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Volumn 26, Issue 8, 2006, Pages 2877-2886

Multiple functions of the integrin α6β4 in epidermal homeostasis and tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA6BETA4 INTEGRIN; PLECTIN;

EID: 33645837225     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.26.8.2877-2886.2006     Document Type: Short Survey
Times cited : (111)

References (102)
  • 1
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andra, K., H. Lassmann, R. Bittner, S. Shorny, R. Fassler, 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
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassler, R.5    Propst, F.6    Wiche, G.7
  • 2
    • 0033615961 scopus 로고    scopus 로고
    • p53 inhibits α6β4 integrin survival signaling by promoting the caspase 3-dependent cleavage of AKT/PKB
    • Bachelder, R. E., M. J. Ribick, A. Marchetti, R. Falcioni, S. Soddu, K. R. Davis, and A. M. Mercurio. 1999. p53 inhibits α6β4 integrin survival signaling by promoting the caspase 3-dependent cleavage of AKT/PKB. J. Cell Biol. 147:1063-1072.
    • (1999) J. Cell Biol. , vol.147 , pp. 1063-1072
    • Bachelder, R.E.1    Ribick, M.J.2    Marchetti, A.3    Falcioni, R.4    Soddu, S.5    Davis, K.R.6    Mercurio, A.M.7
  • 3
    • 28244478626 scopus 로고    scopus 로고
    • β4 integrin is a transforming molecule that unleashes Met tyrosine kinase tumorigenesis
    • Bertotti, A., P. M. Comoglio, and L. Trusolino. 2005. β4 integrin is a transforming molecule that unleashes Met tyrosine kinase tumorigenesis. Cancer Res. 65:10674-10679.
    • (2005) Cancer Res. , vol.65 , pp. 10674-10679
    • Bertotti, A.1    Comoglio, P.M.2    Trusolino, L.3
  • 4
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes
    • Carter, W. G., M. C. Ryan, and P. J. Gahr. 1991. Epiligrin, a new cell adhesion ligand for integrin 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
  • 5
    • 23744484146 scopus 로고    scopus 로고
    • Integrin α6β4 promotes expression of autotaxin/ENPP2 autocrine motility factor in breast carcinoma cells
    • Chen, M., and K. L. O'Connor. 2005. Integrin α6β4 promotes expression of autotaxin/ENPP2 autocrine motility factor in breast carcinoma cells. Oncogene 24:5125-5130.
    • (2005) Oncogene , vol.24 , pp. 5125-5130
    • Chen, M.1    O'Connor, K.L.2
  • 6
    • 4444361792 scopus 로고    scopus 로고
    • Integrin α3β1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1
    • Choma, D. P., K. Pumiglia, and C. M. DiPersio. 2004. Integrin α3β1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1. J. Cell Sci. 117:3947-3959.
    • (2004) J. Cell Sci. , vol.117 , pp. 3947-3959
    • Choma, D.P.1    Pumiglia, K.2    DiPersio, C.M.3
  • 7
    • 0037043329 scopus 로고    scopus 로고
    • Integrin α6β4 regulation of eIF-4E activity and VEGF translation: A survival mechanism for carcinoma cells
    • Chung, J., R. E. Bachelder, E. A. Lipscomb, L. M. Shaw, and A. M. Mercurio. 2002. Integrin α6β4 regulation of eIF-4E activity and VEGF translation: a survival mechanism for carcinoma cells. J. Cell Biol. 158:165-174.
    • (2002) J. Cell Biol. , vol.158 , pp. 165-174
    • Chung, J.1    Bachelder, R.E.2    Lipscomb, E.A.3    Shaw, L.M.4    Mercurio, A.M.5
  • 8
    • 3543011958 scopus 로고    scopus 로고
    • The Met receptor and α6β4 integrin can function independently to promote carcinoma invasion
    • Chung, J., S. O. Yoon, E. A. Lipscomb, and A. M. Mercurio. 2004. The Met receptor and α6β4 integrin can function independently to promote carcinoma invasion. J. Biol. Chem. 279:32287-32293.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32287-32293
    • Chung, J.1    Yoon, S.O.2    Lipscomb, E.A.3    Mercurio, A.M.4
  • 9
    • 0029092648 scopus 로고
    • Activation of the p21 pathway of growth arrest and apoptosis by the β4 integrin cytoplasmic domain
    • Clarke, A. S., M. M. Lotz, C. Chao, and A. M. Mercurio. 1995. Activation of the p21 pathway of growth arrest and apoptosis by the β4 integrin cytoplasmic domain. J. Biol. Chem. 270:22673-22676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22673-22676
    • Clarke, A.S.1    Lotz, M.M.2    Chao, C.3    Mercurio, A.M.4
  • 11
    • 0035847016 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates She signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes
    • Dans, M., L. Gagnoux-Palacios, P. Blaikie, S. Klein, A. Mariotti, and F. G. Giancotti. 2001. Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates She signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes. J. Biol. Chem. 276:1494-1502.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1494-1502
    • Dans, M.1    Gagnoux-Palacios, L.2    Blaikie, P.3    Klein, S.4    Mariotti, A.5    Giancotti, F.G.6
  • 12
    • 0035137742 scopus 로고    scopus 로고
    • Unique expression pattern of the α6β4 integrin and laminin-5 in human prostate carcinoma
    • Davis, T. L., A. E. Cress, B. L. Dalkin, and R. B. Nagle. 2001. Unique expression pattern of the α6β4 integrin and laminin-5 in human prostate carcinoma. Prostate 46:240-248.
