메뉴 건너뛰기




Volumn 286, Issue C, 2011, Pages 223-269

The biology of the desmosome-like junction. A versatile anchoring junction and signal transducer in the seminiferous epithelium

Author keywords

Blood testis barrier; Desmosome like junction; Ectoplasmic specialization; Gap junction; Testis; Tight junction

Indexed keywords

ADAM PROTEIN; ARMADILLO PROTEIN; CADHERIN; CALCIUM ION; CELL MEMBRANE PROTEIN; MATRIX METALLOPROTEINASE; PHOSPHOTRANSFERASE; PLAKIN; PROTEINASE; SCAFFOLD PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 78650740255     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385859-7.00005-7     Document Type: Chapter
Times cited : (46)

References (198)
  • 1
    • 53949119553 scopus 로고    scopus 로고
    • Plakoglobin is required for effective intermediate filament anchorage to desmosomes
    • Acehan D., Petzold C., Gumper I., Sabatini D., Muller E., Cowin P., et al. Plakoglobin is required for effective intermediate filament anchorage to desmosomes. J. Invest. Dermatol.2008, 128:2665-2675.
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 2665-2675
    • Acehan, D.1    Petzold, C.2    Gumper, I.3    Sabatini, D.4    Muller, E.5    Cowin, P.6
  • 2
    • 8344221944 scopus 로고    scopus 로고
    • Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases
    • Aho S. Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases. Exp. Dermatol. 2004, 13:700-707.
    • (2004) Exp. Dermatol. , vol.13 , pp. 700-707
    • Aho, S.1
  • 3
    • 3042832052 scopus 로고    scopus 로고
    • Periplakin gene targeting reveals a constituent of the cornified cell envelope dispensable for normal mouse development
    • Aho S., Li K., Ryoo Y., McGee C., Ishida-Yamamoto A., Uitto J., et al. Periplakin gene targeting reveals a constituent of the cornified cell envelope dispensable for normal mouse development. Mol. Cell. Biol. 2004, 24:6410-6418.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6410-6418
    • Aho, S.1    Li, K.2    Ryoo, Y.3    McGee, C.4    Ishida-Yamamoto, A.5    Uitto, J.6
  • 5
    • 4444279375 scopus 로고    scopus 로고
    • Cryo-electron microscopy of vitreous sections of native biological cells and tissues
    • Al-Amoudi A., Norlen L.P., Dubochet J. Cryo-electron microscopy of vitreous sections of native biological cells and tissues. J. Struct. Biol. 2004, 148:131-135.
    • (2004) J. Struct. Biol. , vol.148 , pp. 131-135
    • Al-Amoudi, A.1    Norlen, L.P.2    Dubochet, J.3
  • 6
    • 36849060240 scopus 로고    scopus 로고
    • The molecular architecture of cadherins in native epidermal desmosomes
    • Al-Amoudi A., Diez D.C., Betts M.J., Frangakis A.S. The molecular architecture of cadherins in native epidermal desmosomes. Nature 2007, 450:832.
    • (2007) Nature , vol.450 , pp. 832
    • Al-Amoudi, A.1    Diez, D.C.2    Betts, M.J.3    Frangakis, A.S.4
  • 7
    • 0028216915 scopus 로고
    • Extracellular domain of pemphigus vulgaris antigen (desmoglein 3) mediates weak homophilic adhesion
    • Amagai M., Karpati S., Klaus-Kovtun V., Udey M.C., Stanley J.R. Extracellular domain of pemphigus vulgaris antigen (desmoglein 3) mediates weak homophilic adhesion. J. Invest. Dermatol. 1994, 102:402-408.
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 402-408
    • Amagai, M.1    Karpati, S.2    Klaus-Kovtun, V.3    Udey, M.C.4    Stanley, J.R.5
  • 8
    • 0029865077 scopus 로고    scopus 로고
    • Pemphigus vulgaris antigen (desmoglein 3) is localized in the lower epidermis, the site of blister formation in patients
    • Amagai M., Koch P.J., Nishikawa T., Stanley J.R. Pemphigus vulgaris antigen (desmoglein 3) is localized in the lower epidermis, the site of blister formation in patients. J. Invest. Dermatol. 1996, 106:351-355.
    • (1996) J. Invest. Dermatol. , vol.106 , pp. 351-355
    • Amagai, M.1    Koch, P.J.2    Nishikawa, T.3    Stanley, J.R.4
  • 9
    • 0025165922 scopus 로고
    • Desmoplakin II expression is not restricted to stratified epithelia
    • Angst B.D., Nilles L.A., Green K.J. Desmoplakin II expression is not restricted to stratified epithelia. J. Cell Sci. 1990, 97:247-257.
    • (1990) J. Cell Sci. , vol.97 , pp. 247-257
    • Angst, B.D.1    Nilles, L.A.2    Green, K.J.3
  • 10
    • 63149170510 scopus 로고    scopus 로고
    • 2+ -switch causes phosphorylation and association of desmocollin 3 with plakoglobin and desmoglein 3 in cultured keratinocytes
    • 2+ -switch causes phosphorylation and association of desmocollin 3 with plakoglobin and desmoglein 3 in cultured keratinocytes. Exp. Dermatol. 2009, 18:404-408.
    • (2009) Exp. Dermatol. , vol.18 , pp. 404-408
    • Aoyama, Y.1    Yamamoto, Y.2    Yamamguchi, F.3    Kitajima, Y.4
  • 11
    • 44149127750 scopus 로고    scopus 로고
    • Plakophilin 2: a critical scaffold for PKCα that regulates intercellular junction assembly
    • Bass-Zubek A.E., Hobbs R.P., Amargo E.V., Garcia N.J., Hsieh S.N., Chen X., et al. Plakophilin 2: a critical scaffold for PKCα that regulates intercellular junction assembly. J. Cell Biol. 2008, 181:605-613.
    • (2008) J. Cell Biol. , vol.181 , pp. 605-613
    • Bass-Zubek, A.E.1    Hobbs, R.P.2    Amargo, E.V.3    Garcia, N.J.4    Hsieh, S.N.5    Chen, X.6
  • 13
    • 33745477470 scopus 로고    scopus 로고
    • Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis
    • Bech-Serra J.J., Santiago-Josefat B., Esselens C., Saftig P., Baselga J., Arribas J., et al. Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis. Mol. Cell. Biol. 2006, 26:5086-5095.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5086-5095
    • Bech-Serra, J.J.1    Santiago-Josefat, B.2    Esselens, C.3    Saftig, P.4    Baselga, J.5    Arribas, J.6
  • 17
    • 0019419693 scopus 로고
    • Inhibition of rat Sertoli cell aromatase by factor(s) secreted specifically at spermatogenic stages VII and VIII
    • Boitani C., Ritzen E.M., Parvinen M. Inhibition of rat Sertoli cell aromatase by factor(s) secreted specifically at spermatogenic stages VII and VIII. Mol. Cell. Endocrinol. 1981, 23:11-22.
    • (1981) Mol. Cell. Endocrinol. , vol.23 , pp. 11-22
    • Boitani, C.1    Ritzen, E.M.2    Parvinen, M.3
  • 18
    • 0032779596 scopus 로고    scopus 로고
    • Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells
    • Bonne S., van Hengel J., Nollet F., Kools P., van Roy F. Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells. J. Cell Biol. 1999, 112:2265-2276.
    • (1999) J. Cell Biol. , vol.112 , pp. 2265-2276
    • Bonne, S.1    van Hengel, J.2    Nollet, F.3    Kools, P.4    van Roy, F.5
  • 20
    • 0035076526 scopus 로고    scopus 로고
    • Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders
    • Bornslaeger E.A., Godsel L.M., Corcoran C.M., Park J.K., Hatzfeld M., Kowalczyk A.P., et al. Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders. J. Cell Sci. 2000, 114:727-738.
    • (2000) J. Cell Sci. , vol.114 , pp. 727-738
    • Bornslaeger, E.A.1    Godsel, L.M.2    Corcoran, C.M.3    Park, J.K.4    Hatzfeld, M.5    Kowalczyk, A.P.6
  • 21
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga V.M., Machesky L.M., Hall A., Hotchin N.A. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 1997, 137:1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 22
    • 21644455018 scopus 로고    scopus 로고
    • Differential structural properties and expression patterns suggest functional significance for multiple mouse desmoglein 1 isoforms
    • Brennan D., Hu Y., Kljuic A., Choi Y.S., Joubeh S., Bashkin M., et al. Differential structural properties and expression patterns suggest functional significance for multiple mouse desmoglein 1 isoforms. Differentiation 2004, 72:434-449.
    • (2004) Differentiation , vol.72 , pp. 434-449
    • Brennan, D.1    Hu, Y.2    Kljuic, A.3    Choi, Y.S.4    Joubeh, S.5    Bashkin, M.6
  • 23
    • 17144371855 scopus 로고    scopus 로고
    • The cornified envelope: a model of cell death in the skin
    • Candi E., Schmidt R., Melino G. The cornified envelope: a model of cell death in the skin. Nat. Rev. Mol. Cell Biol. 2005, 6:328-340.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 328-340
    • Candi, E.1    Schmidt, R.2    Melino, G.3
  • 24
    • 2442428082 scopus 로고    scopus 로고
    • Degradation of cornodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
    • Caubet C., Jonca N., Brattsand M., Guerrin M., Bernard D., Schmidt R., et al. Degradation of cornodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Invest. Dermatol. 2004, 122:1235-1244.
