메뉴 건너뛰기




Volumn 127, Issue 17, 2014, Pages 3782-3793

Palmitoylation of plakophilin is required for desmosome assembly

Author keywords

Desmosome; Palmitoylation; Plakophilin

Indexed keywords

DESMOPLAKIN; PLAKOGLOBIN; PLAKOPHILIN;

EID: 84906861959     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.149849     Document Type: Article
Times cited : (27)

References (58)
  • 2
    • 33644863162 scopus 로고    scopus 로고
    • Desmoglein 4 is expressed in highly differentiated keratinocytes and trichocytes in human epidermis and hair follicle
    • Bazzi, H., Getz, A., Mahoney, M. G., Ishida-Yamamoto, A., Langbein, L., Wahl, J. K., 3rd and Christiano, A. M. (2006). Desmoglein 4 is expressed in highly differentiated keratinocytes and trichocytes in human epidermis and hair follicle. Differentiation 74, 129-140.
    • (2006) Differentiation , vol.74 , pp. 129-140
    • Bazzi, H.1    Getz, A.2    Mahoney, M.G.3    Ishida-Yamamoto, A.4    Langbein, L.5    Wahl III, J.K.6    Christiano, A.M.7
  • 7
    • 82755194912 scopus 로고    scopus 로고
    • Cell-cell connectivity: desmosomes and disease
    • Brooke, M. A., Nitoiu, D. and Kelsell, D. P. (2012). Cell-cell connectivity: desmosomes and disease. J. Pathol. 226, 158-171.
    • (2012) J. Pathol. , vol.226 , pp. 158-171
    • Brooke, M.A.1    Nitoiu, D.2    Kelsell, D.P.3
  • 8
    • 0032526941 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion
    • Calautti, E., Cabodi, S., Stein, P. L., Hatzfeld, M., Kedersha, N. and Paolo Dotto, G. (1998). Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion. J. Cell Biol. 141, 1449-1465.
    • (1998) J. Cell Biol. , vol.141 , pp. 1449-1465
    • Calautti, E.1    Cabodi, S.2    Stein, P.L.3    Hatzfeld, M.4    Kedersha, N.5    Paolo Dotto, G.6
  • 10
    • 12344281930 scopus 로고    scopus 로고
    • Structure of the armadillo repeat domain of plakophilin 1
    • Choi, H. J. and Weis, W. I. (2005). Structure of the armadillo repeat domain of plakophilin 1. J. Mol. Biol. 346, 367-376.
    • (2005) J. Mol. Biol. , vol.346 , pp. 367-376
    • Choi, H.J.1    Weis, W.I.2
  • 11
    • 0025821552 scopus 로고
    • Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains
    • Collins, J. E., Legan, P. K., Kenny, T. P., MacGarvie, J., Holton, J. L. and Garrod, D. R. (1991). Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains. J. Cell Biol. 113, 381-391.
    • (1991) J. Cell Biol. , vol.113 , pp. 381-391
    • Collins, J.E.1    Legan, P.K.2    Kenny, T.P.3    MacGarvie, J.4    Holton, J.L.5    Garrod, D.R.6
  • 13
    • 0033152139 scopus 로고    scopus 로고
    • The immunohistochemical expression of desmoplakin and its role in vivo in the progression and metastasis of breast cancer
    • Davies, E. L., Gee, J. M., Cochrane, R. A., Jiang, W. G., Sharma, A. K., Nicholson, R. I. and Mansel, R. E. (1999). The immunohistochemical expression of desmoplakin and its role in vivo in the progression and metastasis of breast cancer. Eur. J. Cancer 35, 902-907.
    • (1999) Eur. J. Cancer , vol.35 , pp. 902-907
    • Davies, E.L.1    Gee, J.M.2    Cochrane, R.A.3    Jiang, W.G.4    Sharma, A.K.5    Nicholson, R.I.6    Mansel, R.E.7
  • 14
    • 0026331302 scopus 로고
    • Both the 59 untranslated region and the sequences surrounding the start site contribute to efficient initiation of translation in vitro
    • Falcone, D. and Andrews, D. W. (1991). Both the 59 untranslated region and the sequences surrounding the start site contribute to efficient initiation of translation in vitro. Mol. Cell. Biol. 11, 2656-2664.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2656-2664
    • Falcone, D.1    Andrews, D.W.2
  • 15
    • 0031589555 scopus 로고    scopus 로고
    • Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains
    • Feil, R., Wagner, J., Metzger, D. and Chambon, P. (1997). Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains. Biochem. Biophys. Res. Commun. 237, 752-757.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 752-757