    • (2001) Prostate , vol.46 , pp. 240-248
    • Davis, T.L.1    Cress, A.E.2    Dalkin, B.L.3    Nagle, R.B.4
  • 13
    • 0033828682 scopus 로고    scopus 로고
    • α3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development
    • DiPersio, C. M., R. van der Neut, E. Georges-Labouesse, J. A. Kreidberg, A. Sonnenberg, and R. O. Hynes. 2000. α3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development. J. Cell Sci. 113:3051-3062.
    • (2000) J. Cell Sci. , vol.113 , pp. 3051-3062
    • DiPersio, C.M.1    Van Der Neut, R.2    Georges-Labouesse, E.3    Kreidberg, J.A.4    Sonnenberg, A.5    Hynes, R.O.6
  • 14
    • 0029666420 scopus 로고    scopus 로고
    • Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling, J., Q. C. Yu, and E. Fuchs. 1996. Beta4 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
    • 0022976007 scopus 로고
    • Expression of tumor antigen correlated with metastatic potential of Lewis lung carcinoma and B16 melanoma clones in mice
    • Falcioni, R., S. J. Kennel, P. Giacomini, G. Zupi, and A. Sacchi. 1986. Expression of tumor antigen correlated with metastatic potential of Lewis lung carcinoma and B16 melanoma clones in mice. Cancer Res. 46:5772-5778.
    • (1986) Cancer Res. , vol.46 , pp. 5772-5778
    • Falcioni, R.1    Kennel, S.J.2    Giacomini, P.3    Zupi, G.4    Sacchi, A.5
  • 16
    • 0035980013 scopus 로고    scopus 로고
    • The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin β4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression
    • Favre, B., L. Fontao, J. Koster, R. Shafaatian, F. Jaunin, J. H. Saurat, A. Sonnenberg, and L. Borradori. 2001. The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin β4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression. J. Biol. Chem. 276:32427-32436.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32427-32436
    • Favre, B.1    Fontao, L.2    Koster, J.3    Shafaatian, R.4    Jaunin, F.5    Saurat, J.H.6    Sonnenberg, A.7    Borradori, L.8
  • 17
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao, L., D. Geerts, I. Kuikman, J. Koster, D. Kramer, and A. Sonnenberg. 2001. The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114:2065-2076.
    • (2001) J. Cell Sci. , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 18
    • 1642452817 scopus 로고    scopus 로고
    • Molecular consequences of deletion of the cytoplasmic domain of bullous pemphigoid 180 in a patient with predominant features of epidermolysis bullosa simplex
    • Fontao, L., K. Tasanen, M. Huber, D. Hohl, J. Koster, L. Bruckner-Tuderman, A. Sonnenberg, and L. Borradori. 2004. Molecular consequences of deletion of the cytoplasmic domain of bullous pemphigoid 180 in a patient with predominant features of epidermolysis bullosa simplex. J. Investig. Dermatol. 122:65-72.
    • (2004) J. Investig. Dermatol. , vol.122 , pp. 65-72
    • Fontao, L.1    Tasanen, K.2    Huber, M.3    Hohl, D.4    Koster, J.5    Bruckner-Tuderman, L.6    Sonnenberg, A.7    Borradori, L.8
  • 19
    • 2342431917 scopus 로고    scopus 로고
    • Laminin 5 deposition regulates keratinocyte polarization and persistent migration
    • Frank, D. E., and W. G. Carter. 2004. Laminin 5 deposition regulates keratinocyte polarization and persistent migration. J. Cell Sci. 117:1351-1363.
