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Volumn 142, Issue 1, 1998, Pages 271-284

Hemidesmosome formation is initiated by the β4 integrin subunit, requires complex formation of β4 and HD1/plectin, and involves a direct interaction between β4 and the bullous pemphigoid antigen 180

Author keywords

6 4 integrin; Bullous pemphigoid antigens; Hemidesmosome assembly; PA JEB keratinocytes; Protein protein interaction

Indexed keywords

INTEGRIN;

EID: 0032514156     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.142.1.271     Document Type: Article
Times cited : (164)

References (85)
  • 1
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andrä, K., H. Lassmann, R. Bittner, S. Shorny, R. Fässler, F. Propst, and G. Wiche. 1997. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 11:3143-3156.
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, F.6    Wiche, G.7
  • 2
    • 0030753712 scopus 로고    scopus 로고
    • Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: Involvement of IFAP300/HD1 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin
    • Baker, S.E., O. Skalli, R.D. Goldman, and J.C.R. Jones. 1997. Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: involvement of IFAP300/HD1 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin. Cell Motil. Cytoskeleton. 36:271-286.
    • (1997) Cell Motil. Cytoskeleton. , vol.36 , pp. 271-286
    • Baker, S.E.1    Skalli, O.2    Goldman, R.D.3    Jones, J.C.R.4
  • 3
    • 0030272476 scopus 로고    scopus 로고
    • Hemidesmosomes: Roles in adhesion, signaling and human diseases
    • Borradori, L., and A. Sonnenberg. 1996. Hemidesmosomes: roles in adhesion, signaling and human diseases. Curr. Opin. Cell Biol. 8:647-656.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 647-656
    • Borradori, L.1    Sonnenberg, A.2
  • 4
    • 0030773865 scopus 로고    scopus 로고
    • The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the β4 integrin subunit
    • Borradori, L., P.J., Koch, C.M. Niessen, S. Erkeland, M.R. van Leusden, and A. Sonnenberg. 1997. The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the β4 integrin subunit. J. Cell Biol. 136:1333-1347.
    • (1997) J. Cell Biol. , vol.136 , pp. 1333-1347
    • Borradori, L.1    Koch, P.J.2    Niessen, C.M.3    Erkeland, S.4    Van Leusden, M.R.5    Sonnenberg, A.6
  • 5
    • 0031845619 scopus 로고    scopus 로고
    • Role of the bullous pemphigoid antigen 180 (BP180) in the assembly of hemidesmosomes and cell adhesion. Reexpression of BP180 in generalized atrophic benign epidermolysis bullosa keratinocytes
    • Borradori, L., S. Chavanas, R.Q.J. Schaapveld, L. Gagnoux-Palacios, J. Calafat, G. Meneguzzi, and A. Sonnenberg. 1998. Role of the bullous pemphigoid antigen 180 (BP180) in the assembly of hemidesmosomes and cell adhesion. Reexpression of BP180 in generalized atrophic benign epidermolysis bullosa keratinocytes. Exp. Cell Res. 239:463-476.
    • (1998) Exp. Cell Res. , vol.239 , pp. 463-476
    • Borradori, L.1    Chavanas, S.2    Schaapveld, R.Q.J.3    Gagnoux-Palacios, L.4    Calafat, J.5    Meneguzzi, G.6    Sonnenberg, A.7
  • 6
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface strutures
    • Bretscher, A., D. Reczek, and M. Berryman. 1997. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface strutures. J. Cell Sci. 110:3011-3018.
    • (1997) J. Cell Sci. , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 7
    • 0029813342 scopus 로고    scopus 로고
    • Defective integrin α6β4 expression in the skin of patients with junctional epidermolysis bullosa and pyloric atresia
    • Brown, T.A., S.G. Gil, V.P. Sybert, G.G. Lestringant, G. Tadini, R. Caputo, and W.G. Carter. 1996. Defective integrin α6β4 expression in the skin of patients with junctional epidermolysis bullosa and pyloric atresia. J. Invest. Dermatol. 107:385-391.
    • (1996) J. Invest. Dermatol. , vol.107 , pp. 385-391
    • Brown, T.A.1    Gil, S.G.2    Sybert, V.P.3    Lestringant, G.G.4    Tadini, G.5    Caputo, R.6    Carter, W.G.7
  • 9
    • 0025679064 scopus 로고
    • Distinct functions for integrins α3β1 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: Relation to hemidesmosomes
    • Carter, W.G., P. Kaur, S.G. Gil, P.J. Gahr, and E.A. Wayner. 1990. Distinct functions for integrins α3β1 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J. Cell Biol. 111:3141-3154.