    • (2004) J. Invest. Dermatol. , vol.122 , pp. 1235-1244
    • Caubet, C.1    Jonca, N.2    Brattsand, M.3    Guerrin, M.4    Bernard, D.5    Schmidt, R.6
  • 25
    • 0037155877 scopus 로고    scopus 로고
    • Protein binding and functional characterization of plakophilin 2
    • Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J. Protein binding and functional characterization of plakophilin 2. J. Biol. Chem. 2002, 277:10512-10522.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10512-10522
    • Chen, X.1    Bonne, S.2    Hatzfeld, M.3    van Roy, F.4    Green, K.J.5
  • 26
    • 53349175477 scopus 로고    scopus 로고
    • Loss of desmocollin 3 in mice leads to epidermal blistering
    • Chen J., Den Z., Koch P.J. Loss of desmocollin 3 in mice leads to epidermal blistering. J. Cell Sci. 2008, 121:2844-2849.
    • (2008) J. Cell Sci. , vol.121 , pp. 2844-2849
    • Chen, J.1    Den, Z.2    Koch, P.J.3
  • 28
    • 0035956432 scopus 로고    scopus 로고
    • Mice lacking desmocollin 1 show epidermal fragility accompanied by barrier defects and abnormal differentiation
    • Chidgey M., Brakebusch C., Gustafsson E., Cruchley A., Hail C., Kirk S., et al. Mice lacking desmocollin 1 show epidermal fragility accompanied by barrier defects and abnormal differentiation. J. Cell Biol. 2001, 155:821-832.
    • (2001) J. Cell Biol. , vol.155 , pp. 821-832
    • Chidgey, M.1    Brakebusch, C.2    Gustafsson, E.3    Cruchley, A.4    Hail, C.5    Kirk, S.6
  • 29
    • 0030610137 scopus 로고    scopus 로고
    • 2+ -dependent heterophilic interaction between desmosomal cadherins, desmoglein and desmocollin, contributes to cell-cell adhesion
    • 2+ -dependent heterophilic interaction between desmosomal cadherins, desmoglein and desmocollin, contributes to cell-cell adhesion. J. Cell Biol. 1997, 138:193-201.
    • (1997) J. Cell Biol. , vol.138 , pp. 193-201
    • Chitaev, N.A.1    Troyanovsky, S.M.2
  • 30
    • 0025298326 scopus 로고
    • A cadherin-like protein in eggs and cleaving embryos of Xenopus laevis is expressed in oocytes in response to progesterone
    • Choi Y.S., Sehgal R., McCrea P., Gumbiner B. A cadherin-like protein in eggs and cleaving embryos of Xenopus laevis is expressed in oocytes in response to progesterone. J. Cell Biol. 1990, 110:1575-1582.
    • (1990) J. Cell Biol. , vol.110 , pp. 1575-1582
    • Choi, Y.S.1    Sehgal, R.2    McCrea, P.3    Gumbiner, B.4
  • 31
    • 70450280500 scopus 로고    scopus 로고
    • Interactions of plakoglobin and β-catenin with desmosomal cadherins: basis of selective exclusion of α- and β-catenin from desmosomes
    • Choi H., Gross J.C., Weis W.I. Interactions of plakoglobin and β-catenin with desmosomal cadherins: basis of selective exclusion of α- and β-catenin from desmosomes. J. Biol. Chem. 2009, 284:31776-31788.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31776-31788
    • Choi, H.1    Gross, J.C.2    Weis, W.I.3
  • 32
    • 0027972448 scopus 로고
    • N-cadherin expression in developing, adult and denervated chicken neuromuscular system: accumulations at both the neuromuscular junction and the node of Ranvier
    • Cifuentes-Diaz C., Nicolet M., Goudou D., Rieger F., Mege R.M. N-cadherin expression in developing, adult and denervated chicken neuromuscular system: accumulations at both the neuromuscular junction and the node of Ranvier. Development 1994, 120:1-11.
    • (1994) Development , vol.120 , pp. 1-11
    • Cifuentes-Diaz, C.1    Nicolet, M.2    Goudou, D.3    Rieger, F.4    Mege, R.M.5
  • 33
    • 70349878700 scopus 로고    scopus 로고
    • Desmosomal interactome in keratinocytes: a systems biology approach leading to an understanding of the pathogenesis of skin disease
    • Cirillo N., Prime S.S. Desmosomal interactome in keratinocytes: a systems biology approach leading to an understanding of the pathogenesis of skin disease. Cell. Mol. Life Sci. 2009, 66:3517-3533.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3517-3533
    • Cirillo, N.1    Prime, S.S.2
  • 34
    • 38649137691 scopus 로고    scopus 로고
    • The most widespread desmosomal cadherin, desmoglein 2, is a novel target of caspase 3-mediated apoptotic machinery
    • Cirillo N., Lanza M., De Rosa A., Cammarota M., La Gatta A., Gombos F., et al. The most widespread desmosomal cadherin, desmoglein 2, is a novel target of caspase 3-mediated apoptotic machinery. J. Cell. Biochem. 2008, 103:598-606.
    • (2008) J. Cell. Biochem. , vol.103 , pp. 598-606
    • Cirillo, N.1    Lanza, M.2    De Rosa, A.3    Cammarota, M.4    La Gatta, A.5    Gombos, F.6
  • 35
    • 77449142413 scopus 로고    scopus 로고
    • Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC
    • Cirillo N., Lanza A., Prime S.S. Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC. Exp. Cell Res. 2010, 316:580-592.
    • (2010) Exp. Cell Res. , vol.316 , pp. 580-592
    • Cirillo, N.1    Lanza, A.2    Prime, S.S.3
  • 36
    • 0015255225 scopus 로고
    • Kinetics of spermatogenesis in mammals: seminiferous epithelium cycle and spermatogonial renewal
    • Clermont Y. Kinetics of spermatogenesis in mammals: seminiferous epithelium cycle and spermatogonial renewal. Physiol. Rev. 1972, 52:198-235.
    • (1972) Physiol. Rev. , vol.52 , pp. 198-235
    • Clermont, Y.1
  • 37
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling in development and disease
    • Clevers H. Wnt/β-catenin signaling in development and disease. Cell 2006, 127:469-480.
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 39
    • 0022993985 scopus 로고
    • Plakoglobin: a protein common to different kinds of intercellular adhering junctions
    • Cowin P., Kapprell H.P., Franke W.W., Tamkun J., Hynes R.O. Plakoglobin: a protein common to different kinds of intercellular adhering junctions. Cell 1986, 46:1063-1073.
    • (1986) Cell , vol.46 , pp. 1063-1073
    • Cowin, P.1    Kapprell, H.P.2    Franke, W.W.3    Tamkun, J.4    Hynes, R.O.5
  • 41
    • 59849124834 scopus 로고    scopus 로고
    • Regulation of cadherin trafficking
    • Delva E., Kowalczyk A. Regulation of cadherin trafficking. Traffic 2009, 10:259-267.
    • (2009) Traffic , vol.10 , pp. 259-267
    • Delva, E.1    Kowalczyk, A.2
  • 43
    • 19944427605 scopus 로고    scopus 로고
    • Spink5-deficient mice mimic Netherton syndrome through degradation of desmoglein 1 by epidermal protease hyperactivity
    • Descargues P., Deraison C., Bonnart C., Kreft M., Kishibe M., Ishida-Yamamoto A., et al. Spink5-deficient mice mimic Netherton syndrome through degradation of desmoglein 1 by epidermal protease hyperactivity. Nat. Genet. 2005, 37:56-65.
    • (2005) Nat. Genet. , vol.37 , pp. 56-65
    • Descargues, P.1    Deraison, C.2    Bonnart, C.3    Kreft, M.4    Kishibe, M.5    Ishida-Yamamoto, A.6
  • 44
    • 33645647950 scopus 로고    scopus 로고
    • The differentiation-dependent desmosomal cadherin desmoglein 1 is a novel caspase-3 target that regulates apoptosis in keratinocytes
    • Dusek R.L., Getsios S., Chen F., Park J.K., Amargo E.V., Cryns V.L., et al. The differentiation-dependent desmosomal cadherin desmoglein 1 is a novel caspase-3 target that regulates apoptosis in keratinocytes. J. Biol. Chem. 2006, 281:3614-3624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3614-3624
    • Dusek, R.L.1    Getsios, S.2    Chen, F.3    Park, J.K.4    Amargo, E.V.5    Cryns, V.L.6
  • 46
    • 0028952556 scopus 로고
    • Pemphigus foliaceus and pemphigus vulgaris auto-antibodies react with the extracellular domain of desmoglein-1
    • Emery D.J., Diaz L.A., Fairley J.A., Lopez A., Taylor A.F., Giudice G.J. Pemphigus foliaceus and pemphigus vulgaris auto-antibodies react with the extracellular domain of desmoglein-1. J. Invest. Dermatol. 1995, 104:323-328.
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 323-328
    • Emery, D.J.1    Diaz, L.A.2    Fairley, J.A.3    Lopez, A.4    Taylor, A.F.5    Giudice, G.J.6
  • 48
    • 33744983767 scopus 로고    scopus 로고
    • Ectodermal dysplasia-skin fragility syndrome resulting from a new homozygous mutation, 888delC, in the desmosomal protein plakophilin 1
    • Ersoy-Evans S., Erkin G., Fassihi H., Chan I., Paller A.S., Surucu S., et al. Ectodermal dysplasia-skin fragility syndrome resulting from a new homozygous mutation, 888delC, in the desmosomal protein plakophilin 1. J. Am. Acad. Dermatol. 2006, 55:157-161.
    • (2006) J. Am. Acad. Dermatol. , vol.55 , pp. 157-161
    • Ersoy-Evans, S.1    Erkin, G.2    Fassihi, H.3    Chan, I.4    Paller, A.S.5    Surucu, S.6
  • 49
    • 1842857530 scopus 로고    scopus 로고
    • Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells
    • Eshkind L., Tian Q., Schmidt A., Franke W.W., Windoffer R., Leube R.E. Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells. Eur. J. Cell Biol. 2002, 81:592-598.
