메뉴 건너뛰기




Volumn 21, Issue 5, 2009, Pages 708-716

Plakophilins: multifunctional scaffolds for adhesion and signaling

Author keywords

[No Author keywords available]

Indexed keywords

PLAKOPHILIN; PROTEIN KINASE C;

EID: 70349333829     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2009.07.002     Document Type: Review
Times cited : (133)

References (67)
  • 1
    • 0037385290 scopus 로고    scopus 로고
    • Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains
    • Hatzfeld M., Green K.J., and Sauter H. Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. J Cell Sci 116 (2002) 1219-1233
    • (2002) J Cell Sci , vol.116 , pp. 1219-1233
    • Hatzfeld, M.1    Green, K.J.2    Sauter, H.3
  • 2
    • 62149101141 scopus 로고    scopus 로고
    • Protein p0071-an armadillo plaque protein that characterizes a specific subtype of adherens junctions
    • Hofmann I., Schlechter T., Kuhn C., Hergt M., and Franke W.W. Protein p0071-an armadillo plaque protein that characterizes a specific subtype of adherens junctions. J Cell Sci 122 (2009) 21-24
    • (2009) J Cell Sci , vol.122 , pp. 21-24
    • Hofmann, I.1    Schlechter, T.2    Kuhn, C.3    Hergt, M.4    Franke, W.W.5
  • 3
    • 33845383688 scopus 로고    scopus 로고
    • Plakophilins: multifunctional proteins or just regulators of desmosomal adhesions?
    • A comprehensive review of the three main plakophilin isoforms outlines their genetic, structural, and functional similarities and differences in the context of cell adhesion, signaling and disease.
    • Hatzfeld M. Plakophilins: multifunctional proteins or just regulators of desmosomal adhesions?. Biochim Biophys Acta 1773 (2007) 69-77. A comprehensive review of the three main plakophilin isoforms outlines their genetic, structural, and functional similarities and differences in the context of cell adhesion, signaling and disease.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 69-77
    • Hatzfeld, M.1
  • 4
    • 12344281930 scopus 로고    scopus 로고
    • Structure of the armadillo repeat domain of plakophilin 1
    • Choi H.-J., and Weis W.I. Structure of the armadillo repeat domain of plakophilin 1. J Mol Biol 346 (2005) 367-376
    • (2005) J Mol Biol , vol.346 , pp. 367-376
    • Choi, H.-J.1    Weis, W.I.2
  • 6
    • 0030856140 scopus 로고    scopus 로고
    • Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components
    • Schmidt A., Langbein L., Rode M., Pratzel S., Zimbelmann R., and Franke W.W. Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components. Cell Tissue Res 290 (1997) 481-499
    • (1997) Cell Tissue Res , vol.290 , pp. 481-499
    • Schmidt, A.1    Langbein, L.2    Rode, M.3    Pratzel, S.4    Zimbelmann, R.5    Franke, W.W.6
  • 7
    • 0031019355 scopus 로고    scopus 로고
    • The distribution of the desmosomal protein, plakophilin 1, in human skin and skin tumors
    • Moll I., Kurzen H., Langbein L., and Franke W.W. The distribution of the desmosomal protein, plakophilin 1, in human skin and skin tumors. J Invest Dermatol 108 (1997) 139-146
    • (1997) J Invest Dermatol , vol.108 , pp. 139-146
    • Moll, I.1    Kurzen, H.2    Langbein, L.3    Franke, W.W.4
  • 8
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • Mertens C., Kuhn C., and Franke W.W. Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J Cell Biol 135 (1996) 1009-1025
    • (1996) J Cell Biol , vol.135 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 9
    • 0032970165 scopus 로고    scopus 로고
    • Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues
