메뉴 건너뛰기




Volumn 149, Issue 1, 2000, Pages 209-222

The function of plakophilin 1 in desmosome assembly and actin filament organization

Author keywords

Armadillo; Cell adhesion; Cell motility; Desmoglein; Keratinocytes

Indexed keywords

ACTIN; DESMOGLEIN; KERATIN; NERVE CELL ADHESION MOLECULE;

EID: 0034599841     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.149.1.209     Document Type: Article
Times cited : (142)

References (59)
  • 1
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle, H., H., Schwartz, and R. Kemler. 1996. Cadherin-catenin complex: protein interactions and their implications for cadherin function. J. Cell Biolchem. 61:514-523.
    • (1996) J. Cell Biolchem. , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 2
    • 0029035676 scopus 로고
    • The E-cadherin complex contains the src substrate p120
    • Aghib, D.F., and P.D. McCrea. 1995. The E-cadherin complex contains the src substrate p120. Exp. Cell Res. 218:359-369.
    • (1995) Exp. Cell Res. , vol.218 , pp. 359-369
    • Aghib, D.F.1    McCrea, P.D.2
  • 3
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson, S., D.L. Davis, H. Dahlback, H. Jornvall, an D.W. Russell, 1989. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264: 8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 4
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA
    • Auffray, C., and F. Rougeon. 1980. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur. J. Biochem. 107:303-314.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 303-314
    • Auffray, C.1    Rougeon, F.2
  • 5
    • 0032779596 scopus 로고    scopus 로고
    • Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells
    • Bonne, S., J. van Hengel, F. Nollet, P. Kools, and F. van Roy. 1999. Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells. J. Cell Sci. 112:2265-2276.
    • (1999) J. Cell Sci. , vol.112 , pp. 2265-2276
    • Bonne, S.1    Van Hengel, J.2    Nollet, F.3    Kools, P.4    Van Roy, F.5
  • 6
    • 0029847068 scopus 로고    scopus 로고
    • Breaking lhe connection: Displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger, E.A., C.M. Corcoran, T.S. Stappenbeck, and K.J. Green. 1996. Breaking lhe connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J. Cell Biol. 134: 985-1001.
    • (1996) J. Cell Biol. , vol.134 , pp. 985-1001
    • Bornslaeger, E.A.1    Corcoran, C.M.2    Stappenbeck, T.S.3    Green, K.J.4
  • 8
    • 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. 138:193-201.
    • (1997) J. Cell Biol. , vol.138 , pp. 193-201
    • Chitaev, N.A.1    Troyanovsky, S.M.2
  • 10
    • 0029102071 scopus 로고
    • The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin
    • Daniel, J.M., and A.B. Reynolds. 1995. The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin. Mol. Cell. Biol. 15:4819-4824.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4819-4824
    • Daniel, J.M.1    Reynolds, A.B.2
  • 11
    • 0031259778 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and cadherin/ catenin function
    • Daniel, J.M., and A.B. Reynolds. 1997. Tyrosine phosphorylation and cadherin/ catenin function. Bioessays. 19:883-891.
    • (1997) Bioessays , vol.19 , pp. 883-891
    • Daniel, J.M.1    Reynolds, A.B.2
  • 12
    • 0028842803 scopus 로고
    • Continual assembly of half-desmosomal structures in the absence of cell contacts and their frustrated endocytosis: A coordinated Sisyphus cycle
    • Demlehner, M.P., S. Schafer, C. Grund, and W.W. Franke. 1995. Continual assembly of half-desmosomal structures in the absence of cell contacts and their frustrated endocytosis: a coordinated Sisyphus cycle. J. Cell Biol. 131: 745-760.
    • (1995) J. Cell Biol. , vol.131 , pp. 745-760
    • Demlehner, M.P.1    Schafer, S.2    Grund, C.3    Franke, W.W.4
  • 13
    • 0028954815 scopus 로고
    • Embryonic axis induction by the armadillo repeat domain of beta-catenin: Evidence for intracellular signaling
    • Funayama, N., F. Fagotto, P. McCrea, and B.M. Gumbiner. 1995. Embryonic axis induction by the armadillo repeat domain of beta-catenin: evidence for intracellular signaling. J. Cell Biol. 128:959-968.