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 592-598
    • Eshkind, L.1    Tian, Q.2    Schmidt, A.3    Franke, W.W.4    Windoffer, R.5    Leube, R.E.6
  • 50
    • 0000888012 scopus 로고
    • Proteases and antiproteases in the seminiferous tubule
    • Cache River Press, Clearwater, L.D. Russell, M.D. Griswold (Eds.)
    • Fritz I.B., Tung P.S., Ailenberg M. Proteases and antiproteases in the seminiferous tubule. The Sertoli Cell 1993, 217-235. Cache River Press, Clearwater. L.D. Russell, M.D. Griswold (Eds.).
    • (1993) The Sertoli Cell , pp. 217-235
    • Fritz, I.B.1    Tung, P.S.2    Ailenberg, M.3
  • 51
    • 20644437528 scopus 로고    scopus 로고
    • Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage
    • Gallicano G.I., Kouklis P., Bauer C., Yin M., Vasioukhin V., Degenstein L., et al. Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage. J. Cell Biol. 1998, 143:2009-2022.
    • (1998) J. Cell Biol. , vol.143 , pp. 2009-2022
    • Gallicano, G.I.1    Kouklis, P.2    Bauer, C.3    Yin, M.4    Vasioukhin, V.5    Degenstein, L.6
  • 52
    • 33745848407 scopus 로고    scopus 로고
    • Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy
    • Garcia-Gras E., Lombardi R., Giocondo M.J., Willerson J.T., Schneider M.D., Khoury D.S., et al. Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy. J. Clin. Invest. 2006, 116:2012-2021.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2012-2021
    • Garcia-Gras, E.1    Lombardi, R.2    Giocondo, M.J.3    Willerson, J.T.4    Schneider, M.D.5    Khoury, D.S.6
  • 53
    • 39849097562 scopus 로고    scopus 로고
    • Desmosome structure, composition and function
    • Garrod D., Chidgey M. Desmosome structure, composition and function. Biochim. Biophys. Acta 2008, 1778:572-587.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 572-587
    • Garrod, D.1    Chidgey, M.2
  • 54
    • 42449098549 scopus 로고    scopus 로고
    • Hyper-adhesion: a new concept in cell-cell adhesion
    • Garrod D., Kimura T.E. Hyper-adhesion: a new concept in cell-cell adhesion. Biochem. Soc. Trans. 2008, 36:195-201.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 195-201
    • Garrod, D.1    Kimura, T.E.2
  • 55
    • 30544454786 scopus 로고    scopus 로고
    • Hyper-adhesion in desmosomes: its regulation in wound healing and possible relationship to cadherin crystal structure
    • Garrod D.R., Berika M.Y., Bardsley W.F., Holmes D., Tabernero L. Hyper-adhesion in desmosomes: its regulation in wound healing and possible relationship to cadherin crystal structure. J. Cell Sci. 2005, 118:5743-5754.
    • (2005) J. Cell Sci. , vol.118 , pp. 5743-5754
    • Garrod, D.R.1    Berika, M.Y.2    Bardsley, W.F.3    Holmes, D.4    Tabernero, L.5
  • 56
    • 11444264507 scopus 로고    scopus 로고
    • Mutations in the desmosomal protein plakophilin-2 are common in arrhythmogenic right ventricular cardiomyopathy
    • Gerull B., Heuser A., Wichter T., Paul M., Basson C.T., McDermott D.A., et al. Mutations in the desmosomal protein plakophilin-2 are common in arrhythmogenic right ventricular cardiomyopathy. Nat. Genet. 2004, 36:1162-1164.
    • (2004) Nat. Genet. , vol.36 , pp. 1162-1164
    • Gerull, B.1    Heuser, A.2    Wichter, T.3    Paul, M.4    Basson, C.T.5    McDermott, D.A.6
  • 57
  • 58
    • 67649586282 scopus 로고    scopus 로고
    • Desmoglein 1-dependent suppression of EGFR signaling promotes epidermal differentiation and morphogenesis
    • Getsios S., Simpson C.L., Kojima S., Harmon R., Sheu L.J., Dusek R.L., et al. Desmoglein 1-dependent suppression of EGFR signaling promotes epidermal differentiation and morphogenesis. J. Cell Biol. 2009, 185:1243-1258.
    • (2009) J. Cell Biol. , vol.185 , pp. 1243-1258
    • Getsios, S.1    Simpson, C.L.2    Kojima, S.3    Harmon, R.4    Sheu, L.J.5    Dusek, R.L.6
  • 59
    • 59349109991 scopus 로고    scopus 로고
    • Molecular reorganization of Cx43, ZO-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen
    • Gilleron J., Fiorini C., Carette D., Avondet C., Falk M.M., Segretain D., et al. Molecular reorganization of Cx43, ZO-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen. J. Cell Sci. 2008, 121:4069-4078.
    • (2008) J. Cell Sci. , vol.121 , pp. 4069-4078
    • Gilleron, J.1    Fiorini, C.2    Carette, D.3    Avondet, C.4    Falk, M.M.5    Segretain, D.6
  • 60
    • 0026090748 scopus 로고
    • Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos
    • Ginsberg D., DeSimone D., Geiger B. Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos. Development 1991, 111:315-325.
    • (1991) Development , vol.111 , pp. 315-325
    • Ginsberg, D.1    DeSimone, D.2    Geiger, B.3
  • 61
    • 29144493487 scopus 로고    scopus 로고
    • Desmoplakin assembly dynamics in four dimensions: multiple phases differentially regulated by intermediate filaments and actin
    • Godsel L.M., Hsieh S.N., Amargo E.V., Bass A.E., Pascoe-McGillicuddy L.P., Huen A.C., et al. Desmoplakin assembly dynamics in four dimensions: multiple phases differentially regulated by intermediate filaments and actin. J. Cell Biol. 2005, 171:1045-1059.
    • (2005) J. Cell Biol. , vol.171 , pp. 1045-1059
    • Godsel, L.M.1    Hsieh, S.N.2    Amargo, E.V.3    Bass, A.E.4    Pascoe-McGillicuddy, L.P.5    Huen, A.C.6
  • 62
    • 34347364710 scopus 로고    scopus 로고
    • A unique and specific interaction between αT-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs
    • Goossens S., Janssens B., Bonne S., De Rycke R., Braet F., van Hengel J., et al. A unique and specific interaction between αT-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs. J. Cell Sci. 2007, 120:2126-2136.
    • (2007) J. Cell Sci. , vol.120 , pp. 2126-2136
    • Goossens, S.1    Janssens, B.2    Bonne, S.3    De Rycke, R.4    Braet, F.5    van Hengel, J.6
  • 63
    • 0034568948 scopus 로고    scopus 로고
    • Are desmosomes more than tethers for intermediate filaments?
    • Green K.J., Gaudry C.A. Are desmosomes more than tethers for intermediate filaments?. Nat. Rev. Mol. Cell Biol. 2000, 1:208-216.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 208-216
    • Green, K.J.1    Gaudry, C.A.2
  • 64
    • 35348927451 scopus 로고    scopus 로고
    • Desmosomes: new perspectives on a classic
    • Green K.J., Simpson C.L. Desmosomes: new perspectives on a classic. J. Invest. Dermatol. 2007, 127:2499-2515.
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 2499-2515
    • Green, K.J.1    Simpson, C.L.2
  • 65
    • 5444235947 scopus 로고    scopus 로고
    • Requirement of plakophilin 2 for heart morphogenesis and cardiac junction formation
    • Grossmann K.S., Grund C., Huelsken J., Behrend M., Erdmann B., Franke W.W., et al. Requirement of plakophilin 2 for heart morphogenesis and cardiac junction formation. J. Cell Biol. 2004, 167:149-160.
    • (2004) J. Cell Biol. , vol.167 , pp. 149-160
    • Grossmann, K.S.1    Grund, C.2    Huelsken, J.3    Behrend, M.4    Erdmann, B.5    Franke, W.W.6
  • 66
    • 33845414010 scopus 로고    scopus 로고
    • Cadherins in development: cell adhesion, sorting, and tissue morphogenesis
    • Halbleib J.M., Nelson W.J. Cadherins in development: cell adhesion, sorting, and tissue morphogenesis. Genes Dev. 2006, 20:3199-3214.
    • (2006) Genes Dev. , vol.20 , pp. 3199-3214
    • Halbleib, J.M.1    Nelson, W.J.2
  • 67
    • 0036405405 scopus 로고    scopus 로고
    • ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin
    • Ham C., Levkau B., Raines E.W., Herren B. ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin. Exp. Cell Res. 2002, 279:239-247.
    • (2002) Exp. Cell Res. , vol.279 , pp. 239-247
    • Ham, C.1    Levkau, B.2    Raines, E.W.3    Herren, B.4
  • 68
    • 33845383688 scopus 로고    scopus 로고
    • Plakophilins: multifunctional proteins or just regulators of desmosomal adhesion?
    • Hatzfeld M. Plakophilins: multifunctional proteins or just regulators of desmosomal adhesion?. Biochim. Biophys. Acta 2007, 1773:69-77.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 69-77
    • Hatzfeld, M.1
  • 69
    • 0029859086 scopus 로고    scopus 로고
    • Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins
    • Hatzfeld M., Nachtsheim C. Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins. J. Cell Sci. 1996, 109:2767-2778.
    • (1996) J. Cell Sci. , vol.109 , pp. 2767-2778
    • Hatzfeld, M.1    Nachtsheim, C.2
  • 70
    • 0034599841 scopus 로고    scopus 로고
    • The function of plakophilin 1 in desmosome assembly and actin filament organization
    • Hatzfeld M., Haffner C., Schulze K., Vinzens U. The function of plakophilin 1 in desmosome assembly and actin filament organization. J. Cell Biol. 2000, 149:209-222.