    • Mertens C., Kuhn C., Moll R., Schwetlick I., and Franke W.W. Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues. Differentiation 64 (1999) 277-290
    • (1999) Differentiation , vol.64 , pp. 277-290
    • Mertens, C.1    Kuhn, C.2    Moll, R.3    Schwetlick, I.4    Franke, W.W.5
  • 10
    • 0032779596 scopus 로고    scopus 로고
    • Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells
    • Bonne S., van Hengel J., Nollet F., Kools P., and van Roy F. Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells. J Cell Sci 112 (1999) 2265-2276
    • (1999) J Cell Sci , vol.112 , pp. 2265-2276
    • Bonne, S.1    van Hengel, J.2    Nollet, F.3    Kools, P.4    van Roy, F.5
  • 12
    • 0034599841 scopus 로고    scopus 로고
    • The function of plakophilin 1 in desmosome assembly and actin filament organization
    • Hatzfeld M., Haffner C., Schulze K., and Vinzens U. The function of plakophilin 1 in desmosome assembly and actin filament organization. J Cell Biol 149 (2000) 209-222
    • (2000) J Cell Biol , vol.149 , pp. 209-222
    • Hatzfeld, M.1    Haffner, C.2    Schulze, K.3    Vinzens, U.4
  • 13
    • 0033868312 scopus 로고    scopus 로고
    • Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis
    • Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnolzer M., and Herrmann H. Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. J Cell Sci 113 (2000) 2471-2483
    • (2000) J Cell Sci , vol.113 , pp. 2471-2483
    • Hofmann, I.1    Mertens, C.2    Brettel, M.3    Nimmrich, V.4    Schnolzer, M.5    Herrmann, H.6
  • 14
    • 0033603436 scopus 로고    scopus 로고
    • The head domain of plakophilin-1 binds to desmoplakin and enhances its recruitment to desmosomes. Implications for cutaneous disease
    • Kowalczyk A.P., Hatzfeld M., Bornslaeger E.A., Kopp D.S., Borgwardt J.E., Corcoran C.M., Settler A., and Green K.J. The head domain of plakophilin-1 binds to desmoplakin and enhances its recruitment to desmosomes. Implications for cutaneous disease. J Biol Chem 274 (1999) 18145-18148
    • (1999) J Biol Chem , vol.274 , pp. 18145-18148
    • Kowalczyk, A.P.1    Hatzfeld, M.2    Bornslaeger, E.A.3    Kopp, D.S.4    Borgwardt, J.E.5    Corcoran, C.M.6    Settler, A.7    Green, K.J.8
  • 16
    • 0037155877 scopus 로고    scopus 로고
    • Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta-catenin signalling
    • Chen X., Bonne S., Hatzfeld M., van Roy F., and Green K.J. Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta-catenin signalling. J Biol Chem 277 (2002) 10512-10522
    • (2002) J Biol Chem , vol.277 , pp. 10512-10522
    • Chen, X.1    Bonne, S.2    Hatzfeld, M.3    van Roy, F.4    Green, K.J.5
  • 18
    • 44149127750 scopus 로고    scopus 로고
    • Plakophilin 2: a critical scaffold for PKCalpha that regulates intercellular junction assembly
    • This paper demonstrates a novel function for a PKP in the recruitment of a ubiquitous signaling protein, PKCα, to desmosomal precursors. PKP2 regulates cytoskeletal association of these precursors and is required for their proper assembly into junctions.
    • Bass-Zubek A.E., Hobbs R.P., Amargo E.V., Garcia N.J., Hsieh S.N., Chen X., Wahl J.K.I., Denning M.F., and Green K.J. Plakophilin 2: a critical scaffold for PKCalpha that regulates intercellular junction assembly. J Cell Biol 181 (2008) 605-613. This paper demonstrates a novel function for a PKP in the recruitment of a ubiquitous signaling protein, PKCα, to desmosomal precursors. PKP2 regulates cytoskeletal association of these precursors and is required for their proper assembly into junctions.
