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Volumn 289, Issue 21, 2014, Pages 14925-14940

Adducin is required for desmosomal cohesion in keratinocytes

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION;

EID: 84901423904     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.527127     Document Type: Article
Times cited : (35)

References (57)
  • 2
    • 0029022939 scopus 로고
    • Adducin: A physical model with implications for function in assembly of spectrin-actin complexes
    • Hughes, C. A., and Bennett, V. (1995) Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J. Biol. Chem. 270, 18990-18996 .
    • (1995) J. Biol. Chem. , vol.270 , pp. 18990-18996
    • Hughes, C.A.1    Bennett, V.2
  • 3
    • 0032563088 scopus 로고    scopus 로고
    • Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain
    • DOI 10.1074/jbc.273.30.19329
    • Li, X., Matsuoka, Y., and Bennett, V. (1998) Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain. J. Biol. Chem. 273, 19329-19338 . (Pubitemid 28366334)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 19329-19338
    • Li, X.1    Matsuoka, Y.2    Bennett, V.3
  • 4
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducin: Calcium/calmodulin-regulated capping of the barbed ends of actin filaments
    • Kuhlman, P. A., Hughes, C. A., Bennett, V., and Fowler, V. M. (1996) A new function for adducin: calcium/calmodulin-regulated capping of the barbed ends of actin filaments. J. Biol. Chem. 271, 7986-7991 .
    • (1996) J. Biol. Chem. , Issue.271 , pp. 7986-7991
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennett, V.3    Fowler, V.M.4
  • 5
    • 0027992919 scopus 로고
    • Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: Demonstration of unipolar α-actinin-F-actin crosslinking
    • Taylor, K. A., and Taylor, D. W. (1994) Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar α-actinin-F-actin cross-linking. Biophys. J. 67, 1976-1983 . (Pubitemid 24342069)
    • (1994) Biophysical Journal , vol.67 , Issue.5 , pp. 1976-1983
    • Taylor, K.A.1    Taylor, D.W.2
  • 7
    • 0028845349 scopus 로고
    • 35H, a sequence isolated as a protein kinase C-binding protein, is a novel member of the adducin family
    • Dong, L., Chapline, C., Mousseau, B., Fowler, L., Ramsay, K., Stevens, J. L., and Jaken, S. (1995) 35H, a sequence isolated as a protein kinase C-binding protein, is a novel member of the adducin family. J. Biol. Chem. 270, 25534-25540 .
    • (1995) J. Biol. Chem. , vol.270 , pp. 25534-25540
    • Dong, L.1    Chapline, C.2    Mousseau, B.3    Fowler, L.4    Ramsay, K.5    Stevens, J.L.6    Jaken, S.7
  • 8
    • 77958043359 scopus 로고    scopus 로고
    • Adducins regulate remodeling of apical junctions in human epithelial cells
    • Naydenov, N. G., and Ivanov, A. I. (2010) Adducins regulate remodeling of apical junctions in human epithelial cells. Mol. Biol. Cell 21, 3506-3517 .