    • (1990) J. Cell Biol. , vol.111 , pp. 3141-3154
    • Carter, W.G.1    Kaur, P.2    Gil, S.G.3    Gahr, P.J.4    Wayner, E.A.5
  • 10
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for α3β1 in epithelial basement membranes
    • Carter, W.G., M.C. Ryan, and P.J. Gahr. 1991. Epiligrin, a new cell adhesion ligand for α3β1 in epithelial basement membranes. Cell. 65:599-610.
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 11
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen, B.R. 1987. Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol. 152:684-703.
    • (1987) Methods Enzymol. , vol.152 , pp. 684-703
    • Cullen, B.R.1
  • 13
    • 0029666420 scopus 로고    scopus 로고
    • β4 integrin is required for hemidesmosome formation, cell adhesion, and cell survival
    • Dowling, J., Q.-C. Yu, and E. Fuchs. 1996. β4 integrin is required for hemidesmosome formation, cell adhesion, and cell survival. J. Cell Biol. 134:559-572.
    • (1996) J. Cell Biol. , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.-C.2    Fuchs, E.3
  • 15
    • 0024917751 scopus 로고
    • Insulin-induced phosphorylation of the β4 integrin subunit expressed on murine metastatic carcinoma cells
    • Falcioni, R., N. Perrotti, G. Piaggio, S.K. Kennel, and A. Sacchi. 1989. Insulin-induced phosphorylation of the β4 integrin subunit expressed on murine metastatic carcinoma cells. Mol. Carcinogen. 2:361-368.
    • (1989) Mol. Carcinogen. , vol.2 , pp. 361-368
    • Falcioni, R.1    Perrotti, N.2    Piaggio, G.3    Kennel, S.K.4    Sacchi, A.5
  • 16
    • 0024406857 scopus 로고
    • A novel system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel system to detect protein-protein interactions. Nature. 340:245-247.
    • (1989) Nature , vol.340 , pp. 245-247
    • Fields, S.1    Song, O.2
  • 17
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., F.E. Leichtfried, H. Herrmann, J.V. Small, D. Lawson, and G. Wiche. 1988. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106:723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 19
    • 0030718613 scopus 로고    scopus 로고
    • Hemidesmosome assembly assessed by expression of a wild-type integrin β4 cDNA in functional epidermolysis bullosa keratinocytes
    • Gagnoux-Palacios, L., Y. Gache, J.P. Ortonne, and G. Meneguzzi. 1997. Hemidesmosome assembly assessed by expression of a wild-type integrin β4 cDNA in functional epidermolysis bullosa keratinocytes. Lab. Invest. 77:459-468.
    • (1997) Lab. Invest. , vol.77 , pp. 459-468
    • Gagnoux-Palacios, L.1    Gache, Y.2    Ortonne, J.P.3    Meneguzzi, G.4
  • 21
    • 0029999172 scopus 로고    scopus 로고
    • Signal transduction by the α6β4 integrin: Charting the path between laminin binding and nuclear events
    • Giancotti, F.G. 1996. Signal transduction by the α6β4 integrin: charting the path between laminin binding and nuclear events. J. Cell. Sci. 109:1165-1172.
    • (1996) J. Cell. Sci. , vol.109 , pp. 1165-1172
    • Giancotti, F.G.1
  • 22
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R.D., R.H. Schiestl, A.R. Willems, and R.A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast. 11:355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 23
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • Gilmore, A.P., and K. Burridge. 1996. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature. 381:531-535.
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 24
    • 0026726355 scopus 로고
    • Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180
    • Giudice, G.J., D.J. Emery, and L.A. Diaz. 1992. Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180. J. Invest. Dermatol. 99:243-250.
