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Volumn 90, Issue 5, 2011, Pages 390-400

Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin

Author keywords

Desmin; Intermediate filaments; Plakin; Plectin; Vimentin

Indexed keywords

DESMIN; PLAKIN; PLECTIN; VIMENTIN;

EID: 79952361967     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2010.11.013     Document Type: Article
Times cited : (42)

References (54)
  • 1
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andrä K., Lassmann H., Bittner R., Shorny S., Fassler R., Propst F., Wiche G. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 1997, 11:3143-3156.
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassler, R.5    Propst, F.6    Wiche, G.7
  • 3
    • 33646144211 scopus 로고    scopus 로고
    • Forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation
    • Bär H., Kostareva A., Sjöberg G., Sejersen T., Katus H.A., Herrmann H. Forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation. Exp. Cell Res. 2006, 312:1554-1565.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1554-1565
    • Bär, H.1    Kostareva, A.2    Sjöberg, G.3    Sejersen, T.4    Katus, H.A.5    Herrmann, H.6
  • 4
    • 27244439232 scopus 로고    scopus 로고
    • Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages
    • Bär H., Mucke N., Kostareva A., Sjöberg G., Aebi U., Herrmann H. Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:15099-15104.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15099-15104
    • Bär, H.1    Mucke, N.2    Kostareva, A.3    Sjöberg, G.4    Aebi, U.5    Herrmann, H.6
  • 7
    • 0030966537 scopus 로고    scopus 로고
    • Desmin in muscle formation and maintenance: knockouts and consequences
    • Capetanaki Y., Milner D.J., Weitzer G. Desmin in muscle formation and maintenance: knockouts and consequences. Cell Struct. Funct. 1997, 22:103-116.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 103-116
    • Capetanaki, Y.1    Milner, D.J.2    Weitzer, G.3
  • 9
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner R., Leichtfried F.E., Herrmann H., Small J.V., Lawson D., Wiche G. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 1988, 106:723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 10
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • Foisner R., Malecz N., Dressel N., Stadler C., Wiche G. M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol. Biol. Cell 1996, 7:273-288.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 11
    • 0038247863 scopus 로고    scopus 로고
    • Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus
    • Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L. Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus. Mol. Biol. Cell 2003, 14:1978-1992.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1978-1992
    • Fontao, L.1    Favre, B.2    Riou, S.3    Geerts, D.4    Jaunin, F.5    Saurat, J.H.6    Green, K.J.7    Sonnenberg, A.8    Borradori, L.9
  • 12
    • 0035066688 scopus 로고    scopus 로고
    • Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature
    • Gallicano G.I., Bauer C., Fuchs E. Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature. Development 2001, 128:929-941.
    • (2001) Development , vol.128 , pp. 929-941
    • Gallicano, G.I.1    Bauer, C.2    Fuchs, E.3
  • 13
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts D., Fontao L., Nievers M.G., Schaapveld R.Q., Purkis P.E., Wheeler G.N., Lane E.B., Leigh I.M., Sonnenberg A. Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 1999, 147:417-434.
    • (1999) J. Cell Biol. , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 14
    • 68849104798 scopus 로고    scopus 로고
    • Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease
    • Goldfarb L.G., Dalakas M.C. Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease. J. Clin. Invest. 2009, 119:1806-1813.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1806-1813
    • Goldfarb, L.G.1    Dalakas, M.C.2
  • 16
    • 0022538727 scopus 로고
    • Absence of intermediate filaments in a human adrenal cortex carcinoma-derived cell line
    • Hedberg K.K., Chen L.B. Absence of intermediate filaments in a human adrenal cortex carcinoma-derived cell line. Exp. Cell Res. 1986, 163:509-517.
    • (1986) Exp. Cell Res. , vol.163 , pp. 509-517
    • Hedberg, K.K.1    Chen, L.B.2
  • 17