    • (2000) J. Cell Biol. , vol.149 , pp. 209-222
    • Hatzfeld, M.1    Haffner, C.2    Schulze, K.3    Vinzens, U.4
  • 71
    • 0037385290 scopus 로고    scopus 로고
    • Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains
    • Hatzfeld M., Green K.J., Sauter H. Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. J. Cell Sci. 2003, 116:1219-1233.
    • (2003) J. Cell Sci. , vol.116 , pp. 1219-1233
    • Hatzfeld, M.1    Green, K.J.2    Sauter, H.3
  • 72
    • 0141865704 scopus 로고    scopus 로고
    • Untangling desmosomal knots with electron tomography
    • He W., Cowin P., Stokes D.L. Untangling desmosomal knots with electron tomography. Science 2003, 302:109-113.
    • (2003) Science , vol.302 , pp. 109-113
    • He, W.1    Cowin, P.2    Stokes, D.L.3
  • 74
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: primary determinants of cell architecture and plasticity
    • Herrmann H., Strelkov S.V., Burkhard P., Aebi U. Intermediate filaments: primary determinants of cell architecture and plasticity. J. Clin. Invest. 2009, 119:1772-1783.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1772-1783
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 75
    • 49649084477 scopus 로고    scopus 로고
    • Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction
    • Heupel W., Zillikens D., Drenckhahn D., Waschke J. Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction. J. Immunol. 2008, 181:1825.
    • (2008) J. Immunol. , vol.181 , pp. 1825
    • Heupel, W.1    Zillikens, D.2    Drenckhahn, D.3    Waschke, J.4
  • 77
    • 0033868312 scopus 로고    scopus 로고
    • Interaction of plakophilins with desmoplakin and intermediate filmament proteins: an in vitro analysis
    • Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnolzer M. Interaction of plakophilins with desmoplakin and intermediate filmament proteins: an in vitro analysis. J. Cell Sci. 2000, 113:2471-2483.
    • (2000) J. Cell Sci. , vol.113 , pp. 2471-2483
    • Hofmann, I.1    Mertens, C.2    Brettel, M.3    Nimmrich, V.4    Schnolzer, M.5
  • 78
    • 33644854767 scopus 로고    scopus 로고
    • Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules
    • Hofmann I., Casella M., Schnolzer M., Schlechter T., Spring H., Franke W.W. Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules. Mol. Biol. Cell 2006, 17:1388-1398.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1388-1398
    • Hofmann, I.1    Casella, M.2    Schnolzer, M.3    Schlechter, T.4    Spring, H.5    Franke, W.W.6
  • 79
    • 59449092851 scopus 로고    scopus 로고
    • Protein p0071, a major plaque protein of non-desmosomal adhering junctions, is a selective cell-type marker
    • Hofmann I., Kuhn C., Franke W.W. Protein p0071, a major plaque protein of non-desmosomal adhering junctions, is a selective cell-type marker. Cell Tissue Res. 2008, 334:381-399.
    • (2008) Cell Tissue Res. , vol.334 , pp. 381-399
    • Hofmann, I.1    Kuhn, C.2    Franke, W.W.3
  • 80
    • 62149101141 scopus 로고    scopus 로고
    • Protein p0071-an armadillo plaque protein that characterizes a specific subtype of adherens junctions
    • Hofmann I., Schlechter T., Kuhn C., Hergt M., Franke W.W. Protein p0071-an armadillo plaque protein that characterizes a specific subtype of adherens junctions. J. Cell Sci. 2009, 122:21-24.
    • (2009) J. Cell Sci. , vol.122 , pp. 21-24
    • Hofmann, I.1    Schlechter, T.2    Kuhn, C.3    Hergt, M.4    Franke, W.W.5
  • 82
    • 0037164862 scopus 로고    scopus 로고
    • Intermediate filament-membrane attachments function synergistically with actin-dependent contacts to regulate intercellular adhesive strength
    • Huen A.C., Park J.K., Godsel L.M., Chen X., Bannon L.J., Amargo E.V., et al. Intermediate filament-membrane attachments function synergistically with actin-dependent contacts to regulate intercellular adhesive strength. J. Cell Biol. 2002, 159:1005-1017.
    • (2002) J. Cell Biol. , vol.159 , pp. 1005-1017
    • Huen, A.C.1    Park, J.K.2    Godsel, L.M.3    Chen, X.4    Bannon, L.J.5    Amargo, E.V.6
  • 84
    • 33947282628 scopus 로고    scopus 로고
    • Requirement of ZO-1 for the formation of belt-like adherens junctions during epithelial cell polarization
    • Ikenouchi J., Umeda K., Tsukita S., Furuse M., Tsukita S. Requirement of ZO-1 for the formation of belt-like adherens junctions during epithelial cell polarization. J. Cell Biol. 2007, 176:779-786.
    • (2007) J. Cell Biol. , vol.176 , pp. 779-786
    • Ikenouchi, J.1    Umeda, K.2    Tsukita, S.3    Furuse, M.4    Tsukita, S.5
  • 85
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase: at the cross-roads of signal transduction
    • Ilic D., Damsky C., Yamamoto T. Focal adhesion kinase: at the cross-roads of signal transduction. J. Cell Sci. 1997, 110:401-407.
    • (1997) J. Cell Sci. , vol.110 , pp. 401-407
    • Ilic, D.1    Damsky, C.2    Yamamoto, T.3
  • 86
    • 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 α-catenin
    • Itoh M., Morita K., Tsukita S. Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and α-catenin. J. Biol. Chem. 1999, 274:5981-5986.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5981-5986
    • Itoh, M.1    Morita, K.2    Tsukita, S.3
  • 87
  • 88
    • 0037428288 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3
    • Kale G., Naren A.P., Sheth P., Rao R.K. Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3. Biochem. Biophys. Res. Commun. 2003, 302:324-329.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 324-329
    • Kale, G.1    Naren, A.P.2    Sheth, P.3    Rao, R.K.4
  • 89
    • 0023917828 scopus 로고
    • Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia
    • Kapprell H.P., Owaribe K., Franke W.W. Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia. J. Cell Biol. 1988, 106:1679-1691.
    • (1988) J. Cell Biol. , vol.106 , pp. 1679-1691
    • Kapprell, H.P.1    Owaribe, K.2    Franke, W.W.3
  • 90
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational and signaling functions in the cytoplasm
    • Kim S.J., Coulombe P.A. Intermediate filament scaffolds fulfill mechanical, organizational and signaling functions in the cytoplasm. Genes Dev. 2007, 21:1581-1597.
    • (2007) Genes Dev. , vol.21 , pp. 1581-1597
    • Kim, S.J.1    Coulombe, P.A.2
  • 91
    • 9844250201 scopus 로고    scopus 로고
    • CDNA cloning of the 210-kDa paraneoplastic pemphigus antigen reveals that envoplakin is a component of the antigen complex
    • Kim S., Kwon Y.D., Lee I.J., Lee I.J., Chang S.N., Lee T.G. cDNA cloning of the 210-kDa paraneoplastic pemphigus antigen reveals that envoplakin is a component of the antigen complex. J. Invest. Dermatol. 1997, 109:365-369.
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 365-369
    • Kim, S.1    Kwon, Y.D.2    Lee, I.J.3    Lee, I.J.4    Chang, S.N.5    Lee, T.G.6
  • 92
    • 33947191090 scopus 로고    scopus 로고
    • Calcium-independent desmosomes of keratinocytes are hyper-adhesive
    • Kimura T.E., Merritt A.J., Garrod D.R. Calcium-independent desmosomes of keratinocytes are hyper-adhesive. J. Invest. Dermatol. 2007, 127:775-781.
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 775-781
    • Kimura, T.E.1    Merritt, A.J.2    Garrod, D.R.3
  • 93
    • 0036208599 scopus 로고    scopus 로고
    • Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments
    • Kiuchi-Saishin Y., Gotoh S., Furuse M., Takasuga A., Tano Y., Tsukita S. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 2002, 13:875-886.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 875-886
    • Kiuchi-Saishin, Y.1    Gotoh, S.2    Furuse, M.3    Takasuga, A.4    Tano, Y.5    Tsukita, S.6
  • 94
    • 63049110385 scopus 로고    scopus 로고
    • EGFR and ADAMs cooperate to regulate shedding and endocytic trafficking of the desmosomal cadherin desmoglein 2
    • Klessner J.L., Desai B.V., Amargo E.V., Getsios S., Green K.J. EGFR and ADAMs cooperate to regulate shedding and endocytic trafficking of the desmosomal cadherin desmoglein 2. Mol. Biol. Cell 2009, 20:328-337.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 328-337
    • Klessner, J.L.1    Desai, B.V.2    Amargo, E.V.3    Getsios, S.4    Green, K.J.5
  • 95
    • 0037453717 scopus 로고    scopus 로고
    • Desmoglein 4 in hair follicle differentiation and epidermal adhesion: evidence from inherited hypotrichosis and acquired pemphigus vulgaris
    • Kljuic A., Bazzi H., Sundberg J.P., Martinez-Mir A., O'Shaughnessy R., Mahoney M.G., et al. Desmoglein 4 in hair follicle differentiation and epidermal adhesion: evidence from inherited hypotrichosis and acquired pemphigus vulgaris. Cell 2003, 113:249-260.
    • (2003) Cell , vol.113 , pp. 249-260
    • Kljuic, A.1    Bazzi, H.2    Sundberg, J.P.3    Martinez-Mir, A.4    O'Shaughnessy, R.5    Mahoney, M.G.6
  • 96
    • 0030902370 scopus 로고    scopus 로고
    • Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris
    • Koch P.J., Mahoney M.G., Ishikawa H., Pulkkinen L., Uitto J., Shultz L., et al. Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris. J. Cell Biol. 1997, 137:1091-1102.