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 243-250
    • Giudice, G.J.1    Emery, D.J.2    Diaz, L.A.3
  • 25
    • 0025338007 scopus 로고
    • Developmental changes in expression of contractile and cytoskeletal proteins in human aortic smooth muscle
    • Glukhova, M.A., M.G. Frid, and V.E. Koteliansky. 1990. Developmental changes in expression of contractile and cytoskeletal proteins in human aortic smooth muscle. J. Biol. Chem. 265:13042-13046.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13042-13046
    • Glukhova, M.A.1    Frid, M.G.2    Koteliansky, V.E.3
  • 26
    • 0030006606 scopus 로고    scopus 로고
    • Desmosomes and hemidesmosomes: Structure and function of molecular components
    • Green, K.J. and J.C.R. Jones. 1996. Desmosomes and hemidesmosomes: structure and function of molecular components. FASEB (Fed. Am. Soc. Exp. Biol.) J. 10:871-881.
    • (1996) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.10 , pp. 871-881
    • Green, K.J.1    Jones, J.C.R.2
  • 27
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo, L., L. Degenstein, J. Dowling, Q.-C. Yu, R. Wollman, R. Perman, and E. Fuchs. 1995. Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.-C.4    Wollman, R.5    Perman, R.6    Fuchs, E.7
  • 28
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper, J.W., G. Adami, N. Wei, K. Keyomarski, and S.J. Elledge. 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 75:805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.2    Wei, N.3    Keyomarski, K.4    Elledge, S.J.5
  • 29
    • 0023126564 scopus 로고
    • Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • Herrmann, H., and G. Wiche. 1987. Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J. Biol. Chem. 262:1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 30
    • 0021358938 scopus 로고
    • Basement membrane diversity detected by monoclonal antibodies
    • Hessle, H., L.Y. Sakai, D.W. Hollister, and E. Engvall. 1984. Basement membrane diversity detected by monoclonal antibodies. Differentiation. 26:49-54.
    • (1984) Differentiation , vol.26 , pp. 49-54
    • Hessle, H.1    Sakai, L.Y.2    Hollister, D.W.3    Engvall, E.4
  • 31
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda, Y., Y. Nishizawa, J. Uematsu, and K. Owaribe. 1992. Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116:1497-1506.
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 32
    • 0025117579 scopus 로고
    • Cloning and sequence analysis of β4 cDNA: An integrin subunit that contains a unique 118 kD cytoplasmic domain
    • Hogervorst, F., I. Kuikman, A.E.G. Kr. von dem Borne, and A. Sonnenberg. 1990. Cloning and sequence analysis of β4 cDNA: an integrin subunit that contains a unique 118 kD cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 9:765-770.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 765-770
    • Hogervorst, F.1    Kuikman, I.2    Von Dem Borne, A.E.G.Kr.3    Sonnenberg, A.4
  • 34
    • 0026730506 scopus 로고
    • Cytoplasmic domain of the 180-kD bullous pemphigoid antigen, a hemidesmosomal component: Molecular and cell biologic characterization
    • Hopkinson, S.B., K.S. Riddelle, and J.C.R. Jones. 1992. Cytoplasmic domain of the 180-kD bullous pemphigoid antigen, a hemidesmosomal component: molecular and cell biologic characterization. J. Invest. Dermatol. 99:264-270.
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 264-270
    • Hopkinson, S.B.1    Riddelle, K.S.2    Jones, J.C.R.3
  • 35
    • 0029005210 scopus 로고
    • Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/ BP180): Identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and α6 integrin
    • Hopkinson, S.B., S.E. Baker, and J.C.R. Jones. 1995. Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/ BP180): identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and α6 integrin. J. Cell Biol. 130:117-125.
    • (1995) J. Cell Biol. , vol.130 , pp. 117-125
    • Hopkinson, S.B.1    Baker, S.E.2    Jones, J.C.R.3
  • 36
    • 0027174586 scopus 로고
    • Use of the two-hybrid system to identify the domain of p53 involved in oligomerization
    • Iwabuchi, K., B. Li, P. Bartel, and S. Fields. 1993. Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene. 8:1693-1696.
    • (1993) Oncogene , vol.8 , pp. 1693-1696
    • Iwabuchi, K.1    Li, B.2    Bartel, P.3    Fields, S.4
  • 37
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E.A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics. 144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 38
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R.P., and S.W. Craig. 1995. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature. 373:261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 40
    • 0023626543 scopus 로고
    • Biochemical analysis of two cell surface glycoprotein complexes, very common antigen 1 and very common antigen 2
    • Kantor, R.R.S, M.J. Mattes, K.O. Lloyd, L.J. Old, and A.P. Albino. 1987. Biochemical analysis of two cell surface glycoprotein complexes, very common antigen 1 and very common antigen 2. J. Biol. Chem. 262:15158-15165.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15158-15165
    • Kantor, R.R.S.1    Mattes, M.J.2    Lloyd, K.O.3    Old, L.J.4    Albino, A.P.5
  • 41
    • 0023619965 scopus 로고
    • Role of p150,95 in adhesion, migration, chemotaxis and phagocytosis of human monocytes
    • Keizer, G.D., A.A. te Velde, R. Schwarting, C.G. Figdor, and J.E. de Vries. 1987. Role of p150,95 in adhesion, migration, chemotaxis and phagocytosis of human monocytes. Eur. J. Immunol. 17:1317-1322.
