메뉴 건너뛰기




Volumn 62, Issue 1, 2011, Pages 1-7

Hemidesmosomes and focal contact proteins: Functions and cross-talk in keratinocytes, bullous diseases and wound healing

Author keywords

Bullous pemphigoid; Epidermolysis bullosa; Focal adhesion; Focal complex; Matrix adhesion; Wound repair

Indexed keywords

ALPHA6BETA4 INTEGRIN; BETA4 INTEGRIN; CD151 ANTIGEN; COFILIN; COLLAGEN TYPE 17; COLLAGENASE 3; FIBRONECTIN; FOCAL ADHESION KINASE; GELATINASE A; LAMININ; MACROPHAGE ELASTASE; MATRIX METALLOPROTEINASE 19; MATRIX METALLOPROTEINASE 20; MITOGEN ACTIVATED PROTEIN KINASE; PLASMIN; PLECTIN; PROCOLLAGEN C PROTEINASE; RAC PROTEIN; RAC1 PROTEIN; SERINE PROTEINASE; STROMELYSIN; VERY LATE ACTIVATION ANTIGEN 2; VERY LATE ACTIVATION ANTIGEN 3; VERY LATE ACTIVATION ANTIGEN 5;

EID: 79952705436     PISSN: 09231811     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jdermsci.2011.01.005     Document Type: Review
Times cited : (100)

References (66)
  • 1
  • 3
    • 0025248510 scopus 로고
    • The role of integrins alpha 2 beta 1 and alpha 3 beta 1 in cell-cell and cell-substrate adhesion of human epidermal cells
    • Carter W.G., Wayner E.A., Bouchard T.S., Kaur P. The role of integrins alpha 2 beta 1 and alpha 3 beta 1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 1990, 110:1387-1404.
    • (1990) J Cell Biol , vol.110 , pp. 1387-1404
    • Carter, W.G.1    Wayner, E.A.2    Bouchard, T.S.3    Kaur, P.4
  • 4
    • 0025679064 scopus 로고
    • Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes
    • Carter W.G., Kaur P., Gil S.G., Gahr P.J., Wayner E.A. Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J Cell Biol 1990, 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
  • 6
    • 0036615472 scopus 로고    scopus 로고
    • Microfilament-dependent movement of the beta3 integrin subunit within focal contacts of endothelial cells
    • Tsuruta D., Gonzales M., Hopkinson S.B., Otey C., Khuon S., Goldman R.D., et al. Microfilament-dependent movement of the beta3 integrin subunit within focal contacts of endothelial cells. FASEB.J 2002, 16:866-868.
    • (2002) FASEB.J , vol.16 , pp. 866-868
    • Tsuruta, D.1    Gonzales, M.2    Hopkinson, S.B.3    Otey, C.4    Khuon, S.5    Goldman, R.D.6
  • 7
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 8
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes
    • Sterk L.M., Geuijen C.A., Oomen L.C., Calafat J., Janssen H., Sonnenberg A. The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. J Cell Biol 2000, 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
  • 10
    • 0030610163 scopus 로고    scopus 로고
    • Alpha3beta1 Integrin is required for normal development of the epidermal basement membrane
    • DiPersio C.M., Hodivala-Dilke K.M., Jaenisch R., Kreidberg J.A., Hynes R.O. alpha3beta1 Integrin is required for normal development of the epidermal basement membrane. J Cell Biol 1997, 137:729-742.
    • (1997) J Cell Biol , vol.137 , pp. 729-742
    • DiPersio, C.M.1    Hodivala-Dilke, K.M.2    Jaenisch, R.3    Kreidberg, J.A.4    Hynes, R.O.5
  • 11
    • 0028978225 scopus 로고
    • Alpha 3A beta 1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins
    • DiPersio C.M., Shah S., Hynes R.O. alpha 3A beta 1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins. J Cell Sci 1995, 108(Pt 6):2321-2336.
    • (1995) J Cell Sci , vol.108 , Issue.PART 6 , pp. 2321-2336
    • DiPersio, C.M.1    Shah, S.2    Hynes, R.O.3
  • 12
    • 68149163950 scopus 로고    scopus 로고
    • Integrin-linked kinase: a multi-functional regulator modulating extracellular pressure-stimulated cancer cell adhesion through focal adhesion kinase and AKT
    • Wang S., Basson M.D. Integrin-linked kinase: a multi-functional regulator modulating extracellular pressure-stimulated cancer cell adhesion through focal adhesion kinase and AKT. Cell Oncol 2009, 31:273-289.