    • (1995) J. Cell Biol. , vol.128 , pp. 959-968
    • Funayama, N.1    Fagotto, F.2    McCrea, P.3    Gumbiner, B.M.4
  • 14
    • 0030271472 scopus 로고    scopus 로고
    • Desmosomes: Differentiation, development, dynamics and disease
    • Garrod, D., M. Chidgey, and A. North. 1996. Desmosomes: differentiation, development, dynamics and disease. Curr. Opin. Cell Biol. 8:670-678.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 670-678
    • Garrod, D.1    Chidgey, M.2    North, A.3
  • 15
    • 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., and C. Nachtsheim, 1996. 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. 109:2767-2778.
    • (1996) J. Cell Sci. , vol.109 , pp. 2767-2778
    • Hatzfeld, M.1    Nachtsheim, C.2
  • 16
    • 0028144738 scopus 로고
    • Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family
    • Hatzfeld, M., G.I. Kristjansson, U. Plessmann, and K. Weber. 1994. Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family. J. Cell Sci. 107:2259-2270.
    • (1994) J. Cell Sci. , vol.107 , pp. 2259-2270
    • Hatzfeld, M.1    Kristjansson, G.I.2    Plessmann, U.3    Weber, K.4
  • 18
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex assembly
    • Hinck, L., I.S. Nathke, J. Papkoff, and W.J. Nelson. 1994. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol. 125:1327-1340.
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Nathke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 19
    • 0023917828 scopus 로고
    • r 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia
    • r 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia. J. Cell Biol. 106:1679-1691.
    • (1988) J. Cell Biol. , vol.106 , pp. 1679-1691
    • Kapprell, H.P.1    Owaribe, K.2    Franke, W.W.3
  • 20
    • 0029076819 scopus 로고
    • Anterior axis duplication in Xenopus induced by the over-expression of the cadherin-binding protein plakoglobin
    • Karnovsky, A., and M.W. Klymkowsky. 1995. Anterior axis duplication in Xenopus induced by the over-expression of the cadherin-binding protein plakoglobin. Proc. Natl. Acad. Sci. USA. 92:4522-4526.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4522-4526
    • Karnovsky, A.1    Klymkowsky, M.W.2
  • 21
    • 0033119251 scopus 로고    scopus 로고
    • Plakophilin, armadillo repeats, and nuclear localization
    • Klymkowsky, M.W. 1999. Plakophilin, armadillo repeats, and nuclear localization. Microsc. Res. Tech. 45:43-54.
    • (1999) Microsc. Res. Tech. , vol.45 , pp. 43-54
    • Klymkowsky, M.W.1
  • 22
    • 0028022059 scopus 로고
    • Desmosomal cadherins: Another growing multigene family of adhesion molecules
    • Koch, P.J., and W.W. Franke. 1994. Desmosomal cadherins: another growing multigene family of adhesion molecules. Curr. Opin. Cell Biol. 6:682-687.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 682-687
    • Koch, P.J.1    Franke, W.W.2
  • 23
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis, P.D., E. Hutton, and E. Fuchs. 1994. Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. J. Cell Biol. 127:1049-1060.
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 24
    • 0029816439 scopus 로고    scopus 로고
    • Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes
    • Kowalczyk, A.P., J.E. Borgwardt, and K.J. Green. 1996. Analysis of desmosomal cadherin-adhesive function and stoichiometry of desmosomal cadherin-plakoglobin complexes. J. Invest. Dermatol. 107:293-300.