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1317-1322
    • Keizer, G.D.1    Te Velde, A.A.2    Schwarting, R.3    Figdor, C.G.4    De Vries, J.E.5
  • 42
  • 44
    • 0026166472 scopus 로고
    • A novel hemidesmosomal plaque component: Tissue distribution and incorporation into assembling hemidesmosomes in an in vitro model
    • Kurpakus, M.A, and J.C.R. Jones. 1991. A novel hemidesmosomal plaque component: tissue distribution and incorporation into assembling hemidesmosomes in an in vitro model. Exp. Cell Res. 194:139-146.
    • (1991) Exp. Cell Res. , vol.194 , pp. 139-146
    • Kurpakus, M.A.1    Jones, J.C.R.2
  • 45
    • 0027163762 scopus 로고
    • Identification of mutations in p53 that affect its binding to SV40 T antigen by using the yeast two-hybrid system
    • Li, B., and S. Fields. 1993. Identification of mutations in p53 that affect its binding to SV40 T antigen by using the yeast two-hybrid system. FASEB (Fed. Am. Soc. Exp. Biol.) J. 7:957-963.
    • (1993) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.7 , pp. 957-963
    • Li, B.1    Fields, S.2
  • 46
    • 0027477628 scopus 로고
    • Cloning of type XVII collagen. Complementary and genomic DNA sequences of mouse 180-kilodalton bullous pemphigoid antigen (BPAG2) predict an interrupted collagenous domain, a transmembrane segment, and unusual features in the 5′-end of the gene and the 3′-untranslaled region of the mRNA
    • Li, K., K. Tamai, E.M.L. Tan, and J. Uitto. 1993. Cloning of type XVII collagen. Complementary and genomic DNA sequences of mouse 180-kilodalton bullous pemphigoid antigen (BPAG2) predict an interrupted collagenous domain, a transmembrane segment, and unusual features in the 5′-end of the gene and the 3′-untranslaled region of the mRNA. J. Biol. Chem. 268:8825-8834.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8825-8834
    • Li, K.1    Tamai, K.2    Tan, E.M.L.3    Uitto, J.4
  • 47
    • 0029115343 scopus 로고
    • Signal transduction by the α6β4 integrin: Distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • Mainiero, F., A. Pepe, K.K. Wary, L. Spinardi, M. Mohammadi, J. Schlessinger, and F.G. Giancotti. 1995. Signal transduction by the α6β4 integrin: distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. EMBO (Eur. Mol. Biol. Organ.) J. 14: 4470-4481.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 48
    • 0026061088 scopus 로고
    • Polarized expression of integrin receptors (α6β4, α2β1, α3β1, and αvβ5) and their relationship with the cytoskeletal and basement membrane matrix in cultured human keratinocytes
    • Marchisio, P.C., S. Bondanza, O. Cremona, R. Cancedda, and M. De Luca. 1991. Polarized expression of integrin receptors (α6β4, α2β1, α3β1, and αvβ5) and their relationship with the cytoskeletal and basement membrane matrix in cultured human keratinocytes. J. Cell Biol. 112:761-773.
    • (1991) J. Cell Biol. , vol.112 , pp. 761-773
    • Marchisio, P.C.1    Bondanza, S.2    Cremona, O.3    Cancedda, R.4    De Luca, M.5
  • 50
    • 0029121987 scopus 로고
    • Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa
    • McGrath, J.A., B. Gatalica, A.M. Christiano, K. Li, K. Owaribe, J.R. McMillan, R.A. Eady, and J. Uitto. 1995. Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa. Nature Genet. 11:83-86.