    • (2009) Cell Oncol , vol.31 , pp. 273-289
    • Wang, S.1    Basson, M.D.2
  • 14
    • 67449156351 scopus 로고    scopus 로고
    • BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities
    • Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C. BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities. Mol Biol Cell 2009, 20:2954-2962.
    • (2009) Mol Biol Cell , vol.20 , pp. 2954-2962
    • Hamill, K.J.1    Hopkinson, S.B.2    DeBiase, P.3    Jones, J.C.4
  • 15
    • 0032893678 scopus 로고    scopus 로고
    • A cell signal pathway involving laminin-5, alpha3beta1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation
    • Gonzales M., Haan K., Baker S.E., Fitchmun M., Todorov I., Weitzman S., et al. A cell signal pathway involving laminin-5, alpha3beta1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation. Mol Biol Cell 1999, 10:259-270.
    • (1999) Mol Biol Cell , vol.10 , pp. 259-270
    • Gonzales, M.1    Haan, K.2    Baker, S.E.3    Fitchmun, M.4    Todorov, I.5    Weitzman, S.6
  • 16
    • 15444367651 scopus 로고    scopus 로고
    • Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1
    • Zhou H., Kramer R.H. Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1. J Biol Chem 2005, 280:10624-10635.
    • (2005) J Biol Chem , vol.280 , pp. 10624-10635
    • Zhou, H.1    Kramer, R.H.2
  • 17
    • 33845736815 scopus 로고    scopus 로고
    • Integrin alpha3beta1-dependent activation of FAK/Src regulates Rac1-mediated keratinocyte polarization on laminin-5
    • Choma D.P., Milano V., Pumiglia K.M., DiPersio C.M. Integrin alpha3beta1-dependent activation of FAK/Src regulates Rac1-mediated keratinocyte polarization on laminin-5. J Invest Dermatol 2007, 127:31-40.
    • (2007) J Invest Dermatol , vol.127 , pp. 31-40
    • Choma, D.P.1    Milano, V.2    Pumiglia, K.M.3    DiPersio, C.M.4
  • 18
    • 1642457348 scopus 로고    scopus 로고
    • Myosin-mediated cytoskeleton contraction and Rho GTPases regulate laminin-5 matrix assembly
    • DeHart G.W., Jones J.C. Myosin-mediated cytoskeleton contraction and Rho GTPases regulate laminin-5 matrix assembly. Cell Motil Cytoskeleton 2004, 57:107-117.
    • (2004) Cell Motil Cytoskeleton , vol.57 , pp. 107-117
    • DeHart, G.W.1    Jones, J.C.2
  • 19
    • 28544437707 scopus 로고    scopus 로고
    • The Rac activator Tiam1 is required for (alpha)3(beta)1-mediated laminin-5 deposition, cell spreading, and cell migration
    • Hamelers I.H., Olivo C., Mertens A.E., Pegtel D.M., van der Kammen R.A., Sonnenberg A., et al. The Rac activator Tiam1 is required for (alpha)3(beta)1-mediated laminin-5 deposition, cell spreading, and cell migration. J Cell Biol 2005, 171:871-881.
    • (2005) J Cell Biol , vol.171 , pp. 871-881
    • Hamelers, I.H.1    Olivo, C.2    Mertens, A.E.3    Pegtel, D.M.4    van der Kammen, R.A.5    Sonnenberg, A.6
  • 20
    • 21544432425 scopus 로고    scopus 로고
    • The last but not the least: the origin and significance of trailing adhesions in fibroblastic cells
    • Rid R., Schiefermeier N., Grigoriev I., Small J.V., Kaverina I. The last but not the least: the origin and significance of trailing adhesions in fibroblastic cells. Cell Motil Cytoskeleton 2005, 61:161-171.
    • (2005) Cell Motil Cytoskeleton , vol.61 , pp. 161-171
    • Rid, R.1    Schiefermeier, N.2    Grigoriev, I.3    Small, J.V.4    Kaverina, I.5
  • 21
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the alpha6beta4 integrin in keratinocytes
    • Geuijen C.A., Sonnenberg A. Dynamics of the alpha6beta4 integrin in keratinocytes. Mol Biol Cell 2002, 13:3845-3858.