    • (2004) J. Cell Sci. , vol.117 , pp. 1351-1363
    • Frank, D.E.1    Carter, W.G.2
  • 22
    • 0034615933 scopus 로고    scopus 로고
    • Cooperative signaling between α6β4 integrin and ErbB-2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion
    • Gambaletta, D., A. Marchetti, L. Benedetti, A. M. Mercurio, A. Sacchi, and R. Falcioni. 2000. Cooperative signaling between α6β4 integrin and ErbB-2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion. J. Biol. Chem. 275:10604-10610.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10604-10610
    • Gambaletta, D.1    Marchetti, A.2    Benedetti, L.3    Mercurio, A.M.4    Sacchi, A.5    Falcioni, R.6
  • 23
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin α6β4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts, D., L. Fontao, M. G. Nievers, R. Q. Schaapveld, P. E. Purkis, G. N. Wheeler, E. B. Lane, I. M. Leigh, and A. Sonnenberg. 1999. Binding of integrin α6β4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147:417-434.
    • (1999) J. Cell Biol. , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 24
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the α6β4 integrin in keratinocytes
    • Geuijen, C. A., and A. Sonnenberg. 2002. Dynamics of the α6β4 integrin in keratinocytes. Mol. Biol. Cell 13:3845-3858.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 25
    • 0032841440 scopus 로고    scopus 로고
    • The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger, L. E., S. B. Hopkinson, G. W. deHart, S. Collawn, J. R. Couchman, and J. C. Jones. 1999. The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J. Cell Sci. 112:2615-2629.
    • (1999) J. Cell Sci. , vol.112 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    Dehart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.6
  • 26
    • 0026801111 scopus 로고
    • Expression of α6β4 integrin increases during malignant conversion of mouse epidermal keratinocytes: Association of β4 subunit to the cytokeratin fraction
    • Gomez, M., P. Navarro, M. Quintanilla, and A. Cano. 1992. Expression of α6β4 integrin increases during malignant conversion of mouse epidermal keratinocytes: association of β4 subunit to the cytokeratin fraction. Exp. Cell Res. 201:250-261.
    • (1992) Exp. Cell Res. , vol.201 , pp. 250-261
    • Gomez, M.1    Navarro, P.2    Quintanilla, M.3    Cano, A.4
  • 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. Wollmann, B. 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    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 29
    • 0024539022 scopus 로고
    • Association of the VLA α6 subunit with a novel protein. A possible alternative to the common VLA β1 subunit on certain cell lines
    • Hemler, M. E., C. Crouse, and A. Sonnenberg. 1989. Association of the VLA α6 subunit with a novel protein. A possible alternative to the common VLA β1 subunit on certain cell lines. J. Biol. Chem. 264:6529-6535.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6529-6535
    • Hemler, M.E.1    Crouse, C.2    Sonnenberg, A.3
  • 30
    • 0024278668 scopus 로고
    • Multiple very late antigen (VLA) heterodimers on platelets. Evidence for distinct VLA-2, VLA-5 (fibronectin receptor), and VLA-6 structures
    • Hemler, M. E., C. Crouse, Y. Takada, and A. Sonnenberg. 1988. Multiple very late antigen (VLA) heterodimers on platelets. Evidence for distinct VLA-2, VLA-5 (fibronectin receptor), and VLA-6 structures. J. Biol. Chem. 263:7660-7665.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7660-7665
    • Hemler, M.E.1    Crouse, C.2    Takada, Y.3    Sonnenberg, A.4
  • 31
    • 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. 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 J. 9:765-770.
    • (1990) EMBO J. , vol.9 , pp. 765-770
    • Hogervorst, F.1    Kuikman, I.2    Von Dem Borne, A.E.3    Sonnenberg, A.4
  • 32
    • 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. 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.3
  • 33
    • 0032447962 scopus 로고    scopus 로고
    • Interaction of BP180 (type XVII collagen) and α6 integrin is necessary for stabilization of hemidesmosome structure
    • Hopkinson, S. B., K. Findlay, G. W. deHart, and J. C. Jones. 1998. Interaction of BP180 (type XVII collagen) and α6 integrin is necessary for stabilization of hemidesmosome structure. J. Investig. Dermatol. 111:1015-1022.
    • (1998) J. Investig. Dermatol. , vol.111 , pp. 1015-1022
    • Hopkinson, S.B.1    Findlay, K.2    Dehart, G.W.3    Jones, J.C.4
  • 34
    • 0026176844 scopus 로고
    • A function for the integrin α6β4 in the hemidesmosome
    • Jones, J. C., M. A. Kurpakus, H. M. Cooper, and V. Quaranta. 1991. A function for the integrin α6β4 in the hemidesmosome. Cell Regul. 2:427-438.