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3506-3517
    • Naydenov, N.G.1    Ivanov, A.I.2
  • 9
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • DOI 10.1038/328359a0
    • Gardner, K., and Bennett, V. (1987) Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328, 359-362 . (Pubitemid 17097660)
    • (1987) Nature , vol.328 , Issue.6128 , pp. 359-362
    • Gardner, K.1    Bennett, V.2
  • 10
    • 0029841346 scopus 로고    scopus 로고
    • Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C
    • DOI 10.1074/jbc.271.41.25157
    • Matsuoka, Y., Hughes, C. A., and Bennett, V. (1996) Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C. J. Biol. Chem. 271, 25157-25166 . (Pubitemid 26337876)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25157-25166
    • Matsuoka, Y.1    Hughes, C.A.2    Bennett, V.3
  • 12
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho- associated kinase (Rho-kinase) and myosin phosphatase
    • DOI 10.1074/jbc.273.10.5542
    • Kimura, K., Fukata, Y., Matsuoka, Y., Bennett, V., Matsuura, Y., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1998) Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J. Biol. Chem. 273, 5542-5548 . (Pubitemid 28124020)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3    Bennett, V.4    Matsuura, Y.5    Okawa, K.6    Iwamatsu, A.7    Kaibuchi, K.8
  • 13
  • 14
    • 0030035043 scopus 로고    scopus 로고
    • Identification of a putative target for Rho as the serine-threonine kinase protein kinase N
    • Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996) Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 271, 648-650 . (Pubitemid 26052909)
    • (1996) Science , vol.271 , Issue.5249 , pp. 648-650
    • Amano, M.1    Mukai, H.2    Ono, Y.3    Chihara, K.4    Matsui, T.5    Hamajima, Y.6    Okawa, K.7    Iwamatsu, A.8    Kaibuchi, K.9
  • 15
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTpases and the actin cytoskeleton
    • DOI 10.1126/science.279.5350.509
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279, 509-514 . (Pubitemid 28067271)
    • (1998) Science , vol.279 , Issue.5350 , pp. 509-514
    • Hall, A.1
  • 17
    • 34548863639 scopus 로고    scopus 로고
    • Pemphigus IgG causes skin splitting in the presence of both desmoglein 1 and desmoglein 3
    • DOI 10.2353/ajpath.2007.070028
    • Spindler, V., Drenckhahn, D., Zillikens, D., and Waschke, J. (2007) Pemphigus IgG causes skin splitting in the presence of both desmoglein 1 and desmoglein 3. Am. J. Pathol. 171, 906-916 . (Pubitemid 47440989)
    • (2007) American Journal of Pathology , vol.171 , Issue.3 , pp. 906-916
    • Spindler, V.1    Drenckhahn, D.2    Zillikens, D.3    Waschke, J.4
  • 18
    • 79955785245 scopus 로고    scopus 로고
    • Role of Rho GTPases in desmosomal adhesion and pemphigus pathogenesis
    • Spindler, V., and Waschke, J. (2011) Role of Rho GTPases in desmosomal adhesion and pemphigus pathogenesis. Ann. Anat. 193, 177-180 .
    • (2011) Ann. Anat. , vol.193 , pp. 177-180
    • Spindler, V.1    Waschke, J.2
  • 19
    • 84856909766 scopus 로고    scopus 로고
    • Desmoglein as a target in skin disease and beyond
    • Amagai, M., and Stanley, J. R. (2012) Desmoglein as a target in skin disease and beyond. J. Invest. Dermatol. 132, 776-784 .
    • (2012) J. Invest. Dermatol. , vol.132 , pp. 776-784
    • Amagai, M.1    Stanley, J.R.2
  • 20
    • 84907971653 scopus 로고    scopus 로고
    • Desmosomes and extradesmosomal adhesive signaling contacts in pemphigus
    • 10.1002/med.21310
    • Waschke, J., and Spindler, V. (2014) Desmosomes and extradesmosomal adhesive signaling contacts in pemphigus. Med. Res. Rev. 10.1002/med.21310 .
    • (2014) Med. Res. Rev.