    • (1997) J. Cell Biol. , vol.137 , pp. 1091-1102
    • Koch, P.J.1    Mahoney, M.G.2    Ishikawa, H.3    Pulkkinen, L.4    Uitto, J.5    Shultz, L.6
  • 97
    • 4143112597 scopus 로고    scopus 로고
    • Protein kinase C α/β inhibitor Go6976 promotes formation of cell junctions and inhibits invasion of urinary bladder carcinoma cells
    • Koivunen J., Aaltonen V., Koskela S., Lehenkari P., Laato M., Peltonen J. Protein kinase C α/β inhibitor Go6976 promotes formation of cell junctions and inhibits invasion of urinary bladder carcinoma cells. Cancer Res. 2004, 64:5693-5701.
    • (2004) Cancer Res. , vol.64 , pp. 5693-5701
    • Koivunen, J.1    Aaltonen, V.2    Koskela, S.3    Lehenkari, P.4    Laato, M.5    Peltonen, J.6
  • 98
    • 0029816439 scopus 로고    scopus 로고
    • Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes
    • Kowalczyk A.P., Borgwardt J.E., Green K.J. Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes. J. Invest. Dermatol. 1996, 107:293-300.
    • (1996) J. Invest. Dermatol. , vol.107 , pp. 293-300
    • Kowalczyk, A.P.1    Borgwardt, J.E.2    Green, K.J.3
  • 100
    • 0001331879 scopus 로고    scopus 로고
    • Recycling of E-cadherin: a potential mechanism for regulating cadherin dynamics
    • Le T.L., Yap A.S., Stow J.L. Recycling of E-cadherin: a potential mechanism for regulating cadherin dynamics. J. Cell Biol. 1999, 146:219-232.
    • (1999) J. Cell Biol. , vol.146 , pp. 219-232
    • Le, T.L.1    Yap, A.S.2    Stow, J.L.3
  • 101
    • 33748195976 scopus 로고    scopus 로고
    • Mechanism and dynamics of cadherin adhesion
    • Leckband D., Prakasam A. Mechanism and dynamics of cadherin adhesion. Annu. Rev. Biomed. Eng. 2006, 8:259-287.
    • (2006) Annu. Rev. Biomed. Eng. , vol.8 , pp. 259-287
    • Leckband, D.1    Prakasam, A.2
  • 102
    • 0037306844 scopus 로고    scopus 로고
    • Is the cadherin/catenin complex a functional unit of cell-cell-actin-based adherens junctions (AJ) in the rat testis?
    • Lee N.P.Y., Mruk D.D., Lee W.M., Cheng C.Y. Is the cadherin/catenin complex a functional unit of cell-cell-actin-based adherens junctions (AJ) in the rat testis?. Biol. Reprod. 2003, 68:489-508.
    • (2003) Biol. Reprod. , vol.68 , pp. 489-508
    • Lee, N.P.Y.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 103
    • 0028284410 scopus 로고
    • The bovine desmocollin family: a new gene and expression patterns reflecting epithelial cell proliferation and differentiation
    • Legan P.K., Yue K.K.M., Chidgey M.A.J., Holton J.L., Wilkinson R.W., Garrod D.R. The bovine desmocollin family: a new gene and expression patterns reflecting epithelial cell proliferation and differentiation. J. Cell Biol. 1994, 126:507-518.
    • (1994) J. Cell Biol. , vol.126 , pp. 507-518
    • Legan, P.K.1    Yue, K.K.M.2    Chidgey, M.A.J.3    Holton, J.L.4    Wilkinson, R.W.5    Garrod, D.R.6
  • 104
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: a family of versatile cytolinker proteins
    • Leung C.L., Green K.J., Liem R.K.H. Plakins: a family of versatile cytolinker proteins. Trends Cell Biol. 2002, 12:37-45.
    • (2002) Trends Cell Biol. , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.H.3
  • 105
    • 0028293208 scopus 로고
    • Selective disruption of E-cadherin function in early Xenopus embryos by a dominant negative mutant
    • Levine E., Lee C.H., Kinter C., Gumbiner B.M. Selective disruption of E-cadherin function in early Xenopus embryos by a dominant negative mutant. Development 1994, 120:901-909.
    • (1994) Development , vol.120 , pp. 901-909
    • Levine, E.1    Lee, C.H.2    Kinter, C.3    Gumbiner, B.M.4
  • 107
    • 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. 2000, 148:791-800.
    • (2000) J. Cell Biol. , vol.148 , pp. 791-800
    • Li, D.1    Mrsny, R.J.2
  • 108
    • 67649834031 scopus 로고    scopus 로고
    • Connexin 43 and plakophilin-2 as a protein complex that regulates blood-testis barrier dynamics
    • Li M.W.M., Mruk D.D., Lee W.M., Cheng C.Y. Connexin 43 and plakophilin-2 as a protein complex that regulates blood-testis barrier dynamics. Proc. Natl. Acad. Sci. USA 2009, 106:10213-10218.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10213-10218
    • Li, M.W.M.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 109
    • 67649983117 scopus 로고    scopus 로고
    • Coordinating cellular events during spermatogenesis: a biochemical model
    • Lie P.P.Y., Cheng C.Y., Mruk D.D. Coordinating cellular events during spermatogenesis: a biochemical model. Trends Biochem. Sci. 2009, 34:366-373.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 366-373
    • Lie, P.P.Y.1    Cheng, C.Y.2    Mruk, D.D.3
  • 110
    • 77953764845 scopus 로고    scopus 로고
    • Crosstalk between desmoglein-2/desmocollin-2/Src kinase and coxsackie and adenovirus receptor/ZO-1 protein complexes, regulates blood-testis barrier dynamics
    • Lie P.P.Y., Cheng C.Y., Mruk D.D. Crosstalk between desmoglein-2/desmocollin-2/Src kinase and coxsackie and adenovirus receptor/ZO-1 protein complexes, regulates blood-testis barrier dynamics. Int. J. Biochem. Cell Biol. 2010, 42:975-986.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 975-986
    • Lie, P.P.Y.1    Cheng, C.Y.2    Mruk, D.D.3
  • 112
    • 4344680669 scopus 로고    scopus 로고
    • Epidermal growth factor receptor inhibition promotes desmosome assembly and strengthens intercellular adhesion in squamous cell carcinoma cells
    • Lorch J.H., Klessner J., Park J.K., Getsios S., Wu Y.L., Stack M.S., et al. Epidermal growth factor receptor inhibition promotes desmosome assembly and strengthens intercellular adhesion in squamous cell carcinoma cells. J. Biol. Chem. 2004, 279:37191-37200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37191-37200
    • Lorch, J.H.1    Klessner, J.2    Park, J.K.3    Getsios, S.4    Wu, Y.L.5    Stack, M.S.6
  • 113
    • 0028525019 scopus 로고
    • Cloning, sequence analysis and expression pattern of mouse desmocollin 2 (DSC2), a cadherin-like adhesion molecule
    • Lorimer J.E., Hall L.S., Clarke J.P., Collins J.E., Fleming T.P., Garrod D.R. Cloning, sequence analysis and expression pattern of mouse desmocollin 2 (DSC2), a cadherin-like adhesion molecule. Mol. Membr. Biol. 1994, 11:229-236.
    • (1994) Mol. Membr. Biol. , vol.11 , pp. 229-236
    • Lorimer, J.E.1    Hall, L.S.2    Clarke, J.P.3    Collins, J.E.4    Fleming, T.P.5    Garrod, D.R.6
  • 114
    • 0034808105 scopus 로고    scopus 로고
    • Gene targeting of envoplakin, a cytoskeletal linker protein and precursor of the epidermal cornified envelope
    • Maatta A., DiColandrea T., Groot K., Watt F.M. Gene targeting of envoplakin, a cytoskeletal linker protein and precursor of the epidermal cornified envelope. Mol. Cell. Biol. 2001, 21:7047-7053.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7047-7053
    • Maatta, A.1    DiColandrea, T.2    Groot, K.3    Watt, F.M.4
  • 115
    • 0031014550 scopus 로고    scopus 로고
    • Estrogens potentiate the stimulatory effects of follicle-stimulating hormone on N-cadherin messenger ribonucleic acid levels in cultured mouse Sertoli cells
    • MacCalman C.D., Getsios S., Farookhi R., Blaschuk O.W. Estrogens potentiate the stimulatory effects of follicle-stimulating hormone on N-cadherin messenger ribonucleic acid levels in cultured mouse Sertoli cells. Endocrinology 1997, 138:41-48.
    • (1997) Endocrinology , vol.138 , pp. 41-48
    • MacCalman, C.D.1    Getsios, S.2    Farookhi, R.3    Blaschuk, O.W.4
  • 116
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., et al. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 2002, 21:1948-1956.
    • (2002) EMBO J. , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5    Nagy, V.6
  • 117
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/E{open}-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P., Wen P.H., Dutt A., Shioi J., Takashima A., Siman R., et al. A CBP binding transcriptional repressor produced by the PS1/E{open}-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 2003, 114:635-645.