    • (1991) Cell Regul. , vol.2 , pp. 427-438
    • Jones, J.C.1    Kurpakus, M.A.2    Cooper, H.M.3    Quaranta, V.4
  • 35
    • 0036911668 scopus 로고    scopus 로고
    • Deletion of a cytoplasmic domain of integrin β4 causes epidermolysis bullosa simplex
    • Jonkman, M. F., H. H. Pas, M. Nijenhuis, G. Kloosterhuis, and G. Steege. 2002. Deletion of a cytoplasmic domain of integrin β4 causes epidermolysis bullosa simplex. J. Investig. Dermatol. 119:1275-1281.
    • (2002) J. Investig. Dermatol. , vol.119 , pp. 1275-1281
    • Jonkman, M.F.1    Pas, H.H.2    Nijenhuis, M.3    Kloosterhuis, G.4    Steege, G.5
  • 36
    • 0024430105 scopus 로고
    • A novel integrin (αEβ4) from human epithelial cells suggests a fourth family of integrin adhesion receptors
    • Kajiji, S., R. N. Tamura, and V. Quaranta. 1989. A novel integrin (αEβ4) from human epithelial cells suggests a fourth family of integrin adhesion receptors. EMBO J. 8:673-680.
    • (1989) EMBO J. , vol.8 , pp. 673-680
    • Kajiji, S.1    Tamura, R.N.2    Quaranta, V.3
  • 37
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • Karamatic Crew, V., N. Burton, A. Kagan, C. A. Green, C. Levene, F. Flinter, R. L. Brady, G. Daniels, and D. J. Anstee. 2004. CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 104:2217-2223.
    • (2004) Blood , vol.104 , pp. 2217-2223
    • Karamatic Crew, V.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6    Brady, R.L.7    Daniels, G.8    Anstee, D.J.9
  • 38
    • 6044263512 scopus 로고    scopus 로고
    • Identification and characterization of human LLGL4 gene and mouse Llg14 gene in silico
    • Katoh, M. 2004. Identification and characterization of human LLGL4 gene and mouse Llg14 gene in silico. Int. J. Oncol. 24:737-742.
    • (2004) Int. J. Oncol. , vol.24 , pp. 737-742
    • Katoh, M.1
  • 40
    • 0037439896 scopus 로고    scopus 로고
    • Analysis of the interactions between BP180, BP230, plectin and the integrin α6β4 important for hemidesmosome assembly
    • Koster, J., D. Geerts, B. Favre, L. Borradori, and A. Sonnenberg. 2003. Analysis of the interactions between BP180, BP230, plectin and the integrin α6β4 important for hemidesmosome assembly. J. Cell Sci. 116:387-399.
    • (2003) J. Cell Sci. , vol.116 , pp. 387-399
    • Koster, J.1    Geerts, D.2    Favre, B.3    Borradori, L.4    Sonnenberg, A.5
  • 41
    • 0035670672 scopus 로고    scopus 로고
    • Two different mutations in the cytoplasmic domain of the iritegrin β4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of β4 with plectin
    • Koster, J., I. Kuikman, M. Kreft, and A. Sonnenberg. 2001. Two different mutations in the cytoplasmic domain of the iritegrin β4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of β4 with plectin. J. Investig. Dermatol. 117:1405-1411.
    • (2001) J. Investig. Dermatol. , vol.117 , pp. 1405-1411
    • Koster, J.1    Kuikman, I.2    Kreft, M.3    Sonnenberg, A.4
  • 42
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes
    • Koster, J., S. van Wilpe, I. Kuikman, S. H. Litjens, and A. Sonnenberg. 2004. Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes. Mol. Biol. Cell 15:1211-1223.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    Van Wilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 43
    • 28244470818 scopus 로고    scopus 로고
    • The α6β4 integrin maintains the survival of human breast carcinoma cells in vivo
    • Lipscomb, E. A., K. J. Simpson, S. R. Lyle, J. E. Ring, A. S. Dugan, and A. M. Mercurio. 2005. The α6β4 integrin maintains the survival of human breast carcinoma cells in vivo. Cancer Res. 65:10970-10976.
    • (2005) Cancer Res. , vol.65 , pp. 10970-10976
    • Lipscomb, E.A.1    Simpson, K.J.2    Lyle, S.R.3    Ring, J.E.4    Dugan, A.S.5    Mercurio, A.M.6
  • 45
    • 0242391992 scopus 로고    scopus 로고
    • p38 MAPK is a critical regulator of the constitutive and the β4 integrin-regulated expression of IL-6 in human normal thymic epithelial cells
    • Mainiero, F., M. Colombara, V. Antonini, R. Strippoli, M. Merola, O. Poffe, G. Tridente, and D. Ramarli. 2003. p38 MAPK is a critical regulator of the constitutive and the β4 integrin-regulated expression of IL-6 in human normal thymic epithelial cells. Eur. J. Immunol. 33:3038-3048.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 3038-3048
    • Mainiero, F.1    Colombara, M.2    Antonini, V.3    Strippoli, R.4    Merola, M.5    Poffe, O.6    Tridente, G.7    Ramarli, D.8
  • 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 J. 14:4470-4481.