    • (1995) Nature Genet. , vol.11 , pp. 83-86
    • McGrath, J.A.1    Gatalica, B.2    Christiano, A.M.3    Li, K.4    Owaribe, K.5    McMillan, J.R.6    Eady, R.A.7    Uitto, J.8
  • 52
    • 0024428508 scopus 로고
    • The E6 and E7 genes of the human papillomavirus type 16 together are necessary and sufficient for transformation of primary human keratinocytes
    • Münger, K., W.C. Phelps, V. Bubb, P.M. Howley, and R. Schlegel. 1989. The E6 and E7 genes of the human papillomavirus type 16 together are necessary and sufficient for transformation of primary human keratinocytes. J. Virol. 63:4417-4421.
    • (1989) J. Virol. , vol.63 , pp. 4417-4421
    • Münger, K.1    Phelps, W.C.2    Bubb, V.3    Howley, P.M.4    Schlegel, R.5
  • 54
    • 0029990621 scopus 로고    scopus 로고
    • Deficiency of the integrin β4 subunit in junctional epidermolysis bullosa with pyloric atresia: Consequences for hemidesmosome formation and adhesion properties
    • Niessen, C.M., L.M.H. van der Raaij-Helmer, E.H.M. Hulsman, R. van der Neut, M.F. Jonkman, and A. Sonnenberg. 1996. Deficiency of the integrin β4 subunit in junctional epidermolysis bullosa with pyloric atresia: consequences for hemidesmosome formation and adhesion properties. J. Cell Sci. 109:1695-1706.
    • (1996) J. Cell Sci. , vol.109 , pp. 1695-1706
    • Niessen, C.M.1    Van Der Raaij-Helmer, L.M.H.2    Hulsman, E.H.M.3    Van Der Neut, R.4    Jonkman, M.F.5    Sonnenberg, A.6
  • 55
    • 0030820604 scopus 로고    scopus 로고
    • A minimal region on the integrin β4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells
    • Niessen, C.M., E.H.M. Hulsman, L.C.J.M. Oomen, I. Kuikman, and A. Sonnenberg. 1997a. A minimal region on the integrin β4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells. J. Cell Sci. 110:1705-1716.
    • (1997) J. Cell Sci. , vol.110 , pp. 1705-1716
    • Niessen, C.M.1    Hulsman, E.H.M.2    Oomen, L.C.J.M.3    Kuikman, I.4    Sonnenberg, A.5
  • 56
    • 0030975508 scopus 로고    scopus 로고
    • Integrin α6β4 forms a complex with the cytoskeletal protein HD1 and induces its redistribution in transfected COS-7 cells
    • Niessen, C.M., E.H.M. Hulsman, E.S. Rots, P. Sánchez-Aparicio, and A. Sonnenberg. 1997b. Integrin α6β4 forms a complex with the cytoskeletal protein HD1 and induces its redistribution in transfected COS-7 cells. Mol. Biol. Cell. 8:555-566.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 555-566
    • Niessen, C.M.1    Hulsman, E.H.M.2    Rots, E.S.3    Sánchez-Aparicio, P.4    Sonnenberg, A.5
  • 58
    • 0027194934 scopus 로고
    • HD4, a 180 kDa bullous pemphigoid antigen, is a major transmembrane glycoprotein of the hemidesmosome
    • Nishizawa, Y., J. Uematsu, and K. Owaribe. 1993. HD4, a 180 kDa bullous pemphigoid antigen, is a major transmembrane glycoprotein of the hemidesmosome. J. Biochem. (Tokyo). 113:493-501.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 493-501
    • Nishizawa, Y.1    Uematsu, J.2    Owaribe, K.3
  • 59
    • 0030611108 scopus 로고    scopus 로고
    • Homozygous α6 integrin mutation in junctional epidermolysis bullosa with congenital duodenal atresia
    • Pulkkinen, L., V.E. Kimonis, Y. Xu, E.N. Spanou, W.H.I. McLean, and J. Uitto, 1997. Homozygous α6 integrin mutation in junctional epidermolysis bullosa with congenital duodenal atresia. Hum. Mol. Genet. 6:669-674.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 669-674
    • Pulkkinen, L.1    Kimonis, V.E.2    Xu, Y.3    Spanou, E.N.4    McLean, W.H.I.5    Uitto, J.6
  • 60
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle, P., G.P. Lundstrum., D.R. Keene, and R.E. Burgeson. 1991. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114:567-576.
    • (1991) J. Cell Biol. , vol.114 , pp. 567-576
    • Rousselle, P.1    Lundstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 61
    • 0028294842 scopus 로고
    • Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors
    • Rousselle, P., and M. Aumailley. 1994. Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J. Cell Biol. 125:205-214.