    • Waschke, J.1    Spindler, V.2
  • 21
    • 21244476854 scopus 로고    scopus 로고
    • Desmosome signaling: Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization
    • DOI 10.1074/jbc.M501365200
    • Berkowitz, P., Hu, P., Liu, Z., Diaz, L. A., Enghild, J. J., Chua, M. P., and Rubenstein, D. S. (2005) Desmosome signaling. Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization. J. Biol. Chem. 280, 23778-23784 . (Pubitemid 40884862)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23778-23784
    • Berkowitz, P.1    Hu, P.2    Liu, Z.3    Diaz, L.A.4    Enghild, J.J.5    Chua, M.P.6    Rubenstein, D.S.7
  • 22
    • 27644507915 scopus 로고    scopus 로고
    • Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction
    • DOI 10.1172/JCI23475
    • Waschke, J., Bruggeman, P., Baumgartner, W., Zillikens, D., and Drenckhahn, D. (2005) Pemphigus foliaceus IgG causes dissociation of desmoglein 1-containing junctions without blocking desmoglein 1 transinteraction. J. Clin. Invest. 115, 3157-3165 . (Pubitemid 41567580)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.11 , pp. 3157-3165
    • Waschke, J.1    Bruggeman, P.2    Baumgartner, W.3    Zillikens, D.4    Drenckhahn, D.5
  • 24
    • 84865293046 scopus 로고    scopus 로고
    • Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics
    • Tsang, S. M., Brown, L., Gadmor, H., Gammon, L., Fortune, F., Wheeler, A., and Wan, H. (2012) Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42 in the regulation of actin organisation and dynamics. Exp. Cell Res. 318, 2269-2283 .
    • (2012) Exp. Cell Res. , vol.318 , pp. 2269-2283
    • Tsang, S.M.1    Brown, L.2    Gadmor, H.3    Gammon, L.4    Fortune, F.5    Wheeler, A.6    Wan, H.7
  • 26
    • 34248188618 scopus 로고    scopus 로고
    • Phosphorylation of adducin by protein kinase Cδ promotes cell motility
    • Chen, C. L., Hsieh, Y. T., and Chen, H. C. (2007) Phosphorylation of adducin by protein kinase Cδ promotes cell motility. J. Cell Sci. 120, 1157-1167 .
    • (2007) J. Cell Sci. , vol.120 , pp. 1157-1167
    • Chen, C.L.1    Hsieh, Y.T.2    Chen, H.C.3
  • 27
    • 84872224315 scopus 로고    scopus 로고
    • Desmoglein 2 is less important than desmoglein 3 for keratinocyte cohesion
    • Hartlieb, E., Kempf, B., Partilla, M., Vigh, B., Spindler, V., and Waschke, J. (2013) Desmoglein 2 is less important than desmoglein 3 for keratinocyte cohesion. PLoS One 8, e53739 .
    • (2013) PLoS One , vol.8
    • Hartlieb, E.1    Kempf, B.2    Partilla, M.3    Vigh, B.4    Spindler, V.5    Waschke, J.6
  • 29
    • 0033792693 scopus 로고    scopus 로고
    • Assembly pathway of desmoglein 3 to desmosomes and its perturbation by pemphigus vulgaris-IgG in cultured keratinocytes, as revealed by time-lapsed labeling immunoelectron microscopy
    • Sato, M., Aoyama, Y., and Kitajima, Y. (2000) Assembly pathway of desmoglein 3 to desmosomes and its perturbation by pemphigus vulgaris-IgG in cultured keratinocytes, as revealed by time-lapsed labeling immunoelectron microscopy. Lab. Invest. 80, 1583-1592 .
    • (2000) Lab. Invest. , vol.80 , pp. 1583-1592
    • Sato, M.1    Aoyama, Y.2    Kitajima, Y.3
  • 30
    • 49649084477 scopus 로고    scopus 로고
    • Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction
    • Heupel, W. M., Zillikens, D., Drenckhahn, D., and Waschke, J. (2008) Pemphigus vulgaris IgG directly inhibit desmoglein 3-mediated transinteraction. J. Immunol. 181, 1825-1834 .