    • (1995) EMBO 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
    • 0029666451 scopus 로고    scopus 로고
    • The intracellular functions of α6β4 integrin are regulated by EGF
    • Mainiero, F., A. Pepe, M. Yeon, Y. Ren, and F. G. Giancotti. 1996. The intracellular functions of α6β4 integrin are regulated by EGF. J. Cell Biol. 134:241-253.
    • (1996) J. Cell Biol. , vol.134 , pp. 241-253
    • Mainiero, F.1    Pepe, A.2    Yeon, M.3    Ren, Y.4    Giancotti, F.G.5
  • 49
    • 0035851913 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion
    • Mariotti, A., P. A. Kedeshian, M. Dans, A. M. Curatola, L. Gagnoux-Palacios, and F. G. Giancotti. 2001. EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: role in epithelial cell migration and carcinoma invasion. J. Cell Biol. 155:447-458.
    • (2001) J. Cell Biol. , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 51
    • 0035019920 scopus 로고    scopus 로고
    • Towards a mechanistic understanding of tumor invasion-lessons from the α6β4 integrin
    • Mercurio, A. M., and I. Rabinovitz. 2001. Towards a mechanistic understanding of tumor invasion-lessons from the α6β4 integrin. Semin. Cancer Biol. 11:129-141.
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 129-141
    • Mercurio, A.M.1    Rabinovitz, I.2
  • 52
    • 0042887042 scopus 로고    scopus 로고
    • The emerging role of lysophosphatidic acid in cancer
    • Mills, G. B., and W. H. Moolenaar. 2003. The emerging role of lysophosphatidic acid in cancer. Nat. Rev. Cancer 3:582-591.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 582-591
    • Mills, G.B.1    Moolenaar, W.H.2
  • 53
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • Murgia, C., P. Blaikie, N. Kim, M. Dans, H. T. Petrie, and F. G. Giancotti. 1998. Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain. EMBO J. 17:3940-3951.
    • (1998) EMBO J. , vol.17 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6
  • 54
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • Musch, A., D. Cohen, C. Yeaman, W. J. Nelson, E. Rodriguez-Boulan, and P. J. Brennwald. 2002. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol. Biol. Cell 13:158-168.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 158-168
    • Musch, A.1    Cohen, D.2    Yeaman, C.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 55
  • 56
    • 0035941357 scopus 로고    scopus 로고
    • Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen
    • Nguyen, B. P., X. D. Ren, M. A. Schwartz, and W. G. Carter. 2001. Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen. J. Biol. Chem. 276:43860-43870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43860-43870
    • Nguyen, B.P.1    Ren, X.D.2    Schwartz, M.A.3    Carter, W.G.4
  • 58
    • 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. Hulsman, E. S. Rots, P. Sanchez-Aparicio, and A. Sonnenberg. 1997. 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.2    Rots, E.S.3    Sanchez-Aparicio, P.4    Sonnenberg, A.5
  • 59
    • 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., M. H. van der Raaij-Helmer, E. H. 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, M.H.2    Hulsman, E.H.3    Van Der Neut, R.4    Jonkman, M.F.5    Sonnenberg, A.6
  • 60
    • 0031848143 scopus 로고    scopus 로고
    • Ligand-independent role of the β4 integrin subunit in the formation of hemidesmosomes
    • Nievers, M. G., R. Q. Schaapveld, L. C. Oomen, L. Fontao, D. Geerts, and A. Sonnenberg. 1998. Ligand-independent role of the β4 integrin subunit in the formation of hemidesmosomes. J. Cell Sci. 111:1659-1672.