    • (2002) Mol Biol Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 22
    • 77952426752 scopus 로고    scopus 로고
    • Dynamic relationship of focal contacts and hemidesmosome protein complexes in live cells
    • Ozawa T., Tsuruta D., Jones J.C., Ishii M., Ikeda K., Harada T., et al. Dynamic relationship of focal contacts and hemidesmosome protein complexes in live cells. J Invest Dermatol 2010, 130:1624-1635.
    • (2010) J Invest Dermatol , vol.130 , pp. 1624-1635
    • Ozawa, T.1    Tsuruta, D.2    Jones, J.C.3    Ishii, M.4    Ikeda, K.5    Harada, T.6
  • 23
    • 43449084027 scopus 로고    scopus 로고
    • The classification of inherited epidermolysis bullosa (EB): Report of the Third International Consensus Meeting on Diagnosis and Classification of EB
    • Fine J.D., Eady R.A., Bauer E.A., Bauer J.W., Bruckner-Tuderman L., Heagerty A., et al. The classification of inherited epidermolysis bullosa (EB): Report of the Third International Consensus Meeting on Diagnosis and Classification of EB. J Am Acad Dermatol 2008, 58:931-950.
    • (2008) J Am Acad Dermatol , vol.58 , pp. 931-950
    • Fine, J.D.1    Eady, R.A.2    Bauer, E.A.3    Bauer, J.W.4    Bruckner-Tuderman, L.5    Heagerty, A.6
  • 24
    • 77952431203 scopus 로고    scopus 로고
    • A homozygous nonsense mutation within the dystonin gene coding for the coiled-coil domain of the epithelial isoform of BPAG1 underlies a new subtype of autosomal recessive epidermolysis bullosa simplex
    • Groves R.W., Liu L., Dopping-Hepenstal P.J., Markus H.S., Lovell P.A., Ozoemena L., et al. A homozygous nonsense mutation within the dystonin gene coding for the coiled-coil domain of the epithelial isoform of BPAG1 underlies a new subtype of autosomal recessive epidermolysis bullosa simplex. J Invest Dermatol 2010, 130:1551-1557.
    • (2010) J Invest Dermatol , vol.130 , pp. 1551-1557
    • Groves, R.W.1    Liu, L.2    Dopping-Hepenstal, P.J.3    Markus, H.S.4    Lovell, P.A.5    Ozoemena, L.6
  • 25
    • 0036911668 scopus 로고    scopus 로고
    • Deletion of a cytoplasmic domain of integrin beta4 causes epidermolysis bullosa simplex
    • Jonkman M.F., Pas H.H., Nijenhuis M., Kloosterhuis G., Steege G. Deletion of a cytoplasmic domain of integrin beta4 causes epidermolysis bullosa simplex. J Invest Dermatol 2002, 119:1275-1281.
    • (2002) J Invest Dermatol , vol.119 , pp. 1275-1281
    • Jonkman, M.F.1    Pas, H.H.2    Nijenhuis, M.3    Kloosterhuis, G.4    Steege, G.5
  • 26
    • 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., Burton N., Kagan A., Green C.A., Levene C., Flinter F., et al. 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 2004, 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
  • 27
    • 70450225550 scopus 로고    scopus 로고
    • Adhesion and migration, the diverse functions of the laminin alpha3 subunit
    • Hamill K.J., Paller A.S., Jones J.C. Adhesion and migration, the diverse functions of the laminin alpha3 subunit. Dermatol Clin 2010, 28:79-87.
    • (2010) Dermatol Clin , vol.28 , pp. 79-87
    • Hamill, K.J.1    Paller, A.S.2    Jones, J.C.3
  • 30
    • 77649181584 scopus 로고    scopus 로고
    • The role of kindlins in cell biology and relevance to human disease
    • Lai-Cheong J.E., Parsons M., McGrath J.A. The role of kindlins in cell biology and relevance to human disease. Int J Biochem Cell Biol 2010, 42:595-603.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 595-603
    • Lai-Cheong, J.E.1    Parsons, M.2    McGrath, J.A.3
  • 31
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: new members to the club of focal adhesion proteins
    • Meves A., Stremmel C., Gottschalk K., Fassler R. The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol 2009, 19:504-513.
    • (2009) Trends Cell Biol , vol.19 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fassler, R.4
  • 34
    • 85042610490 scopus 로고    scopus 로고
    • IgG from patients with bullous pemphigoid depletes cultured keratinocytes of the 180-kDa bullous pemphigoid antigen (type XVII collagen) and weakens cell attachment
    • Iwata H., Kamio N., Aoyama Y., Yamamoto Y., Hirako Y., Owaribe K., et al. IgG from patients with bullous pemphigoid depletes cultured keratinocytes of the 180-kDa bullous pemphigoid antigen (type XVII collagen) and weakens cell attachment. J Invest Dermatol 2009, 129:919-926.