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6
  • 118
    • 21544467772 scopus 로고    scopus 로고
    • ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and β-catenin translocation
    • Maretzky T., Reiss K., Ludwig A., Buchholz J., Scholz F., Proksch E., et al. ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and β-catenin translocation. Proc. Natl. Acad. Sci. USA 2005, 102:9182-9187.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9182-9187
    • Maretzky, T.1    Reiss, K.2    Ludwig, A.3    Buchholz, J.4    Scholz, F.5    Proksch, E.6
  • 119
    • 24644496823 scopus 로고    scopus 로고
    • Mammalian tight junctions in the regulation of epithelial differentiation and proliferation
    • Matter K., Aijaz S., Tsapara A., Balda M.S. Mammalian tight junctions in the regulation of epithelial differentiation and proliferation. Curr. Opin. Cell Biol. 2005, 17:453-458.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 453-458
    • Matter, K.1    Aijaz, S.2    Tsapara, A.3    Balda, M.S.4
  • 120
    • 67650600991 scopus 로고    scopus 로고
    • Life after proteolysis: exploring the signaling capabilities of classical cadherin cleavage fragments
    • McCusker C.D., Alfandari D. Life after proteolysis: exploring the signaling capabilities of classical cadherin cleavage fragments. Commun. Integr. Biol. 2009, 2:155-157.
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 155-157
    • McCusker, C.D.1    Alfandari, D.2
  • 121
    • 63049120203 scopus 로고    scopus 로고
    • Extracellular cleavage of cadherin-11 by ADAM metalloproteases is essential for Xenopus cranial neural crest cell migration
    • McCusker C.D., Cousin H., Neuner R., Alfandari D. Extracellular cleavage of cadherin-11 by ADAM metalloproteases is essential for Xenopus cranial neural crest cell migration. Mol. Biol. Cell 2008, 20:78-89.
    • (2008) Mol. Biol. Cell , vol.20 , pp. 78-89
    • McCusker, C.D.1    Cousin, H.2    Neuner, R.3    Alfandari, D.4
  • 122
    • 0018611109 scopus 로고
    • Gap junctions between Sertoli and germ cells of rat seminiferous tubules
    • McGinley D.M., Posalaky Z., Provaznik M., Russell L.D. Gap junctions between Sertoli and germ cells of rat seminiferous tubules. Tissue Cell 1979, 11:741-754.
    • (1979) Tissue Cell , vol.11 , pp. 741-754
    • McGinley, D.M.1    Posalaky, Z.2    Provaznik, M.3    Russell, L.D.4
  • 123
    • 84984774604 scopus 로고    scopus 로고
    • Mutations in the plakophilin 1 gene result in ectodermal dysplasia/skin fragility syndrome
    • McGrath J.A., McMillan J.R., Shemanko C.S., Runswick S.K., Leigh I.M., Lane E.B., et al. Mutations in the plakophilin 1 gene result in ectodermal dysplasia/skin fragility syndrome. Nat. Genet. 1997, 17:240-244.
    • (1997) Nat. Genet. , vol.17 , pp. 240-244
    • McGrath, J.A.1    McMillan, J.R.2    Shemanko, C.S.3    Runswick, S.K.4    Leigh, I.M.5    Lane, E.B.6
  • 124
    • 0034679297 scopus 로고    scopus 로고
    • Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease)
    • McKoy G., Protonotarios N., Crosby A., Tsatsopoulou A., Anastasakis A., Coonar A., et al. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet 2000, 355:2119-2421.
    • (2000) Lancet , vol.355 , pp. 2119-2421
    • McKoy, G.1    Protonotarios, N.2    Crosby, A.3    Tsatsopoulou, A.4    Anastasakis, A.5    Coonar, A.6
  • 126
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • Mertens C., Kuhn C., Franke W.W. Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J. Cell Biol. 1996, 135:1009-1025.
    • (1996) J. Cell Biol. , vol.135 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 127
    • 0034932143 scopus 로고    scopus 로고
    • Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2
    • Mertens C., Hofmann I., Wang Z., Teichmann M., Chong S.S., Schnolzer M., et al. Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2. Proc. Natl. Acad. Sci. USA 2001, 98:7795-7800.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7795-7800
    • Mertens, C.1    Hofmann, I.2    Wang, Z.3    Teichmann, M.4    Chong, S.S.5    Schnolzer, M.6
  • 128
    • 0141529737 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates β-catenin-mediated transcription
    • Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M., et al. Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates β-catenin-mediated transcription. Mol. Cell. Biol. 2003, 23:7391-7402.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7391-7402
    • Miravet, S.1    Piedra, J.2    Castano, J.3    Raurell, I.4    Franci, C.5    Dunach, M.6
  • 129
    • 0035958937 scopus 로고    scopus 로고
    • Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases
    • Miyamori H., Takino T., Kobayashi Y., Tokai H., Itoh Y., Seiki M., et al. Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases. J. Biol. Chem. 2001, 276:28204-28211.
    • (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
  • 130
    • 0033523758 scopus 로고    scopus 로고
    • Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells
    • Morita K., Sasaki H., Furuse M., Tsukita S. Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells. J. Cell Biol. 1999, 147:185-194.
    • (1999) J. Cell Biol. , vol.147 , pp. 185-194
    • Morita, K.1    Sasaki, H.2    Furuse, M.3    Tsukita, S.4
  • 132
    • 73349139531 scopus 로고    scopus 로고
    • Claudin 5 expression in mouse seminiferous epithelium is dependent upon the transcription factor Ets-variant 5 and contributes to blood-testis barrier function
    • Morrow C.M.K., Tyagi G., Simon L., Carnes K., Murphy K.M., Cooke P.S., et al. Claudin 5 expression in mouse seminiferous epithelium is dependent upon the transcription factor Ets-variant 5 and contributes to blood-testis barrier function. Biol. Reprod. 2009, 81:871-879.
    • (2009) Biol. Reprod. , vol.81 , pp. 871-879
    • Morrow, C.M.K.1    Tyagi, G.2    Simon, L.3    Carnes, K.4    Murphy, K.M.5    Cooke, P.S.6
  • 133
    • 54549102284 scopus 로고    scopus 로고
    • Derailed endocytosis: an emerging feature of cancer
    • Mosesson Y., Mills G.B., Yarden Y. Derailed endocytosis: an emerging feature of cancer. Nat. Rev. Cancer 2008, 8:835-850.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 835-850
    • Mosesson, Y.1    Mills, G.B.2    Yarden, Y.3
  • 134
    • 7444240899 scopus 로고    scopus 로고
    • Cell-cell interactions at the ectoplasmic specialization in the testis
    • Mruk D.D., Cheng C.Y. Cell-cell interactions at the ectoplasmic specialization in the testis. Trends Endocrinol. Metab. 2004, 15:439-447.
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 439-447
    • Mruk, D.D.1    Cheng, C.Y.2
  • 135
    • 3242879161 scopus 로고    scopus 로고
    • Sertoli-Sertoli and Sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis
    • Mruk D.D., Cheng C.Y. Sertoli-Sertoli and Sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis. Endocr. Rev. 2004, 25:747-806.
    • (2004) Endocr. Rev. , vol.25 , pp. 747-806
    • Mruk, D.D.1    Cheng, C.Y.2
  • 136
    • 46949109724 scopus 로고    scopus 로고
    • Anchoring junctions as drug targets: role in contraceptive development
    • Mruk D.D., Silvestrini B., Cheng C.Y. Anchoring junctions as drug targets: role in contraceptive development. Pharmacol. Rev. 2008, 60:146-180.
    • (2008) Pharmacol. Rev. , vol.60 , pp. 146-180
    • Mruk, D.D.1    Silvestrini, B.2    Cheng, C.Y.3
  • 137
    • 0027618471 scopus 로고
    • Transmembrane control of cadherin-mediated cell-cell adhesion
    • Nagafuchi A., Tsukita S., Takeichi M. Transmembrane control of cadherin-mediated cell-cell adhesion. Semin. Cell Biol. 1993, 4:175-181.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 175-181
    • Nagafuchi, A.1    Tsukita, S.2    Takeichi, M.3
  • 138
    • 49649103585 scopus 로고    scopus 로고
    • The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation
    • Najy A.J., Day K.C., Day M.L. The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation. J. Biol. Chem. 2008, 283:18393-18401.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18393-18401
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 141
    • 0034326902 scopus 로고    scopus 로고
    • Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma
    • Norgett E.E., Hatsell S.J., Carvajal-Huerta L., Cabezas J.R., Common J., Purkis P.E., et al. Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma. Hum. Mol. Genet. 2000, 9:2761-2766.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2761-2766
    • Norgett, E.E.1    Hatsell, S.J.2    Carvajal-Huerta, L.3    Cabezas, J.R.4    Common, J.5    Purkis, P.E.6
  • 142
    • 0028800579 scopus 로고
    • The widespread human desmocollin Dsc2 and tissue-specific patterns of synthesis of various desmocollin subtypes
    • Nuber U.A., Schafer S., Schmidt A., Koch P.J., Franke W.W. The widespread human desmocollin Dsc2 and tissue-specific patterns of synthesis of various desmocollin subtypes. Eur. J. Cell Biol. 1995, 66:69-74.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 69-74
    • Nuber, U.A.1    Schafer, S.2    Schmidt, A.3    Koch, P.J.4    Franke, W.W.5
  • 143
    • 33744903401 scopus 로고    scopus 로고
    • Tight junction protein claudin-1 enhances the invasive activity of oral squamous cell carcinoma cells by promoting cleavage of laminin-5 γ2 chain via matrix metalloproteinase (MMP)-2 and membrane-type MMP-1
    • Oku N., Sasabe E., Ueta E., Yamamoto T., Osaki T. Tight junction protein claudin-1 enhances the invasive activity of oral squamous cell carcinoma cells by promoting cleavage of laminin-5 γ2 chain via matrix metalloproteinase (MMP)-2 and membrane-type MMP-1. Cancer Res. 2006, 66:5251-5257.