    • (1994) J. Cell Biol. , vol.125 , pp. 205-214
    • Rousselle, P.1    Aumailley, M.2
  • 64
    • 0026052915 scopus 로고
    • Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains
    • Sawamura, D., K. Li, M.L. Chu, and J. Uitto. 1991. Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains. J. Biol. Chem. 266:17784-17790.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17784-17790
    • Sawamura, D.1    Li, K.2    Chu, M.L.3    Uitto, J.4
  • 65
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • Skalli, O., J.C.R. Jones, R. Gagescu, and R.D. Goldman. 1994. IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions. J. Cell Biol. 125:159-170.
    • (1994) J. Cell Biol. , vol.125 , pp. 159-170
    • Skalli, O.1    Jones, J.C.R.2    Gagescu, R.3    Goldman, R.D.4
  • 67
    • 0022977799 scopus 로고
    • In vitro differentiation and progression of mouse mammary tumor cells
    • Sonnenberg, A., H. Daams, J. Calafat, and J. Hilgers. 1986. In vitro differentiation and progression of mouse mammary tumor cells. Cancer Res. 46:5913-5922.
    • (1986) Cancer Res. , vol.46 , pp. 5913-5922
    • Sonnenberg, A.1    Daams, H.2    Calafat, J.3    Hilgers, J.4
  • 68
    • 0023664709 scopus 로고
    • A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody
    • Sonnenberg, A., H. Janssen, F. Hogervorst, J. Calafat, and J. Hilgers. 1987. A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody. J. Biol. Chem. 262:10376-10383.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogervorst, F.3    Calafat, J.4    Hilgers, J.5
  • 69
    • 0027746104 scopus 로고
    • Formation of hemidesmosomes in cells of a transformed murine mammary tumor cell line and mechanisms involved in adherence of these cells to laminin and kalinin
    • Sonnenberg, A., A.A. de Melker, A.M. Martínez de Velasco, H. Janssen, J. Calafat, and C.M. Niessen. 1993. Formation of hemidesmosomes in cells of a transformed murine mammary tumor cell line and mechanisms involved in adherence of these cells to laminin and kalinin. J. Cell Sci. 106:1083-1102.
    • (1993) J. Cell Sci. , vol.106 , pp. 1083-1102
    • Sonnenberg, A.1    De Melker, A.A.2    De Martínez Velasco, A.M.3    Janssen, H.4    Calafat, J.5    Niessen, C.M.6
  • 70
    • 0027369205 scopus 로고
    • The β4 subunit cytoplasmic domain mediates the interaction of α6β4 integrin with the cytoskeleton of hemidesmosomes
    • Spinardi, L., Y.-L. Ren, R. Sanders, and F.G. Giancotti. 1993. The β4 subunit cytoplasmic domain mediates the interaction of α6β4 integrin with the cytoskeleton of hemidesmosomes. Mol. Biol. Cell. 4:871-884.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 871-884
    • Spinardi, L.1    Ren, Y.-L.2    Sanders, R.3    Giancotti, F.G.4
  • 71
    • 0028944247 scopus 로고
    • A recombinant tail-less integrin β4 subunit disrupts hemidesmosomes, but does not suppress α6β4-mediated cell adhesion to laminins
    • Spinardi, L., S. Einheber, T. Cullen, T.A. Milner, and F.G. Giancotti. 1995. A recombinant tail-less integrin β4 subunit disrupts hemidesmosomes, but does not suppress α6β4-mediated cell adhesion to laminins. J. Cell Biol. 129:473-487.
    • (1995) J. Cell Biol. , vol.129 , pp. 473-487
    • Spinardi, L.1    Einheber, S.2    Cullen, T.3    Milner, T.A.4    Giancotti, F.G.5
  • 72
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehelin, L.A. 1974. Structure and function of intercellular junctions. Int. Rev. Cytol. 39:191-278.