    • (2009) J Invest Dermatol , vol.129 , pp. 919-926
    • Iwata, H.1    Kamio, N.2    Aoyama, Y.3    Yamamoto, Y.4    Hirako, Y.5    Owaribe, K.6
  • 35
    • 0032857374 scopus 로고    scopus 로고
    • Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell datachment induced by pemphigus IgG in cultured keratinocytes: involvement of protein kinase C
    • Kitajima Y., Aoyama Y., Seishima M. Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell datachment induced by pemphigus IgG in cultured keratinocytes: involvement of protein kinase C. J Investig Dermatol Symp Proc 1999, 4:137-144.
    • (1999) J Investig Dermatol Symp Proc , vol.4 , pp. 137-144
    • Kitajima, Y.1    Aoyama, Y.2    Seishima, M.3
  • 36
    • 0035995039 scopus 로고    scopus 로고
    • An antibody to BP 180kDa antigen is able to induce an increase of intracellular Ca2+ concentration in DJM-1 (human squamous cell carcinoma) cells
    • Suzuki M., Murata S., Yaoita H., Nakagawa H. An antibody to BP 180kDa antigen is able to induce an increase of intracellular Ca2+ concentration in DJM-1 (human squamous cell carcinoma) cells. Autoimmunity 2002, 35:271-276.
    • (2002) Autoimmunity , vol.35 , pp. 271-276
    • Suzuki, M.1    Murata, S.2    Yaoita, H.3    Nakagawa, H.4
  • 37
    • 0028273117 scopus 로고
    • A possible cell-biologic mechanism involved in blister formation of bullous pemphigoid: anti-180-kD BPA antibody is an initiator
    • Kitajima Y., Hirako Y., Owaribe K., Yaoita H. A possible cell-biologic mechanism involved in blister formation of bullous pemphigoid: anti-180-kD BPA antibody is an initiator. Dermatology 1994, 189(Suppl. 1):46-49.
    • (1994) Dermatology , vol.189 , Issue.SUPPL. 1 , pp. 46-49
    • Kitajima, Y.1    Hirako, Y.2    Owaribe, K.3    Yaoita, H.4
  • 38
    • 0026459877 scopus 로고
    • Epiligrin, the major human keratinocyte integrin ligand, is a target in both an acquired autoimmune and an inherited subepidermal blistering skin disease
    • Domloge-Hultsch N., Gammon W.R., Briggaman R.A., Gil S.G., Carter W.G., Yancey K.B. Epiligrin, the major human keratinocyte integrin ligand, is a target in both an acquired autoimmune and an inherited subepidermal blistering skin disease. J Clin Invest 1992, 90:1628-1633.
    • (1992) J Clin Invest , vol.90 , pp. 1628-1633
    • Domloge-Hultsch, N.1    Gammon, W.R.2    Briggaman, R.A.3    Gil, S.G.4    Carter, W.G.5    Yancey, K.B.6
  • 39
    • 0035879096 scopus 로고    scopus 로고
    • Molecular and functional characterization of the four-transmembrane molecule l6 in epidermal keratinocytes
    • Storim J., Friedl P., Schaefer B.M., Bechtel M., Wallich R., Kramer M.D., et al. Molecular and functional characterization of the four-transmembrane molecule l6 in epidermal keratinocytes. Exp Cell Res 2001, 267:233-242.
    • (2001) Exp Cell Res , vol.267 , pp. 233-242
    • Storim, J.1    Friedl, P.2    Schaefer, B.M.3    Bechtel, M.4    Wallich, R.5    Kramer, M.D.6
  • 40
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing-aiming for perfect skin regeneration
    • Martin P. Wound healing-aiming for perfect skin regeneration. Science 1997, 276:75-81.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 41
    • 34347232319 scopus 로고    scopus 로고
    • Wound re-epithelialization: modulating keratinocyte migration in wound healing
    • Raja, Sivamani K., Garcia M.S., Isseroff R.R. Wound re-epithelialization: modulating keratinocyte migration in wound healing. Front Biosci 2007, 12:2849-2868.
    • (2007) Front Biosci , vol.12 , pp. 2849-2868
    • Raja1    Sivamani, K.2    Garcia, M.S.3    Isseroff, R.R.4
  • 42
    • 0038521319 scopus 로고    scopus 로고
    • Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin
    • Veitch D.P., Nokelainen P., McGowan K.A., Nguyen T.T., Nguyen N.E., Stephenson R., et al. Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin. J Biol Chem 2003, 278:15661-15668.