    • Feil, R.1    Wagner, J.2    Metzger, D.3    Chambon, P.4
  • 16
  • 18
    • 79955649200 scopus 로고    scopus 로고
    • DHHC palmitoyl transferases: substrate interactions and (patho)physiology
    • Greaves, J. and Chamberlain, L. H. (2011). DHHC palmitoyl transferases: substrate interactions and (patho)physiology. Trends Biochem. Sci. 36, 245-253.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 245-253
    • Greaves, J.1    Chamberlain, L.H.2
  • 19
    • 72149099859 scopus 로고    scopus 로고
    • Arrhythmogenic right ventricular cardiomyopathy plakophilin-2 mutations disrupt desmosome assembly and stability
    • Hall, C., Li, S., Li, H., Creason, V. and Wahl, J. K., 3rd (2009). Arrhythmogenic right ventricular cardiomyopathy plakophilin-2 mutations disrupt desmosome assembly and stability. Cell Commun. Adhes. 16, 15-27.
    • (2009) Cell Commun. Adhes. , vol.16 , pp. 15-27
    • Hall, C.1    Li, S.2    Li, H.3    Creason, V.4    Wahl III, J.K.5
  • 21
    • 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. (2000). The function of plakophilin 1 in desmosome assembly and actin filament organization. J. Cell Biol. 149, 209-222.
    • (2000) J. Cell Biol. , vol.149 , pp. 209-222
    • Hatzfeld, M.1    Haffner, C.2    Schulze, K.3    Vinzens, U.4
  • 22
    • 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. (2002). Intermediate filament-membrane attachments function synergistically with actin-dependent contacts to regulate intercellular adhesive strength. J. Cell Biol. 159, 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
  • 25
    • 0025736474 scopus 로고
    • Amino acid sequence of bovine muzzle epithelial desmocollin derived from cloned cDNA: a novel subtype of desmosomal cadherins
    • Koch, P. J., Goldschmidt, M. D., Walsh, M. J., Zimbelmann, R., Schmelz, M. and Franke, W. W. (1991). Amino acid sequence of bovine muzzle epithelial desmocollin derived from cloned cDNA: a novel subtype of desmosomal cadherins. Differentiation 47, 29-36.
    • (1991) Differentiation , vol.47 , pp. 29-36
    • Koch, P.J.1    Goldschmidt, M.D.2    Walsh, M.J.3    Zimbelmann, R.4    Schmelz, M.5    Franke, W.W.6
  • 27
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin, B. R. and Cravatt, B. F. (2009). Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6, 135-138.
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 29
    • 84906868159 scopus 로고    scopus 로고
    • Lipid Rafts and Detergent-Resistant Membranes in Epithelial Keratinocytes
    • McGuinn, K. P. and Mahoney, M. G. (2014). Lipid Rafts and Detergent-Resistant Membranes in Epithelial Keratinocytes. Methods Mol. Biol.
    • (2014) Methods Mol. Biol.
    • McGuinn, K.P.1    Mahoney, M.G.2
  • 30
    • 0033014334 scopus 로고    scopus 로고
    • Mechanism of extracellular domain-deleted dominant negative cadherins
    • Nieman, M. T., Kim, J. B., Johnson, K. R. and Wheelock, M. J. (1999). Mechanism of extracellular domain-deleted dominant negative cadherins. J. Cell Sci. 112, 1621-1632.
    • (1999) J. Cell Sci. , vol.112 , pp. 1621-1632
    • Nieman, M.T.1    Kim, J.B.2    Johnson, K.R.3    Wheelock, M.J.4
  • 32
    • 84870478193 scopus 로고    scopus 로고
    • Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
    • Ohno, Y., Kashio, A., Ogata, R., Ishitomi, A., Yamazaki, Y. and Kihara, A. (2012). Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system. Mol. Biol. Cell 23, 4543-4551.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4543-4551
    • Ohno, Y.1    Kashio, A.2    Ogata, R.3    Ishitomi, A.4    Yamazaki, Y.5    Kihara, A.6
  • 33
    • 54249148026 scopus 로고    scopus 로고
    • CSS-Palm 2. 0: an updated software for palmitoylation sites prediction
    • Ren, J., Wen, L., Gao, X., Jin, C., Xue, Y. and Yao, X. (2008). CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng. Des. Sel. 21, 639-644.
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 34