    • (2008) J. Immunol. , vol.181 , pp. 1825-1834
    • Heupel, W.M.1    Zillikens, D.2    Drenckhahn, D.3    Waschke, J.4
  • 31
    • 34547113086 scopus 로고    scopus 로고
    • Anti-desmoglein 3 (Dsg3) monoclonal antibodies deplete desmosomes of Dsg3 and differ in their Dsg3-depleting activities related to pathogenicity
    • DOI 10.1074/jbc.M607963200
    • Yamamoto, Y., Aoyama, Y., Shu, E., Tsunoda, K., Amagai, M., and Kitajima, Y. (2007) Anti-desmoglein 3 (Dsg3) monoclonal antibodies deplete desmosomes of Dsg3 and differ in their Dsg3-depleting activities related to pathogenicity. J. Biol. Chem. 282, 17866-17876 . (Pubitemid 47100314)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17866-17876
    • Yamamoto, Y.1    Aoyama, Y.2    Shu, E.3    Tsunoda, K.4    Amagai, M.5    Kitajima, Y.6
  • 35
    • 0041468477 scopus 로고    scopus 로고
    • Cortactin tyrosine phosphorylation requires Rac1 activity and association with the cortical actin cytoskeleton
    • DOI 10.1091/mbc.E02-11-0753
    • Head, J. A., Jiang, D., Li, M., Zorn, L. J., Schaefer, E. M., Parsons, J. T., and Weed, S. A. (2003) Cortactin tyrosine phosphorylation requires Rac1 activity and association with the cortical actin cytoskeleton. Mol. Biol. Cell 14, 3216-3229 . (Pubitemid 37013122)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.8 , pp. 3216-3229
    • Head, J.A.1    Jiang, D.2    Li, M.3    Zorn, L.J.4    Schaefer, E.M.5    Parsons, J.T.6    Weed, S.A.7
  • 36
    • 0039791449 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase/extracellular signal- regulated kinase pathway by conventional, novel and atypical protein kinase C isotypes
    • Schönwasser, D. C., Marais, R. M., Marshall, C. J., and Parker, P. J. (1998) Activation of the mitogen-activated protein kinase/extracellular signalregulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes. Mol. Cell. Biol. 18, 790-798 . (Pubitemid 28063412)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.2 , pp. 790-798
    • Schonwasser, D.C.1    Marais, R.M.2    Marshall, C.J.3    Parker, P.J.4
  • 37
    • 84870772239 scopus 로고    scopus 로고
    • Protein kinase C, an elusive therapeutic target?
    • Mochly-Rosen, D., Das, K., and Grimes, K. V. (2012) Protein kinase C, an elusive therapeutic target? Nat. Rev. Drug Discov. 11, 937-957 .
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 937-957
    • Mochly-Rosen, D.1    Das, K.2    Grimes, K.V.3
  • 38
    • 0028869473 scopus 로고
    • Pemphigus IgG, but not bullous pemphigoid IgG, causes a transient increase in intracellular calcium and inositol 1,4,5-triphosphate in DJM-1 cells, a squamous cell carcinoma line
    • Seishima, M., Esaki, C., Osada, K., Mori, S., Hashimoto, T., and Kitajima, Y. (1995) Pemphigus IgG, but not bullous pemphigoid IgG, causes a transient increase in intracellular calcium and inositol 1,4,5-triphosphate in DJM-1 cells, a squamous cell carcinoma line. J. Invest. Dermatol. 104, 33-37 .
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 33-37
    • Seishima, M.1    Esaki, C.2    Osada, K.3    Mori, S.4    Hashimoto, T.5    Kitajima, Y.6
  • 39
    • 80052612549 scopus 로고    scopus 로고
    • α-Adducin translocates to the nucleus upon loss of cell-cell adhesions
    • Chen, C. L., Lin, Y. P., Lai, Y. C., and Chen, H. C. (2011) α-Adducin translocates to the nucleus upon loss of cell-cell adhesions. Traffic 12, 1327-1340 .
    • (2011) Traffic , vol.12 , pp. 1327-1340
    • Chen, C.L.1    Lin, Y.P.2    Lai, Y.C.3    Chen, H.C.4
  • 40
    • 0028970587 scopus 로고
    • P80/85 cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells
    • DOI 10.1074/jbc.270.44.26613
    • Okamura, H., and Resh, M. D. (1995) p80/85 cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells. J. Biol. Chem. 270, 26613-26618 . (Pubitemid 3006243)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.44 , pp. 26613-26618
    • Okamura, H.1    Resh, M.D.2
  • 41
    • 79958696268 scopus 로고    scopus 로고
    • Distinct phosphorylation requirements regulate cortactin activation by TirEPEC and its binding to N-WASP
    • Nieto-Pelegrin, E., and Martinez-Quiles, N. (2009) Distinct phosphorylation requirements regulate cortactin activation by TirEPEC and its binding to N-WASP. Cell Commun. Signal. 7, 11 .