    • (2008) J Cell Biol , vol.181 , pp. 605-613
    • Bass-Zubek, A.E.1    Hobbs, R.P.2    Amargo, E.V.3    Garcia, N.J.4    Hsieh, S.N.5    Chen, X.6    Wahl, J.K.I.7    Denning, M.F.8    Green, K.J.9
  • 19
    • 0035076526 scopus 로고    scopus 로고
    • Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders
    • Bornslaeger E.A., Godsel L.M., Corcoran C.M., Park J.K., Hatzfeld M., Kowalczyk A.P., and Green K.J. Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders. J Cell Sci 114 (2001) 727-738
    • (2001) J Cell Sci , vol.114 , pp. 727-738
    • Bornslaeger, E.A.1    Godsel, L.M.2    Corcoran, C.M.3    Park, J.K.4    Hatzfeld, M.5    Kowalczyk, A.P.6    Green, K.J.7
  • 20
    • 0344559106 scopus 로고    scopus 로고
    • De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components
    • Koeser J., Troyanovsky S.M., Grund C., and Franke W.W. De novo formation of desmosomes in cultured cells upon transfection of genes encoding specific desmosomal components. Exp Cell Res 285 (2003) 114-130
    • (2003) Exp Cell Res , vol.285 , pp. 114-130
    • Koeser, J.1    Troyanovsky, S.M.2    Grund, C.3    Franke, W.W.4
  • 21
    • 33745219875 scopus 로고    scopus 로고
    • The carboxyl terminus of plakophilin-1 recruits it to the plasma membrane, whereas amino terminus recruits desmoplakin and promotes desmosome assembly
    • Sobolik-Delmaire T., Katafiasz D., and Wahl III J.K. The carboxyl terminus of plakophilin-1 recruits it to the plasma membrane, whereas amino terminus recruits desmoplakin and promotes desmosome assembly. J Biol Chem 281 (2006) 16962-16970
    • (2006) J Biol Chem , vol.281 , pp. 16962-16970
    • Sobolik-Delmaire, T.1    Katafiasz, D.2    Wahl III, J.K.3
  • 22
    • 0034020357 scopus 로고    scopus 로고
    • The alpha isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells
    • Wallis S., Lloyd S., Wise I., Ireland G., Fleming T.P., and Garrod D. The alpha isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells. Mol Biol Cell 11 (2000) 1077-1092
    • (2000) Mol Biol Cell , vol.11 , pp. 1077-1092
    • Wallis, S.1    Lloyd, S.2    Wise, I.3    Ireland, G.4    Fleming, T.P.5    Garrod, D.6
  • 23
    • 0030902371 scopus 로고    scopus 로고
    • Protein kinase C activation upregulates intercellular adhesion of alpha-catenin-negative human colon cancer cell variants via induction of desmosomes
    • van Hengel J., Gohon L., Bruyneel E., Vermeulen S., Cornelissen M., Mareel M., and von Roy F. Protein kinase C activation upregulates intercellular adhesion of alpha-catenin-negative human colon cancer cell variants via induction of desmosomes. J Cell Biol 137 (1997) 1103-1116
    • (1997) J Cell Biol , vol.137 , pp. 1103-1116
    • van Hengel, J.1    Gohon, L.2    Bruyneel, E.3    Vermeulen, S.4    Cornelissen, M.5    Mareel, M.6    von Roy, F.7
  • 24
    • 33845477045 scopus 로고    scopus 로고
    • p120-ctn: a nexus for contextual signaling via Rho GTPases
    • Anastasiadis P.Z. p120-ctn: a nexus for contextual signaling via Rho GTPases. Biochim Biophys Acta 1773 (2007) 34-46
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 34-46
    • Anastasiadis, P.Z.1
  • 26
    • 1342304120 scopus 로고    scopus 로고
    • p120 catenin associates with microtubules: inverse relationship between microtubule binding and Rho GTPase regulation
    • Franz C.M., and Ridley A.J. p120 catenin associates with microtubules: inverse relationship between microtubule binding and Rho GTPase regulation. J Biol Chem 279 (2004) 6588-6594
    • (2004) J Biol Chem , vol.279 , pp. 6588-6594
    • Franz, C.M.1    Ridley, A.J.2