    • (1998) J. Cell Sci. , vol.111 , pp. 1659-1672
    • Nievers, M.G.1    Schaapveld, R.Q.2    Oomen, L.C.3    Fontao, L.4    Geerts, D.5    Sonnenberg, A.6
  • 62
    • 21744455891 scopus 로고    scopus 로고
    • Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, causing defects in epidermal growth and migration
    • Nikolopoulos, S. N., P. Blaikie, T. Yoshioka, W. Guo, C. Puri, C. Tacchetti, and F. G. Giancotti. 2005. Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, causing defects in epidermal growth and migration. Mol. Cell. Biol. 25:6090-6102.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6090-6102
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Puri, C.5    Tacchetti, C.6    Giancotti, F.G.7
  • 63
    • 0023864876 scopus 로고
    • Platelet glycoproteins Ia, Ic, and IIa are physicochemicaiiy indistinguishable from the very late activation antigens adhesion-related proteins of lymphocytes and other cell types
    • Pischel, K. D., H. G. Bluestein, and V. L. Woods, Jr. 1988. Platelet glycoproteins Ia, Ic, and IIa are physicochemicaiiy indistinguishable from the very late activation antigens adhesion-related proteins of lymphocytes and other cell types. J. Clin. Investig. 81:505-513.
    • (1988) J. Clin. Investig. , vol.81 , pp. 505-513
    • Pischel, K.D.1    Bluestein, H.G.2    Woods Jr., V.L.3
  • 65
    • 0029798270 scopus 로고    scopus 로고
    • Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy
    • Pulkkinen, L., F. J. Smith, H. Shimizu, S. Murata, H. Yaoita, H. Hachisuka, T. Nishikawa, W. H. McLean, and J. Uitto. 1996. Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. Hum. Mol. Genet. 5:1539-1546.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1539-1546
    • Pulkkinen, L.1    Smith, F.J.2    Shimizu, H.3    Murata, S.4    Yaoita, H.5    Hachisuka, H.6    Nishikawa, T.7    McLean, W.H.8    Uitto, J.9
  • 66
    • 0032845770 scopus 로고    scopus 로고
    • Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells
    • Rabinovitz, I., A. Toker, and A. M. Mercurio. 1999. Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells. J. Cell Biol. 146:1147-1160.
    • (1999) J. Cell Biol. , vol.146 , pp. 1147-1160
    • Rabinovitz, I.1    Toker, A.2    Mercurio, A.M.3
  • 67
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase C-α phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes
    • Rabinovitz, I., L. Tsomo, and A. M. Mercurio. 2004. Protein kinase C-α phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes. Mol. Cell. Biol. 24:4351-4360.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 68
    • 0032533242 scopus 로고    scopus 로고
    • Thymocyte contact or monoclonal antibody-mediated clustering of α3β1 or α6β4 integrins activate interleukin-6 (IL-6) transcription factors (NF-κB and NF-IL6) and IL-6 production in human thymic epithelial cells
    • Ramarli, D., M. T. Scupoli, E. Fiorini, O. Poffe, M. Brentegani, A. Villa, G. Cecchini, G. Tridente, and P. C. Marchisio. 1998. Thymocyte contact or monoclonal antibody-mediated clustering of α3β1 or α6β4 integrins activate interleukin-6 (IL-6) transcription factors (NF-κB and NF-IL6) and IL-6 production in human thymic epithelial cells. Blood 92:3745-3755.
    • (1998) Blood , vol.92 , pp. 3745-3755
    • Ramarli, D.1    Scupoli, M.T.2    Fiorini, E.3    Poffe, O.4    Brentegani, M.5    Villa, A.6    Cecchini, G.7    Tridente, G.8    Marchisio, P.C.9
  • 69
    • 16844373398 scopus 로고    scopus 로고
    • Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice
    • Raymond, K., M. Kreft, H. Janssen, J. Calafat, and A. Sonnenberg. 2005. Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice. J. Cell Sci. 118:1045-1060.
    • (2005) J. Cell Sci. , vol.118 , pp. 1045-1060
    • Raymond, K.1    Kreft, M.2    Janssen, H.3    Calafat, J.4    Sonnenberg, A.5
  • 70
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple molecular sites
    • Rezniczek, G. A., J. M. de Pereda, S. Reipert, and G. Wiche. 1998. Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the β4 subunit and plectin at multiple molecular sites. J. Cell Biol. 141:209-225.
    • (1998) J. Cell Biol. , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    De Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 71
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle, P., G. P. Lunstrum, 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    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 73
    • 0032230322 scopus 로고    scopus 로고
    • She phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells
    • Sakaguchi, K., Y. Okabayashi, Y. Kido, S. Kimura, Y. Matsumura, K. Inushima, and M. Kasuga. 1998. She phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. Mol. Endocrinol. 12:536-543.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 536-543
    • Sakaguchi, K.1    Okabayashi, Y.2    Kido, Y.3    Kimura, S.4    Matsumura, Y.5    Inushima, K.6    Kasuga, M.7
  • 74
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro, M. M., G. Gaudino, and P. C. Marchisio. 2003. The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration. Dev. Cell 5:257-271.