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 2004, 73:749-789.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 19
    • 0023126564 scopus 로고
    • Plectin and IFAP-300k are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • Herrmann H., Wiche G. Plectin and IFAP-300k are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J. Biol. Chem. 1987, 262:1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 20
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata T., Murakami T., Imamura M., Fujimaki N., Ishikawa H. Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 1999, 112:867-876.
    • (1999) J. Cell Sci. , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 21
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • Hijikata T., Murakami T., Ishikawa H., Yorifuji H. Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem. Cell Biol. 2003, 119:109-123.
    • (2003) Histochem. Cell Biol. , vol.119 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 23
    • 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., Herrmann H. Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. J. Cell Sci. 2000, 113:2471-2483.
    • (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
  • 24
    • 0030853151 scopus 로고    scopus 로고
    • Tetracycline regulated expression of vimentin in fibroblasts derived from vimentin null mice
    • Holwell T.A., Schweitzer S.C., Evans R.M. Tetracycline regulated expression of vimentin in fibroblasts derived from vimentin null mice. J. Cell Sci. 1997, 110:1947-1956.
    • (1997) J. Cell Sci. , vol.110 , pp. 1947-1956
    • Holwell, T.A.1    Schweitzer, S.C.2    Evans, R.M.3
  • 25
    • 0037115692 scopus 로고    scopus 로고
    • Interaction of periplakin and envoplakin with intermediate filaments
    • Karashima T., Watt F.M. Interaction of periplakin and envoplakin with intermediate filaments. J. Cell Sci. 2002, 115:5027-5037.
    • (2002) J. Cell Sci. , vol.115 , pp. 5027-5037
    • Karashima, T.1    Watt, F.M.2
  • 26
    • 0036781634 scopus 로고    scopus 로고
    • Unique role for the periplakin tail in intermediate filament association: specific binding to keratin 8 and vimentin
    • Kazerounian S., Uitto J., Aho S. Unique role for the periplakin tail in intermediate filament association: specific binding to keratin 8 and vimentin. Exp. Dermatol. 2002, 11:428-438.
    • (2002) Exp. Dermatol. , vol.11 , pp. 428-438
    • Kazerounian, S.1    Uitto, J.2    Aho, S.3
  • 28
    • 0021828069 scopus 로고
    • Identification and spatial arrangement of high molecular weight proteins (Mr 300000-330000) co-assembling with microtubules from a cultured cell line (rat glioma C6)
    • Koszka C., Leichtfried F.E., Wiche G. Identification and spatial arrangement of high molecular weight proteins (Mr 300000-330000) co-assembling with microtubules from a cultured cell line (rat glioma C6). Eur. J. Cell Biol. 1985, 38:149-156.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 149-156
    • Koszka, C.1    Leichtfried, F.E.2    Wiche, G.3
  • 30
    • 0034534608 scopus 로고    scopus 로고
    • Supplementation of a mutant keratin by stable expression of desmin in cultured human EBS keratinocytes
    • Magin T.M., Kaiser H.W., Leitgeb S., Grund C., Leigh I.M., Morley S.M., Lane E.B. Supplementation of a mutant keratin by stable expression of desmin in cultured human EBS keratinocytes. J. Cell Sci. 2000, 113:4231-4239.
    • (2000) J. Cell Sci. , vol.113 , pp. 4231-4239
    • Magin, T.M.1    Kaiser, H.W.2    Leitgeb, S.3    Grund, C.4    Leigh, I.M.5    Morley, S.M.6    Lane, E.B.7
  • 31
    • 51349101743 scopus 로고    scopus 로고
    • A missense mutation in desmin tail domain linked to human dilated cardiomyopathy promotes cleavage of the head domain and abolishes its Z-disc localization
    • Mavroidis M., Panagopoulou P., Kostavasili I., Weisleder N., Capetanaki Y. A missense mutation in desmin tail domain linked to human dilated cardiomyopathy promotes cleavage of the head domain and abolishes its Z-disc localization. FASEB J. 2008, 22:3318-3327.
    • (2008) FASEB J. , vol.22 , pp. 3318-3327
    • Mavroidis, M.1    Panagopoulou, P.2    Kostavasili, I.3    Weisleder, N.4    Capetanaki, Y.5
  • 34
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic B., Mac Nulty E., Mir B., Wiche G. Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J. Cell Biol. 1996, 134:1455-1467.