  • 27
    • 63849176160 scopus 로고    scopus 로고
    • Microtubules and cadherins: a neglected partnership
    • Stehbens S.J., Akhmanova A., and Yap A.S. Microtubules and cadherins: a neglected partnership. Front Biosci 14 (2009) 3159-3167
    • (2009) Front Biosci , vol.14 , pp. 3159-3167
    • Stehbens, S.J.1    Akhmanova, A.2    Yap, A.S.3
  • 28
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • Meng W., Mushika Y., Ichii T., and Takeichi M. Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell 135 (2008) 948-959
    • (2008) Cell , vol.135 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 30
    • 66849106348 scopus 로고    scopus 로고
    • Targeting of p0071 to the midbody depends on KIF3
    • Keil R., Kießling C., and Hatzfeld M. Targeting of p0071 to the midbody depends on KIF3. J Cell Sci 122 (2009) 1174-1183
    • (2009) J Cell Sci , vol.122 , pp. 1174-1183
    • Keil, R.1    Kießling, C.2    Hatzfeld, M.3
  • 31
    • 0037164862 scopus 로고    scopus 로고
    • Intermediate filament-membrane attachments function synergistically with actin-dependent contacts to regulate intercellular adhesive strength
    • Huen A.C., Park J.K., Godsel L.M., Chen X., Bannon L.J., Amargo E.V., Hudson T.Y., Mongiu A.K., Leigh I.M., Kelsell D.P., et al. Intermediate filament-membrane attachments function synergistically with actin-dependent contacts to regulate intercellular adhesive strength. J Cell Biol 159 (2002) 1005-1017
    • (2002) J Cell Biol , vol.159 , pp. 1005-1017
    • Huen, A.C.1    Park, J.K.2    Godsel, L.M.3    Chen, X.4    Bannon, L.J.5    Amargo, E.V.6    Hudson, T.Y.7    Mongiu, A.K.8    Leigh, I.M.9    Kelsell, D.P.10
  • 33
    • 45249088344 scopus 로고    scopus 로고
    • p120 catenin is associated with desmogleins when desmosomes are assembled in high-Ca(2+) medium but not when disassembled in low-Ca(2+) medium in DJM-1 cells
    • Kanno M., Aoyama Y., Isa Y., Yamamoto Y., and Kitajima Y. p120 catenin is associated with desmogleins when desmosomes are assembled in high-Ca(2+) medium but not when disassembled in low-Ca(2+) medium in DJM-1 cells. J Dermatol 35 (2008) 317-324
    • (2008) J Dermatol , vol.35 , pp. 317-324
    • Kanno, M.1    Aoyama, Y.2    Isa, Y.3    Yamamoto, Y.4    Kitajima, Y.5
  • 34
    • 31344461886 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. I. Molecular definition in intercalated disks of cardiomyocytes by immunoelectron microsocopy of desmosomal proteins
    • Franke W.W., Borrmann C.M., Grund C., and Pieperhoff S. The area composita of adhering junctions connecting heart muscle cells of vertebrates. I. Molecular definition in intercalated disks of cardiomyocytes by immunoelectron microsocopy of desmosomal proteins. Eur J Cell Biol 85 (2006) 69-82
    • (2006) Eur J Cell Biol , vol.85 , pp. 69-82
    • Franke, W.W.1    Borrmann, C.M.2    Grund, C.3    Pieperhoff, S.4
  • 35
    • 2442532569 scopus 로고    scopus 로고
    • The intercalated disk as a single functional unit
    • Delmar M. The intercalated disk as a single functional unit. Heart Rhythm 1 (2004) 12-13
    • (2004) Heart Rhythm , vol.1 , pp. 12-13
    • Delmar, M.1
  • 36
    • 23744463471 scopus 로고    scopus 로고
    • Dependence of electrical coupling on mechanical coupling in cardiac myocytes: insights gained from cardiomyopathies caused by defects in cell-cell connections
    • Saffitz J.E. Dependence of electrical coupling on mechanical coupling in cardiac myocytes: insights gained from cardiomyopathies caused by defects in cell-cell connections. Ann NY Acad Sci 1047 (2005) 336-344
    • (2005) Ann NY Acad Sci , vol.1047 , pp. 336-344