    • (2003) Dev. Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3
  • 75
    • 0032514156 scopus 로고    scopus 로고
    • 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
    • Schaapveld, R. Q., L. Borradori, D. Geerts, M. R. van Leusden, I. Kuikman. M. G. Nievers, C. M. Niessen, R. D. Steenbergen, P. J. Snijders, and A. Sonnenberg. 1998. 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. J. Cell Biol. 142:271-284.
    • (1998) J. Cell Biol. , vol.142 , pp. 271-284
    • Schaapveld, R.Q.1    Borradori, L.2    Geerts, D.3    Van Leusden, M.R.4    Kuikman, I.5    Nievers, M.G.6    Niessen, C.M.7    Steenbergen, R.D.8    Snijders, P.J.9    Sonnenberg, A.10
  • 76
    • 0034764209 scopus 로고    scopus 로고
    • Pemphigoid nodularis associated with autoantibodies to the NC16A domain of BP180 and a hyperproliferative integrin profile
    • Schachter, M., J. C. Brieva, J. C. Jones, D. Zillikens, C. Skrobek, and L. S. Chan. 2001. Pemphigoid nodularis associated with autoantibodies to the NC16A domain of BP180 and a hyperproliferative integrin profile. J. Am. Acad. Dermatol. 45:747-754.
    • (2001) J. Am. Acad. Dermatol. , vol.45 , pp. 747-754
    • Schachter, M.1    Brieva, J.C.2    Jones, J.C.3    Zillikens, D.4    Skrobek, C.5    Chan, L.S.6
  • 77
    • 0030955318 scopus 로고    scopus 로고
    • Calx, a Na-Ca exchanger gene of Drosophila melanogaster
    • Schwarz, E. M., and S. Benzer. 1997. Calx, a Na-Ca exchanger gene of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 94:10249-10254.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10249-10254
    • Schwarz, E.M.1    Benzer, S.2
  • 78
    • 0033624673 scopus 로고    scopus 로고
    • Nuclear factor κB subunits induce epithelial cell growth arrest
    • Seitz, C. S., H. Deng, K. Hinata, Q. Lin, and P. A. Khavari. 2000. Nuclear factor κB subunits induce epithelial cell growth arrest. Cancer Res. 60:4085-4092.
    • (2000) Cancer Res. , vol.60 , pp. 4085-4092
    • Seitz, C.S.1    Deng, H.2    Hinata, K.3    Lin, Q.4    Khavari, P.A.5
  • 79
    • 0032477945 scopus 로고    scopus 로고
    • Alterations in NF-κB function in transgenic epithelial tissue demonstrate a growth inhibitory role for NF-κB
    • Seitz, C. S., Q. Lin, H. Deng, and P. A. Khavari. 1998. Alterations in NF-κB function in transgenic epithelial tissue demonstrate a growth inhibitory role for NF-κB. Proc. Natl. Acad. Sci. USA 95:2307-2312.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2307-2312
    • Seitz, C.S.1    Lin, Q.2    Deng, H.3    Khavari, P.A.4
  • 80
    • 0034951677 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion
    • Shaw, L. M. 2001. Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion. Mol. Cell. Biol. 21:5082-5093.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5082-5093
    • Shaw, L.M.1
  • 81
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion
    • Shaw, L. M., I. Rabinovitz, H. H. Wang, A. Toker, and A. M. Mercurio. 1997. Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion. Cell 91:949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.3    Toker, A.4    Mercurio, A.M.5
  • 83
    • 23844484860 scopus 로고    scopus 로고
    • Zebrafish penner/lethal giant larvae 2 functions in hemidesmosome formation, maintenance of cellular morphology and growth regulation in the developing basal epidermis
    • Sonawane, M., Y. Carpio, R. Geisler, H. Schwarz, H. M. Maischein, and C. Nuesslein-Volhard. 2005. Zebrafish penner/lethal giant larvae 2 functions in hemidesmosome formation, maintenance of cellular morphology and growth regulation in the developing basal epidermis. Development 132:3255-3265.
    • (2005) Development , vol.132 , pp. 3255-3265
    • Sonawane, M.1    Carpio, Y.2    Geisler, R.3    Schwarz, H.4    Maischein, H.M.5    Nuesslein-Volhard, C.6
  • 85
    • 0023771015 scopus 로고
    • Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic
    • Sonnenberg, A., F. Hogervorst, A. Osterop, and F. E. Veltman. 1988. Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic. J. Biol. Chem. 263:14030-14038.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14030-14038
    • Sonnenberg, A.1    Hogervorst, F.2    Osterop, A.3    Veltman, F.E.4
  • 86
    • 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
  • 88
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes
    • Sterk, L. M., C. A. Geuijen, L. C. Oomen, J. Calafat, H. Janssen, and A. Sonnenberg. 2000. The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes. J. Cell Biol. 149:969-982.