    • (1996) J. Invest. Dermatol. , vol.107 , pp. 293-300
    • Kowalczyk, A.P.1    Borgwardt, J.E.2    Green, K.J.3
  • 26
    • 0033603436 scopus 로고    scopus 로고
    • The head domain of plakophilin-1 binds to desmoplakin and enhances its recruitment to desmosomes. Implications for cutaneous disease
    • Kowalczyk, A.P., M. Hatzfeld, E.A. Bornslaeger, D.S. Kopp, J.E. Borgwardt, C.M. Corcoran, A. Settler, and K.J. Green. 1999. The head domain of plakophilin-1 binds to desmoplakin and enhances its recruitment to desmosomes. Implications for cutaneous disease. J. Biol. Chem. 274:18145-18148.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18145-18148
    • Kowalczyk, A.P.1    Hatzfeld, M.2    Bornslaeger, E.A.3    Kopp, D.S.4    Borgwardt, J.E.5    Corcoran, C.M.6    Settler, A.7    Green, K.J.8
  • 27
    • 0028365071 scopus 로고
    • Cadherin function is required for human keratinocytes to assemble desmosomes and stratify in response to calcium
    • Lewis, J.E., P.J. Jensen, and M.J. Wheelock, 1994. Cadherin function is required for human keratinocytes to assemble desmosomes and stratify in response to calcium. J. Invest. Dermatol. 102:870-877.
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 870-877
    • Lewis, J.E.1    Jensen, P.J.2    Wheelock, M.J.3
  • 30
    • 0028318203 scopus 로고
    • Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin
    • Mathur, M., L. Goodwin, and P. Cowin. 1994. Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin. J. Biol. Chem. 269:14075-14080.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14075-14080
    • Mathur, M.1    Goodwin, L.2    Cowin, P.3
  • 32
    • 0030856050 scopus 로고    scopus 로고
    • Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments
    • Meng, J.J., E.A. Bornslaeger, K.J. Green, P.M. Steinert, and W. Ip. 1997. Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments. J. Biol. Chem. 272:21495-21503.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21495-21503
    • Meng, J.J.1    Bornslaeger, E.A.2    Green, K.J.3    Steinert, P.M.4    Ip, W.5
  • 33
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: Constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • Mertens, C., C. Kuhn, and W.W. Franke. 1996. Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J. Cell Biol. 135:1009-1025.
    • (1996) J. Cell Biol. , vol.135 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 34
    • 0029798055 scopus 로고    scopus 로고
    • Distinct desmocollin isoforms occur in the same desmosomes and show reciprocally graded distributions in bovine nasal epidermis
    • North, A.J., M.A. Chidgey, J.P. Clarke, W.G. Bardsley, and D.R. Garrod. 1996. Distinct desmocollin isoforms occur in the same desmosomes and show reciprocally graded distributions in bovine nasal epidermis. Proc. Natl. Acad. Sci. USA. 93:7701-7705.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7701-7705
    • North, A.J.1    Chidgey, M.A.2    Clarke, J.P.3    Bardsley, W.G.4    Garrod, D.R.5
  • 35
    • 21544441484 scopus 로고    scopus 로고
    • Roles of plakoglobin end domains in desmosome assembly
    • Palka, H., and K. Green. 1997. Roles of plakoglobin end domains in desmosome assembly. J. Cell Sci. 110:2359-2371.
    • (1997) J. Cell Sci. , vol.110 , pp. 2359-2371
    • Palka, H.1    Green, K.2
  • 36
    • 0023864445 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilisation upon cell-cell contact. I. Biochemical analysis
    • Pasdar, M., and W.J. Nelson. 1988. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilisation upon cell-cell contact. I. Biochemical analysis. J. Cell Biol. 106:677-685.
    • (1988) J. Cell Biol. , vol.106 , pp. 677-685
    • Pasdar, M.1    Nelson, W.J.2
  • 37
    • 0024383949 scopus 로고
    • Regulation of desmosome assembly in epithelial cells: Kinetics of synthesis, transport, and stabilisation of desmoglein 1, a major protein of the membrane core domain
    • Pasdar, M., and W.J. Nelson. 1989. Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilisation of desmoglein 1, a major protein of the membrane core domain. J. Cell Biol. 109:163-177.
    • (1989) J. Cell Biol. , vol.109 , pp. 163-177
    • Pasdar, M.1    Nelson, W.J.2
  • 38
    • 0028019276 scopus 로고
    • Identification of a new catenin: The tyrosine kinase substrate p120cas associates with E-cadherin complexes
    • Reynolds, A.B., J. Daniel, P.D. McCrea, M.J. Wheelock, J. Wu, and Z. Zhang. 1994. Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes. Mol. Cell. Biol. 14:8333-8342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8333-8342
    • Reynolds, A.B.1    Daniel, J.2    McCrea, P.D.3    Wheelock, M.J.4    Wu, J.5    Zhang, Z.6
  • 39
    • 0029665589 scopus 로고    scopus 로고
    • The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts
    • Reynolds, A.B., J.M. Daniel, Y.Y. Mo, J. Wu, and Z. Zhang. 1996. The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts. Exp. Cell Res. 225:328-337.