    • (2003) J Biol Chem , vol.278 , pp. 15661-15668
    • Veitch, D.P.1    Nokelainen, P.2    McGowan, K.A.3    Nguyen, T.T.4    Nguyen, N.E.5    Stephenson, R.6
  • 43
    • 16544391155 scopus 로고    scopus 로고
    • Laminin-5 in epithelial tumour invasion
    • Katayama M., Sekiguchi K. Laminin-5 in epithelial tumour invasion. J Mol Histol 2004, 35:277-286.
    • (2004) J Mol Histol , vol.35 , pp. 277-286
    • Katayama, M.1    Sekiguchi, K.2
  • 45
    • 0025615956 scopus 로고
    • The hemidesmosomal plaque I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia.
    • Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A., et al. The hemidesmosomal plaque I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia. Differentiation 1990, 45:207-220.
    • (1990) Differentiation , vol.45 , pp. 207-220
    • Owaribe, K.1    Kartenbeck, J.2    Stumpp, S.3    Magin, T.M.4    Krieg, T.5    Diaz, L.A.6
  • 46
    • 0027744501 scopus 로고
    • Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo
    • Juhasz I., Murphy G.F., Yan H.C., Herlyn M., Albelda S.M. Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo. Am J Pathol 1993, 143:1458-1469.
    • (1993) Am J Pathol , vol.143 , pp. 1458-1469
    • Juhasz, I.1    Murphy, G.F.2    Yan, H.C.3    Herlyn, M.4    Albelda, S.M.5
  • 47
    • 67650436092 scopus 로고    scopus 로고
    • Clustering of syndecan-4 and integrin beta1 by laminin alpha 3 chain-derived peptide promotes keratinocyte migration
    • Araki E., Momota Y., Togo T., Tanioka M., Hozumi K., Nomizu M., et al. Clustering of syndecan-4 and integrin beta1 by laminin alpha 3 chain-derived peptide promotes keratinocyte migration. Mol Biol Cell 2009, 20:3012-3024.
    • (2009) Mol Biol Cell , vol.20 , pp. 3012-3024
    • Araki, E.1    Momota, Y.2    Togo, T.3    Tanioka, M.4    Hozumi, K.5    Nomizu, M.6
  • 48
    • 0032841440 scopus 로고    scopus 로고
    • The alpha3 laminin subunit, alpha6beta4 and alpha3beta1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger L.E., Hopkinson S.B., deHart G.W., Collawn S., Couchman J.R., Jones J.C. The alpha3 laminin subunit, alpha6beta4 and alpha3beta1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J Cell Sci 1999, 112(16):2615-2629.
    • (1999) J Cell Sci , vol.112 , Issue.16 , 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
  • 49
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator
    • Goldfinger L.E., Stack M.S., Jones J.C. Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J Cell Biol 1998, 141:255-265.
    • (1998) J Cell Biol , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3
  • 50
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • Litjens S.H., de Pereda J.M., Sonnenberg A. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol 2006, 16:376-383.
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    de Pereda, J.M.2    Sonnenberg, A.3
  • 51
    • 61949421021 scopus 로고    scopus 로고
    • Integrin alpha3beta1 inhibits directional migration and wound re-epithelialization in the skin
    • Margadant C., Raymond K., Kreft M., Sachs N., Janssen H., Sonnenberg A. Integrin alpha3beta1 inhibits directional migration and wound re-epithelialization in the skin. J Cell Sci 2009, 122:278-288.
    • (2009) J Cell Sci , vol.122 , pp. 278-288
    • Margadant, C.1    Raymond, K.2    Kreft, M.3    Sachs, N.4    Janssen, H.5    Sonnenberg, A.6
  • 52
    • 75049085620 scopus 로고    scopus 로고
    • Transdominant regulation of integrin function: mechanisms of crosstalk
    • Gonzalez A.M., Bhattacharya R., deHart G.W., Jones J.C. Transdominant regulation of integrin function: mechanisms of crosstalk. Cell Signal 2010, 22:578-583.