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh, M. D. (2006). Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, re14.
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 35
    • 78651404102 scopus 로고    scopus 로고
    • Desmosome assembly and cell-cell adhesion are membrane raftdependent processes
    • Resnik, N., Sepcic, K., Plemenitas, A., Windoffer, R., Leube, R. and Veranic, P. (2011). Desmosome assembly and cell-cell adhesion are membrane raftdependent processes. J. Biol. Chem. 286, 1499-1507.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1499-1507
    • Resnik, N.1    Sepcic, K.2    Plemenitas, A.3    Windoffer, R.4    Leube, R.5    Veranic, P.6
  • 36
    • 82555187993 scopus 로고    scopus 로고
    • Desmosome dynamics in migrating epithelial cells requires the actin cytoskeleton
    • Roberts, B. J., Pashaj, A., Johnson, K. R. and Wahl, J. K., III (2011). Desmosome dynamics in migrating epithelial cells requires the actin cytoskeleton. Exp. Cell Res. 317, 2814-2822.
    • (2011) Exp. Cell Res. , vol.317 , pp. 2814-2822
    • Roberts, B.J.1    Pashaj, A.2    Johnson, K.R.3    Wahl III, J.K.4
  • 37
    • 84885045091 scopus 로고    scopus 로고
    • Stratifin (14-3-3 s) limits plakophilin-3 exchange with the desmosomal plaque
    • Roberts, B. J., Reddy, R. and Wahl, J. K., III (2013). Stratifin (14-3-3 s) limits plakophilin-3 exchange with the desmosomal plaque. PLoS ONE 8, e77012.
    • (2013) PLoS ONE , vol.8
    • Roberts, B.J.1    Reddy, R.2    Wahl III, J.K.3
  • 38
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteinerich domain protein Akr1p is a palmitoyl transferase
    • Roth, A. F., Feng, Y., Chen, L. and Davis, N. G. (2002). The yeast DHHC cysteinerich domain protein Akr1p is a palmitoyl transferase. J. Cell Biol. 159, 23-28.
    • (2002) J. Cell Biol. , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 40
    • 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. (2004). Comparative analysis of armadillo family proteins in the regulation of a431 epithelial cell junction assembly, adhesion and migration. J. Invest. Dermatol. 123, 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
  • 41
    • 33745219875 scopus 로고    scopus 로고
    • Carboxyl terminus of Plakophilin-1 recruits it to plasma membrane, whereas amino terminus recruits desmoplakin and promotes desmosome assembly
    • Sobolik-Delmaire, T., Katafiasz, D. and Wahl, J. K., III (2006). Carboxyl terminus of Plakophilin-1 recruits it to plasma membrane, whereas amino terminus recruits desmoplakin and promotes desmosome assembly. J. Biol. Chem. 281, 16962-16970.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16962-16970
    • Sobolik-Delmaire, T.1    Katafiasz, D.2    Wahl III, J.K.3
  • 42
    • 34547675938 scopus 로고    scopus 로고
    • Decreased plakophilin-1 expression promotes increased motility in head and neck squamous cell carcinoma cells
    • Sobolik-Delmaire, T., Katafiasz, D., Keim, S. A., Mahoney, M. G. and Wahl, J. K., III (2007). Decreased plakophilin-1 expression promotes increased motility in head and neck squamous cell carcinoma cells. Cell Commun. Adhes. 14, 99-109.
    • (2007) Cell Commun. Adhes. , vol.14 , pp. 99-109
    • Sobolik-Delmaire, T.1    Katafiasz, D.2    Keim, S.A.3    Mahoney, M.G.4    Wahl III, J.K.5
  • 44
    • 0029979539 scopus 로고    scopus 로고
    • Purification, cDNA cloning, and regulation of lysophospholipase from rat liver
    • Sugimoto, H., Hayashi, H. and Yamashita, S. (1996). Purification, cDNA cloning, and regulation of lysophospholipase from rat liver. J. Biol. Chem. 271, 7705-7711.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7705-7711
    • Sugimoto, H.1    Hayashi, H.2    Yamashita, S.3
  • 46
    • 84862016040 scopus 로고    scopus 로고
    • Direct evidence that PKCa positively regulates wound re-epithelialization: correlation with changes in desmosomal adhesiveness
