    Capaldo, C.T.3    Nusrat, A.4    Parkos, C.A.5
  • 158
    • 61949276292 scopus 로고    scopus 로고
    • JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling
    • Cera, M. R. et al. JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling. J. Cell Sci. 122, 268-277 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 268-277
    • Cera, M.R.1
  • 159
    • 84860389407 scopus 로고    scopus 로고
    • Breast cancer cell migration is regulated through junctional adhesion molecule-A-mediated activation of Rap1 GTPase
    • McSherry, E. A., Brennan, K., Hudson, L., Hill, A. D. K. & Hopkins, A. M. Breast cancer cell migration is regulated through junctional adhesion molecule-A-mediated activation of Rap1 GTPase. Breast Cancer Res. 13, R31 (2011).
    • (2011) Breast Cancer Res. , vol.13 , pp. R31
    • McSherry, E.A.1    Brennan, K.2    Hudson, L.3    Hill, A.D.K.4    Hopkins, A.M.5
  • 160
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation
    • Kuo, J. C. et al. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13, 383-393 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 383-393
    • Kuo, J.C.1
  • 161
    • 0032567341 scopus 로고    scopus 로고
    • Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
    • Ren, Y., Li, R., Zheng, Y. & Busch, H. Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J. Biol. Chem. 273, 34954-34960 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 34954-34960
    • Ren, Y.1    Li, R.2    Zheng, Y.3    Busch, H.4
  • 162
    • 0036228955 scopus 로고    scopus 로고
    • Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
    • Krendel, M., Zenke, F. T. & Bokoch, G. M. Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat. Cell Biol. 4, 294-301 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 294-301
    • Krendel, M.1    Zenke, F.T.2    Bokoch, G.M.3
  • 163
    • 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
    • Aijaz, S., D'Atri, F., Citi, S., Balda, M. S. & Matter, K. 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, 777-786 (2005).
    • (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
  • 164
    • 84913609685 scopus 로고    scopus 로고
    • GEF-H1 controls focal adhesion signaling that regulates mesenchymal stem cell lineage commitment
    • Huang, I. H. et al. GEF-H1 controls focal adhesion signaling that regulates mesenchymal stem cell lineage commitment. J. Cell Sci. 127, 4186-4200 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 4186-4200
    • Huang, I.H.1
  • 165
    • 79957889032 scopus 로고    scopus 로고
    • The Rho GEFs LARG and GEF-H1 regulate the mechanical response to force on integrins
    • Guilluy, C. et al. The Rho GEFs LARG and GEF-H1 regulate the mechanical response to force on integrins. Nat. Cell Biol. 13, 722-727 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 722-727
    • Guilluy, C.1
  • 166
    • 0035897413 scopus 로고    scopus 로고
    • OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and β1 integrin and regulates proliferation and migration of oligodendrocytes
    • Tiwari-Woodruff, S. K. et al. OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and β1 integrin and regulates proliferation and migration of oligodendrocytes. J. Cell Biol. 153, 295-305 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 295-305
    • Tiwari-Woodruff, S.K.1
  • 167
    • 84935906852 scopus 로고    scopus 로고
    • A non-tight junction function of claudin-7-interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment
    • Lu, Z. et al. A non-tight junction function of claudin-7-Interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment. Mol. Cancer 14, 120 (2015).
    • (2015) Mol. Cancer , vol.14 , pp. 120
    • Lu, Z.1
  • 168
    • 22144499164 scopus 로고    scopus 로고
    • Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer
    • Dhawan, P. et al. Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer. J. Clin. Invest. 115, 1765-1776 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 1765-1776
    • Dhawan, P.1
  • 169
    • 84875465330 scopus 로고    scopus 로고
    • Tetraspanin CD9 links junctional adhesion molecule-A to αvβ3 integrin to mediate basic fibroblast growth factor-specific angiogenic signaling
    • Peddibhotla, S. S. et al. Tetraspanin CD9 links junctional adhesion molecule-A to αvβ3 integrin to mediate basic fibroblast growth factor-specific angiogenic signaling. Mol. Biol. Cell 24, 933-944 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 933-944
    • Peddibhotla, S.S.1
  • 171
    • 84912126840 scopus 로고    scopus 로고
    • Molecular organization and function of invertebrate occluding junctions
    • Izumi, Y. & Furuse, M. Molecular organization and function of invertebrate occluding junctions. Semin. Cell Dev. Biol. 36, 186-193 (2014).