    • Saffitz, J.E.1
  • 37
    • 0033597942 scopus 로고    scopus 로고
    • Spatiotemporal development and distribution of intercellular junctions in adult rat cardiomyocytes in culture
    • Kostin S., Hein S., Bauer E.P., and Schaper J. Spatiotemporal development and distribution of intercellular junctions in adult rat cardiomyocytes in culture. Circ Res 85 (1999) 154-167
    • (1999) Circ Res , vol.85 , pp. 154-167
    • Kostin, S.1    Hein, S.2    Bauer, E.P.3    Schaper, J.4
  • 38
    • 34250811969 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. IV. Coalescence and amalgamation of desmosomal and adherens junction components-late processes in mammalian heart development
    • This article demonstrates that the mixed cardiac adhesion junctions, the area composita, coalesce from once distant complexes, desmosomes and adherens junctions, as cardiac tissue matures.
    • Pieperhoff S., and Franke W.W. The area composita of adhering junctions connecting heart muscle cells of vertebrates. IV. Coalescence and amalgamation of desmosomal and adherens junction components-late processes in mammalian heart development. Eur J Cell Biol 86 (2007) 377-391. This article demonstrates that the mixed cardiac adhesion junctions, the area composita, coalesce from once distant complexes, desmosomes and adherens junctions, as cardiac tissue matures.
    • (2007) Eur J Cell Biol , vol.86 , pp. 377-391
    • Pieperhoff, S.1    Franke, W.W.2
  • 39
    • 34347364710 scopus 로고    scopus 로고
    • A unique and specific interaction between {alpha}T-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs
    • This article demonstrates a cardiac specific co-localization of, and interaction between PKP2 and α-catenin, suggesting a potential mechanism by which mixed cardiac junctions occur.
    • Goossens S., Janssens B., Bonne S., De Ryke R., Braet F., van Hengel J., and van Roy F. A unique and specific interaction between {alpha}T-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs. J Cell Sci 120 (2007) 2126-2136. This article demonstrates a cardiac specific co-localization of, and interaction between PKP2 and α-catenin, suggesting a potential mechanism by which mixed cardiac junctions occur.
    • (2007) J Cell Sci , vol.120 , pp. 2126-2136
    • Goossens, S.1    Janssens, B.2    Bonne, S.3    De Ryke, R.4    Braet, F.5    van Hengel, J.6    van Roy, F.7
  • 41
    • 44449156929 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNA-mediated knockdown in cultured rat cardiomyocytes
    • This article demonstrates that RNAi-mediated loss of PKP2 expression led to the disintegration of area compositae in the intercalated junctions of neonatal rat cardiomyocytes.
    • Pieperhoff S., Schumacher H., and Franke W.W. The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNA-mediated knockdown in cultured rat cardiomyocytes. Eur J Cell Biol 87 (2008) 399-411. This article demonstrates that RNAi-mediated loss of PKP2 expression led to the disintegration of area compositae in the intercalated junctions of neonatal rat cardiomyocytes.
    • (2008) Eur J Cell Biol , vol.87 , pp. 399-411
    • Pieperhoff, S.1    Schumacher, H.2    Franke, W.W.3
  • 42
    • 34848820956 scopus 로고    scopus 로고
    • Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells
    • This article is the first to demonstrate a direct interaction between PKP2 and gap junction protein connexin43, and provides supporting evidence for the idea that the pathogenetic mechanism of PKP2-related ARVC may be due to disruption of cardiac myocyte coupling.