    • (1996) J. Cell Biol. , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 35
    • 6344260556 scopus 로고    scopus 로고
    • Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle
    • Paulin D., Li Z. Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp. Cell Res. 2004, 301:1-7.
    • (2004) Exp. Cell Res. , vol.301 , pp. 1-7
    • Paulin, D.1    Li, Z.2
  • 36
    • 16844381122 scopus 로고    scopus 로고
    • Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations
    • Pfendner E., Rouan F., Uitto J. Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations. Exp. Dermatol. 2005, 14:241-249.
    • (2005) Exp. Dermatol. , vol.14 , pp. 241-249
    • Pfendner, E.1    Rouan, F.2    Uitto, J.3
  • 37
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • Reipert S., Steinbock F., Fischer I., Bittner R.E., Zeold A., Wiche G. Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 1999, 252:479-491.
    • (1999) Exp. Cell Res. , vol.252 , pp. 479-491
    • Reipert, S.1    Steinbock, F.2    Fischer, I.3    Bittner, R.E.4    Zeold, A.5    Wiche, G.6
  • 38
    • 0344668724 scopus 로고    scopus 로고
    • Plectin 5′-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms
    • Rezniczek G.A., Abrahamsberg C., Fuchs P., Spazierer D., Wiche G. Plectin 5′-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum. Mol. Genet. 2003, 12:3181-3194.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3181-3194
    • Rezniczek, G.A.1    Abrahamsberg, C.2    Fuchs, P.3    Spazierer, D.4    Wiche, G.5
  • 43
    • 3042778127 scopus 로고    scopus 로고
    • A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation
    • Sjöberg G., Saavedra-Matiz C.A., Rosen D.R., Wijsman E.M., Borg K., Horowitz S.H., Sejersen T. A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation. Hum. Mol. Genet. 1999, 8:2191-2198.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2191-2198
    • Sjöberg, G.1    Saavedra-Matiz, C.A.2    Rosen, D.R.3    Wijsman, E.M.4    Borg, K.5    Horowitz, S.H.6    Sejersen, T.7
  • 44
    • 2542526921 scopus 로고    scopus 로고
    • Modeling effects of mutations in coiled-coil structures: case study using epidermolysis bullosa simplex mutations in segment 1A of K5/K14 intermediate filaments
    • Smith T.A., Steinert P.M., Parry D.A. Modeling effects of mutations in coiled-coil structures: case study using epidermolysis bullosa simplex mutations in segment 1A of K5/K14 intermediate filaments. Proteins 2004, 55:1043-1052.
    • (2004) Proteins , vol.55 , pp. 1043-1052
    • Smith, T.A.1    Steinert, P.M.2    Parry, D.A.3
  • 45
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • Sonnenberg A., Liem R.K. Plakins in development and disease. Exp. Cell Res. 2007, 313:2189-2203.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.2
  • 46
    • 0028028177 scopus 로고
    • Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks
    • Stappenbeck T.S., Lamb J.A., Corcoran C.M., Green K.J. Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. J. Biol. Chem. 1994, 269:29351-29354.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29351-29354
    • Stappenbeck, T.S.1    Lamb, J.A.2    Corcoran, C.M.3    Green, K.J.4
  • 47
    • 0034003558 scopus 로고    scopus 로고
    • Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain
    • Steinbock F.A., Nikolic B., Coulombe P.A., Fuchs E., Traub P., Wiche G. Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain. J. Cell Sci. 2000, 113:483-491.
    • (2000) J. Cell Sci. , vol.113 , pp. 483-491
    • Steinbock, F.A.1    Nikolic, B.2    Coulombe, P.A.3    Fuchs, E.4    Traub, P.5    Wiche, G.6
  • 49
    • 0035147233 scopus 로고    scopus 로고
    • Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins
    • Sun D., Leung C.L., Liem R.K. Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins. J. Cell Sci. 2001, 114:161-172.
    • (2001) J. Cell Sci. , vol.114 , pp. 161-172
    • Sun, D.1    Leung, C.L.2    Liem, R.K.3
  • 50
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina T.M., Verkhovsky A.B., Borisy G.G. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Cell Biol. 1996, 135:991-1007.
    • (1996) J. Cell Biol. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 53
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 1998, 111:2477-2486.
    • (1998) J. Cell Sci. , vol.111 , pp. 2477-2486
    • Wiche, G.1


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