    • (2010) Cell Signal , vol.22 , pp. 578-583
    • Gonzalez, A.M.1    Bhattacharya, R.2    deHart, G.W.3    Jones, J.C.4
  • 53
    • 57649136750 scopus 로고    scopus 로고
    • Integrin cross-talk in endothelial cells is regulated by protein kinase A and protein phosphatase 1
    • Gonzalez A.M., Claiborne J., Jones J.C. Integrin cross-talk in endothelial cells is regulated by protein kinase A and protein phosphatase 1. J Biol Chem 2008, 283:31849-31860.
    • (2008) J Biol Chem , vol.283 , pp. 31849-31860
    • Gonzalez, A.M.1    Claiborne, J.2    Jones, J.C.3
  • 54
    • 33845923906 scopus 로고    scopus 로고
    • Integrin beta4 regulates migratory behavior of keratinocytes by determining laminin-332 organization
    • Sehgal B.U., DeBiase P.J., Matzno S., Chew T.L., Claiborne J.N., Hopkinson S.B., et al. Integrin beta4 regulates migratory behavior of keratinocytes by determining laminin-332 organization. J Biol Chem 2006, 281:35487-35498.
    • (2006) J Biol Chem , vol.281 , pp. 35487-35498
    • Sehgal, B.U.1    DeBiase, P.J.2    Matzno, S.3    Chew, T.L.4    Claiborne, J.N.5    Hopkinson, S.B.6
  • 55
    • 66349125931 scopus 로고    scopus 로고
    • 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes
    • Kligys K., Yao J., Yu D., Jones J.C. 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes. Biochem Biophys Res Commun 2009, 383:450-454.
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 450-454
    • Kligys, K.1    Yao, J.2    Yu, D.3    Jones, J.C.4
  • 56
    • 36148996844 scopus 로고    scopus 로고
    • The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes
    • Kligys K., Claiborne J.N., DeBiase P.J., Hopkinson S.B., Wu Y., Mizuno K., et al. The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes. J Biol Chem 2007, 282:32520-32528.
    • (2007) J Biol Chem , vol.282 , pp. 32520-32528
    • Kligys, K.1    Claiborne, J.N.2    DeBiase, P.J.3    Hopkinson, S.B.4    Wu, Y.5    Mizuno, K.6
  • 57
    • 33750514792 scopus 로고    scopus 로고
    • Beta4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1
    • Pullar C.E., Baier B.S., Kariya Y., Russell A.J., Horst B.A., Marinkovich M.P., et al. beta4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1. Mol Biol Cell 2006, 17:4925-4935.
    • (2006) Mol Biol Cell , vol.17 , pp. 4925-4935
    • Pullar, C.E.1    Baier, B.S.2    Kariya, Y.3    Russell, A.J.4    Horst, B.A.5    Marinkovich, M.P.6
  • 58
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B., et al. Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell 1995, 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
  • 59
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh M., Song X., Mouneimne G., Sidani M., Lawrence D.S., Condeelis J.S. Cofilin promotes actin polymerization and defines the direction of cell motility. Science 2004, 304:743-746.
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 60
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers
    • Kiuchi T., Ohashi K., Kurita S., Mizuno K. Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J Cell Biol 2007, 177:465-476.
    • (2007) J Cell Biol , vol.177 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4
  • 61
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan A.Y., Bailly M., Zebda N., Segall J.E., Condeelis J.S. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J Cell Biol 2000, 148:531-542.
    • (2000) J Cell Biol , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 62
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla A., Birkenfeld J., Bokoch G.M. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 2005, 7:21-29.
    • (2005) Nat Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 63
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 2002, 108:233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 64
    • 0031283128 scopus 로고    scopus 로고
    • The integrin alpha6beta4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • Rabinovitz I., Mercurio A.M. The integrin alpha6beta4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J Cell Biol 1997, 139:1873-1884.
    • (1997) J Cell Biol , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 65
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation
    • Svitkina T.M., Verkhovsky A.B., McQuade K.M., Borisy G.G. Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J Cell Biol 1997, 139:397-415.
    • (1997) J Cell Biol , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 66
    • 0023225091 scopus 로고
    • The relationship between intermediate filaments and microfilaments before and during the formation of desmosomes and adherens-type junctions in mouse epidermal keratinocytes
    • Green K.J., Geiger B., Jones J.C., Talian J.C., Goldman R.D. The relationship between intermediate filaments and microfilaments before and during the formation of desmosomes and adherens-type junctions in mouse epidermal keratinocytes. J Cell Biol 1987, 104:1389-1402.
    • (1987) J Cell Biol , vol.104 , pp. 1389-1402
    • Green, K.J.1    Geiger, B.2    Jones, J.C.3    Talian, J.C.4    Goldman, R.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.