    • (2009) Cell Commun. Signal. , vol.7 , pp. 11
    • Nieto-Pelegrin, E.1    Martinez-Quiles, N.2
  • 42
    • 84866508744 scopus 로고    scopus 로고
    • Regulation of late endosomal/lysosomal maturation and trafficking by cortactin affects Golgi morphology
    • Kirkbride, K. C., Hong, N. H., French, C. L., Clark, E. S., Jerome, W. G., and Weaver, A. M. (2012) Regulation of late endosomal/lysosomal maturation and trafficking by cortactin affects Golgi morphology. Cytoskeleton 69, 625-643 .
    • (2012) Cytoskeleton , vol.69 , pp. 625-643
    • Kirkbride, K.C.1    Hong, N.H.2    French, C.L.3    Clark, E.S.4    Jerome, W.G.5    Weaver, A.M.6
  • 43
    • 0032820709 scopus 로고    scopus 로고
    • Mobility and cytoskeletal interactions of cell adhesion receptors
    • DOI 10.1016/S0955-0674(99)00020-4
    • Kusumi, A., Suzuki, K., and Koyasako, K. (1999) Mobility and cytoskeletal interactions of cell adhesion receptors. Curr. Opin. Cell Biol. 11, 582-590 . (Pubitemid 29460399)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.5 , pp. 582-590
    • Kusumi, A.1    Suzuki, K.2    Koyasako, K.3
  • 44
    • 0032498847 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: Corralling and tethering by the membrane skeleton
    • DOI 10.1083/jcb.140.5.1227
    • Sako, Y., Nagafuchi, A., Tsukita, S., Takeichi, M., and Kusumi, A. (1998) Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton. J. Cell Biol. 140, 1227-1240 . (Pubitemid 28128881)
    • (1998) Journal of Cell Biology , vol.140 , Issue.5 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 45
    • 0037444477 scopus 로고    scopus 로고
    • Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells
    • DOI 10.1242/jcs.00322
    • Baumgartner, W., Schütz, G. J., Wiegand, J., Golenhofen, N., and Drenckhahn, D. (2003) Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells. J. Cell Sci. 116, 1001-1011 . (Pubitemid 36395611)
    • (2003) Journal of Cell Science , vol.116 , Issue.6 , pp. 1001-1011
    • Baumgartner, W.1    Schutz, G.J.2    Wiegand, J.3    Golenhofen, N.4    Drenckhahn, D.5
  • 48
    • 78650630568 scopus 로고    scopus 로고
    • Protective endogenous cyclic adenosine 5′-monophosphate signaling triggered by pemphigus autoantibodies
    • Spindler, V., Vielmuth, F., Schmidt, E., Rubenstein, D. S., and Waschke, J. (2010) Protective endogenous cyclic adenosine 5′-monophosphate signaling triggered by pemphigus autoantibodies. J. Immunol. 185, 6831-6838 .
    • (2010) J. Immunol. , vol.185 , pp. 6831-6838
    • Spindler, V.1    Vielmuth, F.2    Schmidt, E.3    Rubenstein, D.S.4    Waschke, J.5
  • 49
    • 0029059657 scopus 로고
    • Pharmacologic evidence for involvement of phospholipase C in pemphigus IgG-induced inositol 1,4,5-trisphosphate generation, intracellular calcium increase, and plasminogen activator secretion in DJM-1 cells, a squamous cell carcinoma line
    • Esaki, C., Seishima, M., Yamada, T., Osada, K., and Kitajima, Y. (1995) Pharmacologic evidence for involvement of phospholipase C in pemphigus IgG-induced inositol 1,4,5-trisphosphate generation, intracellular calcium increase, and plasminogen activator secretion in DJM-1 cells, a squamous cell carcinoma line. J. Invest. Dermatol. 105, 329-333 .