    • (2000) J. Cell Biol. , vol.149 , pp. 969-982
    • Sterk, L.M.1    Geuijen, C.A.2    Oomen, L.C.3    Calafat, J.4    Janssen, H.5    Sonnenberg, A.6
  • 89
    • 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 J. 9:757-763.
    • (1990) EMBO J. , vol.9 , pp. 757-763
    • Suzuki, S.1    Naitoh, Y.2
  • 90
    • 0037903293 scopus 로고    scopus 로고
    • Expression of NF-κB in epidermis and the relationship between NF-κB activation and inhibition of keratinocyte growth
    • Takao, J., T. Yudate, A. Das, S. Shikano, M. Bonkobara, K. Ariizumi, and P. D. Cruz. 2003. Expression of NF-κB in epidermis and the relationship between NF-κB activation and inhibition of keratinocyte growth. Br. J. Dermatol. 148:680-688.
    • (2003) Br. J. Dermatol. , vol.148 , pp. 680-688
    • Takao, J.1    Yudate, T.2    Das, A.3    Shikano, S.4    Bonkobara, M.5    Ariizumi, K.6    Cruz, P.D.7
  • 91
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth
    • Trusolino, L., A. Bertotti, and P. M. Comoglio. 2001. A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth. Cell 107:643-654.
    • (2001) Cell , vol.107 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 92
  • 93
    • 0025911170 scopus 로고
    • The A9 antigen associated with aggressive human squamous carcinoma is structurally and functionally similar to the newly defined integrin α6β4
    • Van Waes, C., K. F. Kozarsky, A. B. Warren, L. Kidd, D. Paugh, M. Liebert, and T. E. Carey. 1991. The A9 antigen associated with aggressive human squamous carcinoma is structurally and functionally similar to the newly defined integrin α6β4. Cancer Res. 51:2395-2402.
    • (1991) Cancer Res. , vol.51 , pp. 2395-2402
    • Van Waes, C.1    Kozarsky, K.F.2    Warren, A.B.3    Kidd, L.4    Paugh, D.5    Liebert, M.6    Carey, T.E.7
  • 96
    • 0036726312 scopus 로고    scopus 로고
    • β4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium
    • Weaver, V. M., S. Lelievre, J. N. Lakins, M. A. Chrenek, J. C. Jones, F. Giancotti, Z. Werb, and M. J. Bissell. 2002. β4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium. Cancer Cell 2:205-216.
    • (2002) Cancer Cell , vol.2 , pp. 205-216
    • Weaver, V.M.1    Lelievre, S.2    Lakins, J.N.3    Chrenek, M.A.4    Jones, J.C.5    Giancotti, F.6    Werb, Z.7    Bissell, M.J.8
  • 100
    • 0035936556 scopus 로고    scopus 로고
    • Mitochondrial division: New partners in membrane pinching
    • Yoon, Y., and M. A. McNiven. 2001. Mitochondrial division: new partners in membrane pinching. Curr. Biol. 11:R67-R70.
    • (2001) Curr. Biol. , vol.11
    • Yoon, Y.1    McNiven, M.A.2
  • 101
    • 0347363470 scopus 로고    scopus 로고
    • Autocrine laminin-5 ligates α6β4 integrin and activates RAC and NF-κB to mediate anchorage-independent survival of mammary tumors
    • Zahir, N., J. N. Lakins, A. Russell, W. Ming, C. Chatterjee, G. I. Rozenberg, M. P. Marinkovich, and V. M. Weaver. 2003. Autocrine laminin-5 ligates α6β4 integrin and activates RAC and NF-κB to mediate anchorage-independent survival of mammary tumors. J. Cell Biol. 163:1397-1407.
    • (2003) J. Cell Biol. , vol.163 , pp. 1397-1407
    • Zahir, N.1    Lakins, J.N.2    Russell, A.3    Ming, W.4    Chatterjee, C.5    Rozenberg, G.I.6    Marinkovich, M.P.7    Weaver, V.M.8
  • 102
    • 0346497823 scopus 로고    scopus 로고
    • NF-κB RelA opposes epidermal proliferation driven by TNFR1 and JNK
    • Zhang, J. Y., C. L. Green, S. Tao, and P. A. Khavari. 2004. NF-κB RelA opposes epidermal proliferation driven by TNFR1 and JNK. Genes Dev. 18:17-22.
    • (2004) Genes Dev. , vol.18 , pp. 17-22
    • Zhang, J.Y.1    Green, C.L.2    Tao, S.3    Khavari, P.A.4


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