    • Oxford E.M., Musa H., Maass K., Coombs W., Taffet S.M., and Delmar M. Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells. Circ Res 101 (2007) 703-711. This article is the first to demonstrate a direct interaction between PKP2 and gap junction protein connexin43, and provides supporting evidence for the idea that the pathogenetic mechanism of PKP2-related ARVC may be due to disruption of cardiac myocyte coupling.
    • (2007) Circ Res , vol.101 , pp. 703-711
    • Oxford, E.M.1    Musa, H.2    Maass, K.3    Coombs, W.4    Taffet, S.M.5    Delmar, M.6
  • 44
    • 4143119057 scopus 로고    scopus 로고
    • Comparative analysis of armadillo family proteins in the regulation of A431 epithelial cell junction assembly, adhesion and migration
    • Setzer S.V., Calkins C.C., Garner J., Summers S., Green K.J., and Kowalczyk A.P. Comparative analysis of armadillo family proteins in the regulation of A431 epithelial cell junction assembly, adhesion and migration. J Invest Dermatol 123 (2004) 426-433
    • (2004) J Invest Dermatol , vol.123 , pp. 426-433
    • Setzer, S.V.1    Calkins, C.C.2    Garner, J.3    Summers, S.4    Green, K.J.5    Kowalczyk, A.P.6
  • 45
    • 0034932143 scopus 로고    scopus 로고
    • Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2
    • Mertens C., Hofmann I., Wang Z., Teichmann M., Chong S.S., Schnolzer M., and Franke W.W. Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2. Proc Natl Acad Sci 98 (2001) 7795-7800
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 7795-7800
    • Mertens, C.1    Hofmann, I.2    Wang, Z.3    Teichmann, M.4    Chong, S.S.5    Schnolzer, M.6    Franke, W.W.7
  • 46
    • 0042738101 scopus 로고    scopus 로고
    • Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate
    • Muller J., Ritt D.A., Copeland T.D., and Morrison D.K. Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate. EMBO J 22 (2003) 4431-4442
    • (2003) EMBO J , vol.22 , pp. 4431-4442
    • Muller, J.1    Ritt, D.A.2    Copeland, T.D.3    Morrison, D.K.4
  • 47
    • 33644854767 scopus 로고    scopus 로고
    • Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules
    • Hofmann I., Casella M., Schnolzer M., Schlechter T., Spring H., and Franke W.W. Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules. Mol Biol Cell 17 (2006) 1388-1398
    • (2006) Mol Biol Cell , vol.17 , pp. 1388-1398
    • Hofmann, I.1    Casella, M.2    Schnolzer, M.3    Schlechter, T.4    Spring, H.5    Franke, W.W.6
  • 48
    • 0034703093 scopus 로고    scopus 로고
    • PAPIN. A novel multiple PSD-95/Dlg-A/ZO-1 protein interacting with neural plakophilin-related armadillo repeat protein/delta-catenin and p0071
    • Deguchi M., Iizuka T., Hata Y., Nishimura W., Hirao K., Yao I., Kawabe H., and Takai Y. PAPIN. A novel multiple PSD-95/Dlg-A/ZO-1 protein interacting with neural plakophilin-related armadillo repeat protein/delta-catenin and p0071. J Biol Chem 275 (2000) 29875-29880
    • (2000) J Biol Chem , vol.275 , pp. 29875-29880
    • Deguchi, M.1    Iizuka, T.2    Hata, Y.3    Nishimura, W.4    Hirao, K.5    Yao, I.6    Kawabe, H.7    Takai, Y.8
  • 49
    • 0037057290 scopus 로고    scopus 로고
    • Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells
    • Ohno H., Hirabayashi S., Iizuka T., Ohnishi H., Fujita T., and Hata Y. Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells. Oncogene 21 (2002) 7042-7049
    • (2002) Oncogene , vol.21 , pp. 7042-7049
    • Ohno, H.1    Hirabayashi, S.2    Iizuka, T.3    Ohnishi, H.4    Fujita, T.5    Hata, Y.6
  • 51
    • 0036100483 scopus 로고    scopus 로고
    • ERBIN associates with p0071, an armadillo protein, at cell-cell junctions of epithelial cells
    • Izawa I., Nishizawa M., Tomono Y., Ohtakara K., Takahashi T., and Inagaki M. ERBIN associates with p0071, an armadillo protein, at cell-cell junctions of epithelial cells. Genes Cells 7 (2002) 475-485
    • (2002) Genes Cells , vol.7 , pp. 475-485
    • Izawa, I.1    Nishizawa, M.2    Tomono, Y.3    Ohtakara, K.4    Takahashi, T.5    Inagaki, M.6
  • 59
    • 59749097091 scopus 로고    scopus 로고
    • Characterization of the molecular phenotype of two arrhythmogenic right ventricular cardiomyopathy (ARVC)-related plakophilin-2 (PKP2) mutations
    • This article investigates the molecular mechanism underlying ARVC via ectopic expression of ARVC-mutant PKP2. Disruption of interactions between mutant PKP2 and junctional proteins leads to reduced connexin43 and HSP90 expression.