    • (2014) Semin. Cell Dev. Biol. , vol.36 , pp. 186-193
    • Izumi, Y.1    Furuse, M.2
  • 172
    • 79960716090 scopus 로고    scopus 로고
    • Claudin family proteins in Caenorhabditis elegans
    • Simske, J. S. & Hardin, J. Claudin family proteins in Caenorhabditis elegans. Methods Mol. Biol. 762, 147-169 (2011).
    • (2011) Methods Mol. Biol. , vol.762 , pp. 147-169
    • Simske, J.S.1    Hardin, J.2
  • 173
    • 1642458089 scopus 로고    scopus 로고
    • Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control
    • Wu, V. M., Schulte, J., Hirschi, A., Tepass, U. & Beitel, G. J. Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control. J. Cell Biol. 164, 313-323 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 313-323
    • Wu, V.M.1    Schulte, J.2    Hirschi, A.3    Tepass, U.4    Beitel, G.J.5
  • 174
    • 34248561159 scopus 로고    scopus 로고
    • Drosophila Varicose, a member of a new subgroup of basolateral MAGUKs, is required for septate junctions and tracheal morphogenesis
    • Wu, V. M. et al. Drosophila Varicose, a member of a new subgroup of basolateral MAGUKs, is required for septate junctions and tracheal morphogenesis. Development 134, 999-1009 (2007).
    • (2007) Development , vol.134 , pp. 999-1009
    • Wu, V.M.1
  • 175
    • 0141920729 scopus 로고    scopus 로고
    • The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila
    • Behr, M., Riedel, D. & Schuh, R. The claudin-like megatrachea is essential in septate junctions for the epithelial barrier function in Drosophila. Dev. Cell 5, 611-620 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 611-620
    • Behr, M.1    Riedel, D.2    Schuh, R.3
  • 176
    • 0038457822 scopus 로고    scopus 로고
    • + ATPase are essential for septate junction function in Drosophila
    • + ATPase are essential for septate junction function in Drosophila. J. Cell Biol. 161, 979-989 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 979-989
    • Genova, J.L.1    Fehon, R.G.2
  • 177
    • 77956134851 scopus 로고    scopus 로고
    • The Drosophila claudin Kune-kune is required for septate junction organization and tracheal tube size control
    • Nelson, K. S., Furuse, M. & Beitel, G. J. The Drosophila claudin Kune-kune is required for septate junction organization and tracheal tube size control. Genetics 185, 831-839 (2010).
    • (2010) Genetics , vol.185 , pp. 831-839
    • Nelson, K.S.1    Furuse, M.2    Beitel, G.J.3
  • 178
    • 0038679606 scopus 로고    scopus 로고
    • Claudins in Caenorhabditis elegans: Their distribution and barrier function in the epithelium
    • Asano, A., Asano, K., Sasaki, H., Furuse, M. & Tsukita, S. Claudins in Caenorhabditis elegans: their distribution and barrier function in the epithelium. Curr. Biol. 13, 1042-1046 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1042-1046
    • Asano, A.1    Asano, K.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 179
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: Lessons in polarity
    • Suzuki, A. & Ohno, S. 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
  • 180
    • 0037336565 scopus 로고    scopus 로고
    • Signalling to and from tight junctions
    • Matter, K. & Balda, M. S. Signalling to and from tight junctions. Nat. Rev. Mol. Cell. Biol. 4, 225-236 (2003).
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 225-236
    • Matter, K.1    Balda, M.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.