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 329-333
    • Esaki, C.1    Seishima, M.2    Yamada, T.3    Osada, K.4    Kitajima, Y.5
  • 50
    • 0030890618 scopus 로고    scopus 로고
    • Pemphigus IgG activates and translocates protein kinase C from the cytosol to the particulate/cytoskeleton fractions in human keratinocytes
    • Osada, K., Seishima, M., and Kitajima, Y. (1997) Pemphigus IgG activates and translocates protein kinase C from the cytosol to the particulate/ cytoskeleton fractions in human keratinocytes. J. Invest. Dermatol. 108, 482-487 . (Pubitemid 27148285)
    • (1997) Journal of Investigative Dermatology , vol.108 , Issue.4 , pp. 482-487
    • Osada, K.1    Seishima, M.2    Kitajima, Y.3
  • 51
    • 84896990480 scopus 로고    scopus 로고
    • Desmosomal cadherins and signaling: Lessons from autoimmune disease
    • Spindler, V., and Waschke, J. (2014) Desmosomal cadherins and signaling: lessons from autoimmune disease. Cell. Commun. Adhes. 21, 77-84 .
    • (2014) Cell. Commun. Adhes. , vol.21 , pp. 77-84
    • Spindler, V.1    Waschke, J.2
  • 52
    • 44449092953 scopus 로고    scopus 로고
    • The desmosome and pemphigus
    • Waschke, J. (2008) The desmosome and pemphigus. Histochem. Cell Biol. 130, 21-54 .
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 21-54
    • Waschke, J.1
  • 53
    • 77449142413 scopus 로고    scopus 로고
    • Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC
    • Cirillo, N., Lanza, A., and Prime, S. S. (2010) Induction of hyper-adhesion attenuates autoimmune-induced keratinocyte cell-cell detachment and processing of adhesion molecules via mechanisms that involve PKC. Exp. Cell Res. 316, 580-592 .
    • (2010) Exp. Cell Res. , vol.316 , pp. 580-592
    • Cirillo, N.1    Lanza, A.2    Prime, S.S.3
  • 54
    • 33947191090 scopus 로고    scopus 로고
    • Calcium-independent desmosomes of keratinocytes are hyper-adhesive
    • DOI 10.1038/sj.jid.5700643, PII 5700643
    • Kimura, T. E., Merritt, A. J., and Garrod, D. R. (2007) Calcium-independent desmosomes of keratinocytes are hyper-adhesive. J. Invest. Dermatol. 127, 775-781 . (Pubitemid 46434658)
    • (2007) Journal of Investigative Dermatology , vol.127 , Issue.4 , pp. 775-781
    • Kimura, T.E.1    Merritt, A.J.2    Garrod, D.R.3
  • 55
    • 84855945224 scopus 로고    scopus 로고
    • Desmoplakin regulates desmosome hyperadhesion
    • Hobbs, R. P., and Green, K. J. (2012) Desmoplakin regulates desmosome hyperadhesion. J. Invest. Dermatol. 132, 482-485 .
    • (2012) J. Invest. Dermatol. , vol.132 , pp. 482-485
    • Hobbs, R.P.1    Green, K.J.2
  • 56
    • 84878537119 scopus 로고    scopus 로고
    • Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation
    • Kröger, C., Loschke, F., Schwarz, N., Windoffer, R., Leube, R. E., and Magin, T. M. (2013) Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation. J. Cell Biol. 201, 681-692 .
    • (2013) J. Cell Biol. , vol.201 , pp. 681-692
    • Kröger, C.1    Loschke, F.2    Schwarz, N.3    Windoffer, R.4    Leube, R.E.5    Magin, T.M.6


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