    • Joshi-Mukherjee R., Coombs W., Musa H., Oxford E., Taffet S., and Delmar M. Characterization of the molecular phenotype of two arrhythmogenic right ventricular cardiomyopathy (ARVC)-related plakophilin-2 (PKP2) mutations. Heart Rhythm 5 (2008) 1715-1723. This article investigates the molecular mechanism underlying ARVC via ectopic expression of ARVC-mutant PKP2. Disruption of interactions between mutant PKP2 and junctional proteins leads to reduced connexin43 and HSP90 expression.
    • (2008) Heart Rhythm , vol.5 , pp. 1715-1723
    • Joshi-Mukherjee, R.1    Coombs, W.2    Musa, H.3    Oxford, E.4    Taffet, S.5    Delmar, M.6
  • 60
    • 33745848407 scopus 로고    scopus 로고
    • Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy
    • Garcia-Gras E., Lombardi R., Giocondo M.J., Willerson J.T., Schneider M.D., Khoury D.S., and Marian A.J. Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy. J Clin Invest 116 (2006) 2012-2021
    • (2006) J Clin Invest , vol.116 , pp. 2012-2021
    • Garcia-Gras, E.1    Lombardi, R.2    Giocondo, M.J.3    Willerson, J.T.4    Schneider, M.D.5    Khoury, D.S.6    Marian, A.J.7
  • 61
    • 4444317085 scopus 로고    scopus 로고
    • Regulation of cadherin stability and turnover by p120ctn: implications in disease and cancer
    • Reynolds A.B., and Carnahan R.H. Regulation of cadherin stability and turnover by p120ctn: implications in disease and cancer. Sem Cell Dev Biol 15 (2004) 657-663
    • (2004) Sem Cell Dev Biol , vol.15 , pp. 657-663
    • Reynolds, A.B.1    Carnahan, R.H.2
  • 65
    • 0038207089 scopus 로고    scopus 로고
    • Immunohistochemical localization of plakophilins (PKP1, PKP2, PKP3, and p0071) in primary oropharyngeal tumors: correlation with clinical parameters
    • Papagerakis S., Shabana A.H., Depondt J., Gehanno P., and Forest N. Immunohistochemical localization of plakophilins (PKP1, PKP2, PKP3, and p0071) in primary oropharyngeal tumors: correlation with clinical parameters. Hum Pathol 34 (2003) 565-572
    • (2003) Hum Pathol , vol.34 , pp. 565-572
    • Papagerakis, S.1    Shabana, A.H.2    Depondt, J.3    Gehanno, P.4    Forest, N.5
  • 67
    • 59849124834 scopus 로고    scopus 로고
    • Regulation of cadherin trafficking
    • Delva E., and Kowalczyk A.P. Regulation of cadherin trafficking. Traffic 10 (2009) 259-267
    • (2009) Traffic , vol.10 , pp. 259-267
    • Delva, E.1    Kowalczyk, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.