    • (2006) Cancer Res. , vol.66 , pp. 5251-5257
    • Oku, N.1    Sasabe, E.2    Ueta, E.3    Yamamoto, T.4    Osaki, T.5
  • 146
    • 34848820956 scopus 로고    scopus 로고
    • Connexin-43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells
    • Oxford E.M., Musa H., Maass K., Coombs W., Taffet S.M., Delmar M. Connexin-43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells. Circ. Res. 2007, 101:703-711.
    • (2007) Circ. Res. , vol.101 , pp. 703-711
    • Oxford, E.M.1    Musa, H.2    Maass, K.3    Coombs, W.4    Taffet, S.M.5    Delmar, M.6
  • 147
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A., Ewald A.J., Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 2007, 8:221-233.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 148
    • 0027328498 scopus 로고
    • Purification and characterization of NCAD90, a soluble endogenous form of N-cadherin, which is generated by proteolysis during retinal development and retains adhesive and neurite-promoting function
    • Paradies N.E., Grunwald G.B. Purification and characterization of NCAD90, a soluble endogenous form of N-cadherin, which is generated by proteolysis during retinal development and retains adhesive and neurite-promoting function. J. Neurosci. Res. 1993, 36:33-45.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 33-45
    • Paradies, N.E.1    Grunwald, G.B.2
  • 149
    • 0020181783 scopus 로고
    • Regulation of the seminiferous epithelium
    • Parvinen M. Regulation of the seminiferous epithelium. Endocr. Rev. 1982, 3:404-417.
    • (1982) Endocr. Rev. , vol.3 , pp. 404-417
    • Parvinen, M.1
  • 150
    • 44449156929 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNA-mediated knockdown in cultured rat cardiomyocytes
    • Pieperhoff S., Schumacher H., Franke W.W. The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNA-mediated knockdown in cultured rat cardiomyocytes. Eur. J. Cell Biol. 2008, 87:399-411.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 399-411
    • Pieperhoff, S.1    Schumacher, H.2    Franke, W.W.3
  • 151
    • 33645527574 scopus 로고    scopus 로고
    • Mutations in desmoglein-2 gene are associated with arrhythmogenic right ventricular cardiomyopathy
    • Pilichou K., Nava A., Basso C., Beffagna G., Bauce B., Lorenzon A., et al. Mutations in desmoglein-2 gene are associated with arrhythmogenic right ventricular cardiomyopathy. Circulation 2006, 113:1171-1179.
    • (2006) Circulation , vol.113 , pp. 1171-1179
    • Pilichou, K.1    Nava, A.2    Basso, C.3    Beffagna, G.4    Bauce, B.5    Lorenzon, A.6
  • 152
    • 0028093281 scopus 로고
    • Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding
    • Pokutta S., Herrenknecht K., Kemler R., Engel J. Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding. Eur. J. Biochem. 1994, 223:1019-1026.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1019-1026
    • Pokutta, S.1    Herrenknecht, K.2    Kemler, R.3    Engel, J.4
  • 153
    • 41949131198 scopus 로고    scopus 로고
    • Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins binding through the same adhesive interface?
    • Posy S., Shapiro L., Honig B. Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins binding through the same adhesive interface?. J. Mol. Biol. 2008, 378:954-968.
    • (2008) J. Mol. Biol. , vol.378 , pp. 954-968
    • Posy, S.1    Shapiro, L.2    Honig, B.3
  • 154
    • 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. 1996, 132:451-463.
    • (1996) J. Cell Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 155
    • 63649141727 scopus 로고    scopus 로고
    • The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: physiological and cellular functions
    • Reiss K., Saftig P. The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: physiological and cellular functions. Semin. Cell Dev. Biol. 2009, 20:126-137.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 156
    • 0032970153 scopus 로고    scopus 로고
    • N-terminal deletion in a desmosomal cadherin causes the autosomal dominant skin disease striate palmoplantar keratoderma
    • Rickman L., Simrak D., Stevens H.P., Hunt D.M., King I.A., Bryant S.P., et al. N-terminal deletion in a desmosomal cadherin causes the autosomal dominant skin disease striate palmoplantar keratoderma. Hum. Mol. Genet. 1999, 8:971-976.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 971-976
    • Rickman, L.1    Simrak, D.2    Stevens, H.P.3    Hunt, D.M.4    King, I.A.5    Bryant, S.P.6
  • 157
    • 0029741672 scopus 로고    scopus 로고
    • Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin
    • Ruhrberg C., Hajibagheri M.A.N., Simon M., Dooley T.P., Watt F.M. Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin. J. Cell Biol. 1996, 134:715-729.
    • (1996) J. Cell Biol. , vol.134 , pp. 715-729
    • Ruhrberg, C.1    Hajibagheri, M.A.N.2    Simon, M.3    Dooley, T.P.4    Watt, F.M.5
  • 158
    • 0031417774 scopus 로고    scopus 로고
    • Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin
    • Ruhrberg C., Hajibagheri M.A.N., Parry D.A.D., Watt F.M. Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin. J. Cell Biol. 1997, 139:1835-1849.
    • (1997) J. Cell Biol. , vol.139 , pp. 1835-1849
    • Ruhrberg, C.1    Hajibagheri, M.A.N.2    Parry, D.A.D.3    Watt, F.M.4
  • 159
    • 10144229330 scopus 로고    scopus 로고
    • Targeted mutation of plakoglobin in mice reveals essential functions of desmosomes in the embryonic heart
    • Ruiz P., Brinkmann V., Ledermann B., Behrend M., Grund C., Thalhammer C., et al. Targeted mutation of plakoglobin in mice reveals essential functions of desmosomes in the embryonic heart. J. Cell Biol. 1996, 135:215-225.
    • (1996) J. Cell Biol. , vol.135 , pp. 215-225
    • Ruiz, P.1    Brinkmann, V.2    Ledermann, B.3    Behrend, M.4    Grund, C.5    Thalhammer, C.6
  • 160
    • 0017362507 scopus 로고
    • Desmosome-like junctions between Sertoli and germ cells in the rat testis
    • Russell L.D. Desmosome-like junctions between Sertoli and germ cells in the rat testis. Am. J. Anat. 1977, 148:301-312.
    • (1977) Am. J. Anat. , vol.148 , pp. 301-312
    • Russell, L.D.1
  • 161
    • 0017709496 scopus 로고
    • Observations on rat Sertoli ectoplasmic ("junctional") specializations in their association with germ cells of the rat testis
    • Russell L.D. Observations on rat Sertoli ectoplasmic ("junctional") specializations in their association with germ cells of the rat testis. Tissue Cell 1977, 9:475-498.
    • (1977) Tissue Cell , vol.9 , pp. 475-498
    • Russell, L.D.1
  • 162
    • 0020644649 scopus 로고
    • Three-dimensional reconstruction of a rat stage V Sertoli cell: III. A study of specific cellular relationships
    • Russell L.D., Tallon-Doran M., Weber J.E., Wong V., Peterson R.N. Three-dimensional reconstruction of a rat stage V Sertoli cell: III. A study of specific cellular relationships. Am. J. Anat. 1983, 167:181-192.
    • (1983) Am. J. Anat. , vol.167 , pp. 181-192
    • Russell, L.D.1    Tallon-Doran, M.2    Weber, J.E.3    Wong, V.4    Peterson, R.N.5
  • 163
    • 0033635344 scopus 로고    scopus 로고
    • Complex phenotype of mice lacking occludin, a component of tight junction strands
    • Saitou M., Furuse M., Sasaki H., Schulzke J.D., Fromm M., Takano H., et al. Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol. Biol. Cell 2000, 11:4131-4142.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4131-4142
    • Saitou, M.1    Furuse, M.2    Sasaki, H.3    Schulzke, J.D.4    Fromm, M.5    Takano, H.6
  • 164
    • 34247236142 scopus 로고    scopus 로고
    • Post-transcriptional up-regulation of ADAM17 upon epidermal growth factor receptor activation and in breast tumors
    • Santiago-Josefat B., Esselens C., Bech-Serra J.J., Arribas J. Post-transcriptional up-regulation of ADAM17 upon epidermal growth factor receptor activation and in breast tumors. J. Biol. Chem. 2007, 282:8325-8331.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8325-8331
    • Santiago-Josefat, B.1    Esselens, C.2    Bech-Serra, J.J.3    Arribas, J.4
  • 165
    • 0028360311 scopus 로고
    • Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins
    • Schafer S., Koch P.J., Franke W.W. Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins. Exp. Cell Res. 1994, 211:391-399.
    • (1994) Exp. Cell Res. , vol.211 , pp. 391-399
    • Schafer, S.1    Koch, P.J.2    Franke, W.W.3
  • 166
    • 14844357389 scopus 로고    scopus 로고
    • Plakophilins-hard work in the desmosome, recreation in the nucleus?
    • Schmidt A., Jager S. Plakophilins-hard work in the desmosome, recreation in the nucleus?. Eur. J. Cell Biol. 2005, 84:189-204.
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 189-204
    • Schmidt, A.1    Jager, S.2
  • 170
    • 0035827559 scopus 로고    scopus 로고
    • Refined characterization of corneodesmosin proteolysis during terminal differentiation of human epidermis and its relationship to desquamation
    • Simon M., Jonca N., Guerrin M., Haftek M., Bernard D., Caubet C., et al. Refined characterization of corneodesmosin proteolysis during terminal differentiation of human epidermis and its relationship to desquamation. J. Biol. Chem. 2001, 276:20292-20299.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20292-20299
    • Simon, M.1    Jonca, N.2    Guerrin, M.3    Haftek, M.4    Bernard, D.5    Caubet, C.6
  • 171
    • 0037230154 scopus 로고    scopus 로고
    • The interplay of collagen IV, tumor necrosis factor α, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloprotease-1 in the basal lamina regulates Sertoli cell-tight junction dynamics in the rat testis
    • Siu M.K.Y., Lee W.M., Cheng C.Y. The interplay of collagen IV, tumor necrosis factor α, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloprotease-1 in the basal lamina regulates Sertoli cell-tight junction dynamics in the rat testis. Endocrinology 2003, 144:371-387.