    • (1996) Exp. Cell Res. , vol.225 , pp. 328-337
    • Reynolds, A.B.1    Daniel, J.M.2    Mo, Y.Y.3    Wu, J.4    Zhang, Z.5
  • 40
    • 0030887357 scopus 로고    scopus 로고
    • Localizing the adhesive and signaling functions of plakoglobin
    • Rubenstein, A., J. Merriam, and M.W. Klymkowsky. 1997. Localizing the adhesive and signaling functions of plakoglobin. Dev. Genet. 20:91-102.
    • (1997) Dev. Genet. , vol.20 , pp. 91-102
    • Rubenstein, A.1    Merriam, J.2    Klymkowsky, M.W.3
  • 42
    • 0029123863 scopus 로고
    • Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin
    • Sacco, P.A., T.M. McGranahan, M.J. Wheelock, and K.R. Johnson. 1995. Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin. J. Biol. Chem. 270:20201-20206.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20201-20206
    • Sacco, P.A.1    McGranahan, T.M.2    Wheelock, M.J.3    Johnson, K.R.4
  • 43
    • 0028577357 scopus 로고
    • Desmosomes and cytoskeletal architecture in epithelial differentiation: Cell type-specific plaque components and intermediate filament anchorage
    • Schmidt, A., H.W. Heid, S. Schafer, U.A. Nuber, R. Zimbelmann, and W.W. Franke. 1994. Desmosomes and cytoskeletal architecture in epithelial differentiation: cell type-specific plaque components and intermediate filament anchorage. Eur. J. Cell Biol. 65:229-245.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 229-245
    • Schmidt, A.1    Heid, H.W.2    Schafer, S.3    Nuber, U.A.4    Zimbelmann, R.5    Franke, W.W.6
  • 44
    • 0030856140 scopus 로고    scopus 로고
    • Plakophilins 1a and 1b: Widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components
    • Schmidt, A., L. Langbein, M. Rode, S. Pratzel, R. Zimbelmann, and W.W. Franke. 1997. Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components. Cell Tissue Res. 290:481-499.
    • (1997) Cell Tissue Res. , vol.290 , pp. 481-499
    • Schmidt, A.1    Langbein, L.2    Rode, M.3    Pratzel, S.4    Zimbelmann, R.5    Franke, W.W.6
  • 46
    • 0032557825 scopus 로고    scopus 로고
    • Protein-protein interactions between keratin polypeptides expressed in the yeast two-hybrid system
    • Schnabel, J., K. Weber, and M. Hatzfeld. 1998. Protein-protein interactions between keratin polypeptides expressed in the yeast two-hybrid system. Biochim. Biophys. Acta. 1403:158-168.
    • (1998) Biochim. Biophys. Acta. , vol.1403 , pp. 158-168
    • Schnabel, J.1    Weber, K.2    Hatzfeld, M.3
  • 48
    • 0032100705 scopus 로고    scopus 로고
    • Defining the interactions between intermediate filaments and desmosomes
    • Smith, E.A., and F. Fuchs. 1998. Defining the interactions between intermediate filaments and desmosomes. J. Cell Biol. 141:1229-1241.
    • (1998) J. Cell Biol. , vol.141 , pp. 1229-1241
    • Smith, E.A.1    Fuchs, F.2
  • 49
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • Stappenbeck, T.S., E.A. Bornslaeger, C.M. Corcoran, H.H. Luu, M.L. Virata, and K.J. Green. 1993. Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks. J. Cell Biol. 123:691-705.