    • (1974) Int. Rev. Cytol. , vol.39 , pp. 191-278
    • Staehelin, L.A.1
  • 73
    • 0024272151 scopus 로고
    • Isolation of cDNA for bullous pemphigoid antigen by use of patients' autoantibodies
    • Stanley, J.R., T. Tanaka, S. Mueller, V. Klaus-Kovtun, and D. Roop. 1988. Isolation of cDNA for bullous pemphigoid antigen by use of patients' autoantibodies. J. Clin. Invest. 82:1864-1870.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1864-1870
    • Stanley, J.R.1    Tanaka, T.2    Mueller, S.3    Klaus-Kovtun, V.4    Roop, D.5
  • 74
    • 0029826757 scopus 로고    scopus 로고
    • Transition of human papillomavirus type 16 and 18 transfected human foreskin keratinocytes towards immortality: Activation of telomerase and allele losses at 3p, 10p, 11q and/or 18q
    • Steenbergen, R.D.M., J.M.M. Walboomers, C.J.L.M. Meijer, E.M.H. van der Raaij-Helmer, J.N. Parker, L.T. Chow, T.R. Broker, and P.J.F. Snijders. 1996. Transition of human papillomavirus type 16 and 18 transfected human foreskin keratinocytes towards immortality: activation of telomerase and allele losses at 3p, 10p, 11q and/or 18q. Oncogene. 13:1249-1257.
    • (1996) Oncogene , vol.13 , pp. 1249-1257
    • Steenbergen, R.D.M.1    Walboomers, J.M.M.2    Meijer, C.J.L.M.3    Van Der Raaij-Helmer, E.M.H.4    Parker, J.N.5    Chow, L.T.6    Broker, T.R.7    Snijders, P.J.F.8
  • 75
    • 0025020280 scopus 로고
    • Amino acid sequence of a novel integrin β4 subunit and primary expression of the mRNA in epithelial cells
    • Suzuki, S., and Y. Naitoh. 1990. Amino acid sequence of a novel integrin β4 subunit and primary expression of the mRNA in epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 9:757-763.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 757-763
    • Suzuki, S.1    Naitoh, Y.2
  • 80
    • 0003708810 scopus 로고
    • W. Knapp, B. Dörken, W.R. Gilks, E.P. Rieber, R.E. Schmidt, H. Stein, and A.E.G. Kr. von dem Borne, editors. Oxford University Press, New York
    • Von dem Borne, A.E.G. Kr., P.W. Modderman, L.G. Admiraal, H.K. Nieuwenhuis. 1989. In Leukocyte Typing IV. W. Knapp, B. Dörken, W.R. Gilks, E.P. Rieber, R.E. Schmidt, H. Stein, and A.E.G. Kr. von dem Borne, editors. Oxford University Press, New York. 951 pp.
    • (1989) Leukocyte Typing IV
    • Von Dem Borne, A.E.G.Kr.1    Modderman, P.W.2    Admiraal, L.G.3    Nieuwenhuis, H.K.4
  • 81
    • 0023555151 scopus 로고
    • Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cell possessing unique α and common β subunits
    • Wayner, E.A., and W.G. Carter. 1987. Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cell possessing unique α and common β subunits. J. Cell Biol. 105:1873-1884.
    • (1987) J. Cell Biol. , vol.105 , pp. 1873-1884
    • Wayner, E.A.1    Carter, W.G.2
  • 82
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., P.M. Tremble, O. Behrendtsen, E. Crowley, and C.H. Damsky. 1989. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109:877-889.
    • (1989) J. Cell Biol. , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 83
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three domain structure based on a central α-helical coiled-coil
    • Wiche, G., B. Becker, K. Luber, G. Weitzer, M.J. Castanon, R. Hauptmann, C. Stratowa, and M. Stewart. 1991. Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three domain structure based on a central α-helical coiled-coil. J. Cell Biol. 114:83-99.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castanon, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 84
    • 0021947315 scopus 로고
    • A 300,000 mol-wt intermediate filament-associated protein in baby hamster kidney (BHK-21) cells
    • Yang, H.-Y., N. Lieska, A.E. Goldman, and R.D. Goldman. 1985. A 300,000 mol-wt intermediate filament-associated protein in baby hamster kidney (BHK-21) cells. J. Cell Biol. 100:620-631.
    • (1985) J. Cell Biol. , vol.100 , pp. 620-631
    • Yang, H.-Y.1    Lieska, N.2    Goldman, A.E.3    Goldman, R.D.4
  • 85
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • Yang, Y.M., J. Dowling, Q.C. Yu, P. Kouklis, D.W. Cleveland, and E. Fuchs. 1996. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. Cell. 86:655-665.
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.M.1    Dowling, J.2    Yu, Q.C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6


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