    • (2003) Endocrinology , vol.144 , pp. 371-387
    • Siu, M.K.Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 173
    • 43749116674 scopus 로고    scopus 로고
    • Plakophilin-3-deficient mice develop hair coat abnormalities and are prone to cutaneous inflammation
    • Sklyarova T., Bonne S., D'hooge P., Denecker G., Goossens S., De Rycke R., et al. Plakophilin-3-deficient mice develop hair coat abnormalities and are prone to cutaneous inflammation. J. Invest. Dermatol. 2008, 128:1375-1385.
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 1375-1385
    • Sklyarova, T.1    Bonne, S.2    D'hooge, P.3    Denecker, G.4    Goossens, S.5    De Rycke, R.6
  • 175
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • Sonnenerg A., Liem R.K.H. Plakins in development and disease. Exp. Cell Res. 2007, 313:2189-2203.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2189-2203
    • Sonnenerg, A.1    Liem, R.K.H.2
  • 177
    • 71049116456 scopus 로고    scopus 로고
    • Desmocollin 3-mediated binding is crucial for keratinocyte cohesion and is impaired in pemphigus
    • Spindler V., Heupel W., Efthymidadis A., Schmidt E., Eming E.R., Rank C., et al. Desmocollin 3-mediated binding is crucial for keratinocyte cohesion and is impaired in pemphigus. J. Biol. Chem. 2009, 284:30556.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30556
    • Spindler, V.1    Heupel, W.2    Efthymidadis, A.3    Schmidt, E.4    Eming, E.R.5    Rank, C.6
  • 178
    • 35548987124 scopus 로고    scopus 로고
    • Desmosomes from a structural perspective
    • Stokes D. Desmosomes from a structural perspective. Curr. Opin. Cell Biol. 2007, 19:565-571.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 565-571
    • Stokes, D.1
  • 179
    • 48649101326 scopus 로고    scopus 로고
    • Endothelial adherens junctions control tight junctions by VE-cadherin-mediated upregulation of claudin-5
    • Taddei A., Giampietro C., Conti A., Orsenigo F., Breviario F., Pirazzoli V., et al. Endothelial adherens junctions control tight junctions by VE-cadherin-mediated upregulation of claudin-5. Nat. Cell Biol. 2008, 10:923-934.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 923-934
    • Taddei, A.1    Giampietro, C.2    Conti, A.3    Orsenigo, F.4    Breviario, F.5    Pirazzoli, V.6
  • 181
    • 0242580176 scopus 로고    scopus 로고
    • Adhesive and lateral E-cadherin dimers are mediated by the same interface
    • Troyanovsky R.B., Sokolov E., Troyanovsky S.M. Adhesive and lateral E-cadherin dimers are mediated by the same interface. Mol. Cell. Biol. 2003, 23:7965-7972.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7965-7972
    • Troyanovsky, R.B.1    Sokolov, E.2    Troyanovsky, S.M.3
  • 182
    • 0037442123 scopus 로고    scopus 로고
    • Induction of pemphigus phenotype by a mouse monoclonal antibody against the amino-terminal adhesive interface of desmoglein 3
    • Tsunoda K., Ota T., Aoki M., Yamada T., Nagai T., Nakagawa T., et al. Induction of pemphigus phenotype by a mouse monoclonal antibody against the amino-terminal adhesive interface of desmoglein 3. J. Immunol. 2003, 170:2170-2178.
    • (2003) J. Immunol. , vol.170 , pp. 2170-2178
    • Tsunoda, K.1    Ota, T.2    Aoki, M.3    Yamada, T.4    Nagai, T.5    Nakagawa, T.6
  • 183
    • 0035089312 scopus 로고    scopus 로고
    • Soluble N-cadherin stimulates fibroblast growth factor receptor dependent neurite outgrowth and N-cadherin and the fibroblast growth factor receptor co-cluster in cells
    • Utton M.A., Eickholt B., Howell F.V., Wallis J., Doherty P. Soluble N-cadherin stimulates fibroblast growth factor receptor dependent neurite outgrowth and N-cadherin and the fibroblast growth factor receptor co-cluster in cells. J. Neurochem. 2001, 76:1421-1430.
    • (2001) J. Neurochem. , vol.76 , pp. 1421-1430
    • Utton, M.A.1    Eickholt, B.2    Howell, F.V.3    Wallis, J.4    Doherty, P.5
  • 186
    • 58149490806 scopus 로고    scopus 로고
    • The Sertoli cell cytoskeleton
    • Landes Bioscience, Austin, TX, C.Y. Cheng (Ed.) Molecular Mechanisms in Spermatogenesis
    • Vogl A.W., Vaid K.S., Guttman J. The Sertoli cell cytoskeleton. Advances in Experimental Medicine and Biology 2008, 186-211. Landes Bioscience, Austin, TX. C.Y. Cheng (Ed.).
    • (2008) Advances in Experimental Medicine and Biology , pp. 186-211
    • Vogl, A.W.1    Vaid, K.S.2    Guttman, J.3
  • 187
    • 0034020357 scopus 로고    scopus 로고
    • The α isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells
    • Wallis S., Lloyd S., Wise I., Ireland G., Fleming T.P., Garrod D. The α isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells. Mol. Biol. Cell 2000, 11:1077-1092.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1077-1092
    • Wallis, S.1    Lloyd, S.2    Wise, I.3    Ireland, G.4    Fleming, T.P.5    Garrod, D.6
  • 188
    • 33847282998 scopus 로고    scopus 로고
    • Raf1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor Slug
    • Wang Z., Wade P., Mandell K.J., Akyildiz A., Parkos C.A., Mrsny R.J., et al. Raf1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor Slug. Oncogene 2007, 26:1222-1230.
    • (2007) Oncogene , vol.26 , pp. 1222-1230
    • Wang, Z.1    Wade, P.2    Mandell, K.J.3    Akyildiz, A.4    Parkos, C.A.5    Mrsny, R.J.6
  • 189
    • 73649096912 scopus 로고    scopus 로고
    • A proteomics analysis of rat liver membrane skeletons: the investigation of actin-and cytokeratin-based protein components
    • Wang Q., He J., Meng L., Liu Y., Pu H., Ji J. A proteomics analysis of rat liver membrane skeletons: the investigation of actin-and cytokeratin-based protein components. J. Proteome Res. 2010, 9:22-29.
    • (2010) J. Proteome Res. , vol.9 , pp. 22-29
    • Wang, Q.1    He, J.2    Meng, L.3    Liu, Y.4    Pu, H.5    Ji, J.6
  • 190
    • 27644507915 scopus 로고    scopus 로고
    • Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction
    • Waschke J., Bruggeman P., Baumgartner W., Zillikens D., Drenckhahn D. Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction. J. Clin. Invest. 2005, 115:3157-3165.
    • (2005) J. Clin. Invest. , vol.115 , pp. 3157-3165
    • Waschke, J.1    Bruggeman, P.2    Baumgartner, W.3    Zillikens, D.4    Drenckhahn, D.5
  • 192
    • 0037377674 scopus 로고    scopus 로고
    • Genetic evidence for a novel human desmosomal cadherin, desmoglein 4
    • Whittock N.V., Bower C. Genetic evidence for a novel human desmosomal cadherin, desmoglein 4. J. Invest. Dermatol. 2003, 120:523-530.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 523-530
    • Whittock, N.V.1    Bower, C.2
  • 193
    • 33746494904 scopus 로고    scopus 로고
    • Pemphigus vulgaris identifies plakoglobin as key suppressor of c-Myc in the skin
    • Williamson L., Raess N.A., Caldelari R., Zakher A., de Bruin A., Posthaus H., et al. Pemphigus vulgaris identifies plakoglobin as key suppressor of c-Myc in the skin. EMBO J. 2006, 25:3298-3309.
    • (2006) EMBO J. , vol.25 , pp. 3298-3309
    • Williamson, L.1    Raess, N.A.2    Caldelari, R.3    Zakher, A.4    de Bruin, A.5    Posthaus, H.6
  • 195
    • 23844511497 scopus 로고    scopus 로고
    • Blood-testis barrier dynamics are regulated by an engagement/disengagement mechanism between tight and adherens junctions via peripheral adaptors
    • Yan H.H.N., Cheng C.Y. Blood-testis barrier dynamics are regulated by an engagement/disengagement mechanism between tight and adherens junctions via peripheral adaptors. Proc. Natl. Acad. Sci. USA 2005, 102:11722-11727.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11722-11727
    • Yan, H.H.N.1    Cheng, C.Y.2
  • 197
    • 17244371252 scopus 로고    scopus 로고
    • Plakoglobin suppresses keratinocyte motility through both cell-cell adhesion-dependent and -independent mechanisms
    • Yin T., Getsios S., Caldelari R., Kowalczyk A.P., Muller E.J., Jones J.C.R., et al. Plakoglobin suppresses keratinocyte motility through both cell-cell adhesion-dependent and -independent mechanisms. Proc. Natl. Acad. Sci. USA 2005, 102:5420-5425.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5420-5425
    • Yin, T.1    Getsios, S.2    Caldelari, R.3    Kowalczyk, A.P.4    Muller, E.J.5    Jones, J.C.R.6
  • 198
    • 3342982322 scopus 로고    scopus 로고
    • JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration
    • Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A. JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration. Mol. Biol. Cell 2004, 15:3926-3937.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3926-3937
    • Zen, K.1    Babbin, B.A.2    Liu, Y.3    Whelan, J.B.4    Nusrat, A.5    Parkos, C.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.