    • (1993) J. Cell Biol. , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3    Luu, H.H.4    Virata, M.L.5    Green, K.J.6
  • 50
    • 0028028177 scopus 로고
    • Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks
    • Stappenbeck, T.S., J.A. Lamb, C.M. Corcoran, and K.J. Green. 1994. Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. J. Biol. Chem. 269:29351-29354.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29351-29354
    • Stappenbeck, T.S.1    Lamb, J.A.2    Corcoran, C.M.3    Green, K.J.4
  • 51
    • 0029776445 scopus 로고    scopus 로고
    • β-Catenin associates with the actin-bundling protein fascin in a noncadherin complex
    • Tao, Y.S., R.A. Edwards, B. Tubb, S. Wang, J. Bryan, and P.D. McCrea. 1996. β-Catenin associates with the actin-bundling protein fascin in a noncadherin complex. J. Cell Biol. 134:1271-1281.
    • (1996) J. Cell Biol. , vol.134 , pp. 1271-1281
    • Tao, Y.S.1    Edwards, R.A.2    Tubb, B.3    Wang, S.4    Bryan, J.5    McCrea, P.D.6
  • 52
    • 0030479469 scopus 로고    scopus 로고
    • Cadherin binding sites of plakoglobin: Localization, specificity and role in targeting to adhering junctions
    • Troyanovsky, R.B., N.A. Chitaev, and S.M. Troyanovsky. 1996. Cadherin binding sites of plakoglobin: localization, specificity and role in targeting to adhering junctions. J. Cell Sci. 109:3069-3078.
    • (1996) J. Cell Sci. , vol.109 , pp. 3069-3078
    • Troyanovsky, R.B.1    Chitaev, N.A.2    Troyanovsky, S.M.3
  • 53
    • 0027468175 scopus 로고
    • Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage
    • Troyanovsky, S.M., L.G. Eshkind, R.B. Troyanovsky, R.E. Leube, and W.W. Franke. 1993. Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage. Cell. 72:561-574.
    • (1993) Cell , vol.72 , pp. 561-574
    • Troyanovsky, S.M.1    Eshkind, L.G.2    Troyanovsky, R.B.3    Leube, R.E.4    Franke, W.W.5
  • 54
    • 0028031044 scopus 로고
    • Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage
    • Troyanovsky, S.M., R.B. Troyanovsky, L.G. Eshkind, V.A. Krutovskikh, R.E. Leube, and W.W. Franke. 1994a. Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage. J. Cell Biol. 127:151-160.
    • (1994) J. Cell Biol. , vol.127 , pp. 151-160
    • Troyanovsky, S.M.1    Troyanovsky, R.B.2    Eshkind, L.G.3    Krutovskikh, V.A.4    Leube, R.E.5    Franke, W.W.6
  • 55
    • 0028153267 scopus 로고
    • Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation
    • Troyanovsky, S.M., R.B. Troyanovsky, L.G. Eshkind, R.E. Leube, and W.W. Franke. 1994b. Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation. Proc. Natl. Acad. Sci. USA. 91:10790-10794.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10790-10794
    • Troyanovsky, S.M.1    Troyanovsky, R.B.2    Eshkind, L.G.3    Leube, R.E.4    Franke, W.W.5
  • 56
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukila, S., S. Yonemura, and S. Tsukita. 1997. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22:53-58.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 53-58
    • Tsukila, S.1    Yonemura, S.2    Tsukita, S.3
  • 57
    • 0029941032 scopus 로고    scopus 로고
    • Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: Identification of unique and shared domains
    • Wahl, J.K., P.A. Sacco, T.M. McGranahan-Sadler, L.M. Sauppe, M.J. Wheelock, and K.R. Johnson. 1996. Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: identification of unique and shared domains. J. Cell Sci. 109:1143-1154.
    • (1996) J. Cell Sci. , vol.109 , pp. 1143-1154
    • Wahl, J.K.1    Sacco, P.A.2    McGranahan-Sadler, T.M.3    Sauppe, L.M.4    Wheelock, M.J.5    Johnson, K.R.6
  • 58
    • 0343058961 scopus 로고    scopus 로고
    • The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy
    • Winkler, J., H. Lunsdorf, and B.M. Jockusch. 1996. The ultrastructure of chicken gizzard vinculin as visualized by high-resolution electron microscopy. J. Struct. Biol. 116:270-277.
    • (1996) J. Struct. Biol. , vol.116 , pp. 270-277
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.