    • Thomason, H. A., Cooper, N. H., Ansell, D. M., Chiu, M., Merrit, A. J., Hardman, M. J. and Garrod, D. R. (2012). Direct evidence that PKCa positively regulates wound re-epithelialization: correlation with changes in desmosomal adhesiveness. J. Pathol. 227, 346-356.
    • (2012) J. Pathol. , vol.227 , pp. 346-356
    • Thomason, H.A.1    Cooper, N.H.2    Ansell, D.M.3    Chiu, M.4    Merrit, A.J.5    Hardman, M.J.6    Garrod, D.R.7
  • 47
    • 84860374340 scopus 로고    scopus 로고
    • Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels
    • Tian, L., McClafferty, H., Knaus, H. G., Ruth, P. and Shipston, M. J. (2012). Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels. J. Biol. Chem. 287, 14718-14725.
    • (2012) J. Biol. Chem. , vol.287 , pp. 14718-14725
    • Tian, L.1    McClafferty, H.2    Knaus, H.G.3    Ruth, P.4    Shipston, M.J.5
  • 48
    • 78649789580 scopus 로고    scopus 로고
    • Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43
    • Tomatis, V. M., Trenchi, A., Gomez, G. A. and Daniotti, J. L. (2010). Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43. PLoS ONE 5, e15045.
    • (2010) PLoS ONE , vol.5
    • Tomatis, V.M.1    Trenchi, A.2    Gomez, G.A.3    Daniotti, J.L.4
  • 49
    • 0033602204 scopus 로고    scopus 로고
    • Sequence, expression in Escherichia coli, and characterization of lysophospholipase II
    • Toyoda, T., Sugimoto, H. and Yamashita, S. (1999). Sequence, expression in Escherichia coli, and characterization of lysophospholipase II. Biochim. Biophys. Acta 1437, 182-193.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 182-193
    • Toyoda, T.1    Sugimoto, H.2    Yamashita, S.3
  • 50
    • 0035885077 scopus 로고    scopus 로고
    • Enzymatic depalmitoylation of viral glycoproteins with acyl-protein thioesterase 1 in vitro
    • Veit, M. and Schmidt, M. F. (2001). Enzymatic depalmitoylation of viral glycoproteins with acyl-protein thioesterase 1 in vitro. Virology 288, 89-95.
    • (2001) Virology , vol.288 , pp. 89-95
    • Veit, M.1    Schmidt, M.F.2
  • 51
    • 0036075759 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies specific for desmoglein family members
    • Wahl, J. K., 3rd (2002). Generation of monoclonal antibodies specific for desmoglein family members. Hybrid. Hybridomics 21, 37-44.
    • (2002) Hybrid. Hybridomics , vol.21 , pp. 37-44
    • Wahl III, J.K.1
  • 52
    • 26444498679 scopus 로고    scopus 로고
    • A role for plakophilin-1 in the initiation of desmosome assembly
    • Wahl, J. K., 3rd (2005). A role for plakophilin-1 in the initiation of desmosome assembly. J. Cell. Biochem. 96, 390-403.
    • (2005) J. Cell. Biochem. , vol.96 , pp. 390-403
    • Wahl III, J.K.1
  • 53
    • 0029941032 scopus 로고    scopus 로고
    • Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: identification of unique and shared domains
    • Wahl, J. K., Sacco, P. A., McGranahan-Sadler, T. M., Sauppé, L. M., Wheelock, M. J. and Johnson, K. R. (1996). Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: identification of unique and shared domains. J. Cell Sci. 109, 1143-1154.
    • (1996) J. Cell Sci. , vol.109 , pp. 1143-1154
    • Wahl, J.K.1    Sacco, P.A.2    McGranahan-Sadler, T.M.3    Sauppé, L.M.4    Wheelock, M.J.5    Johnson, K.R.6
  • 54
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: purification and identification
    • Wan, J., Roth, A. F., Bailey, A. O. and Davis, N. G. (2007). Palmitoylated proteins: purification and identification. Nat. Protoc. 2, 1573-1584.
    • (2007) Nat. Protoc. , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 56
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raftenriched and non-raft membranes
    • Yang, W., Di Vizio, D., Kirchner, M., Steen, H. and Freeman, M. R. (2010). Proteome scale characterization of human S-acylated proteins in lipid raftenriched and non-raft membranes. Mol. Cell. Proteomics 9, 54-70.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.