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Volumn 140, Issue 1, 2013, Pages 33-53

Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve

Author keywords

EBS; Intermediate filaments; Plectin; Schwann cells; Skeletal muscle; Skin

Indexed keywords

DESMIN; ISOPROTEIN; PLECTIN;

EID: 84879796143     PISSN: 09486143     EISSN: 1432119X     Source Type: Journal    
DOI: 10.1007/s00418-013-1102-0     Document Type: Review
Times cited : (116)

References (151)
  • 1
    • 29444448260 scopus 로고    scopus 로고
    • Targeted ablation of plectin isoform 1 uncovers role of cytolinker proteins in leukocyte recruitment
    • 16344482 1:CAS:528:DC%2BD28Xpt1Kj 10.1073/pnas.0505380102
    • Abrahamsberg C, Fuchs P, Osmanagic-Myers S, Fischer I, Propst F, Elbe-Bürger A, Wiche G (2005) Targeted ablation of plectin isoform 1 uncovers role of cytolinker proteins in leukocyte recruitment. Proc Natl Acad Sci USA 102(51):18449-18454
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.51 , pp. 18449-18454
    • Abrahamsberg, C.1    Fuchs, P.2    Osmanagic-Myers, S.3    Fischer, I.4    Propst, F.5    Elbe-Bürger, A.6    Wiche, G.7
  • 2
    • 34547757016 scopus 로고    scopus 로고
    • Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects
    • 17606998 1:CAS:528:DC%2BD2sXpslChsb0%3D 10.1242/jcs.004481
    • Ackerl R, Walko G, Fuchs P, Fischer I, Schmuth M, Wiche G (2007) Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects. J Cell Sci 120:2435-2443
    • (2007) J Cell Sci , vol.120 , pp. 2435-2443
    • Ackerl, R.1    Walko, G.2    Fuchs, P.3    Fischer, I.4    Schmuth, M.5    Wiche, G.6
  • 3
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • 9389647 10.1101/gad.11.23.3143
    • Andrä K, Lassmann H, Bittner R, Shorny S, Fässler R, Propst F, Wiche G (1997) Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev 11:3143-3156
    • (1997) Genes Dev , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, F.6    Wiche, G.7
  • 4
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: Plectin regulates actin dynamics in cultured cells
    • 9808630 10.1101/gad.12.21.3442
    • Andrä K, Nikolic B, Stöcher M, Drenckhahn D, Wiche G (1998) Not just scaffolding: plectin regulates actin dynamics in cultured cells. Genes Dev 12:3442-3451
    • (1998) Genes Dev , vol.12 , pp. 3442-3451
    • Andrä, K.1    Nikolic, B.2    Stöcher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 6
    • 77149175645 scopus 로고    scopus 로고
    • Respiratory tract involvement in a child with epidermolysis bullosa simplex with plectin deficiency: A case report
    • 20044146 10.1016/j.ijporl.2009.10.002
    • Babic I, Karaman-Ilic M, Pustisek N, Susic S, Skaric I, Kljenak A, Cikojevic D (2010) Respiratory tract involvement in a child with epidermolysis bullosa simplex with plectin deficiency: a case report. Int J Pediatr Otorhinolaryngol 74:302-305
    • (2010) Int J Pediatr Otorhinolaryngol , vol.74 , pp. 302-305
    • Babic, I.1    Karaman-Ilic, M.2    Pustisek, N.3    Susic, S.4    Skaric, I.5    Kljenak, A.6    Cikojevic, D.7
  • 7
    • 0032811908 scopus 로고    scopus 로고
    • Myopathy, myasthenic syndrome, and epidermolysis bullosa simplex due to plectin deficiency
    • 10446808 1:STN:280:DyaK1MznsVCktg%3D%3D 10.1097/00005072-199908000-00006
    • Banwell BL, Russel J, Fukudome T, Shen XM, Stilling G, Engel AG (1999) Myopathy, myasthenic syndrome, and epidermolysis bullosa simplex due to plectin deficiency. J Neuropathol Exp Neurol 58:832-846
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 832-846
    • Banwell, B.L.1    Russel, J.2    Fukudome, T.3    Shen, X.M.4    Stilling, G.5    Engel, A.G.6
  • 8
    • 0035134083 scopus 로고    scopus 로고
    • A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency
    • 11159198 1:CAS:528:DC%2BD3MXhsFWmtLw%3D 10.1016/S0002-9440(10)64003-5
    • Bauer JW, Rouan F, Kofler B, Rezniczek GA, Kornacker I, Muss W, Hametner R, Klausegger A, Huber A, Pohla-Gubo G et al (2001) A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency. Am J Pathol 158:617-625
    • (2001) Am J Pathol , vol.158 , pp. 617-625
    • Bauer, J.W.1    Rouan, F.2    Kofler, B.3    Rezniczek, G.A.4    Kornacker, I.5    Muss, W.6    Hametner, R.7    Klausegger, A.8    Huber, A.9    Pohla-Gubo, G.10
  • 11
    • 67650558915 scopus 로고    scopus 로고
    • Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength
    • 19366731 1:CAS:528:DC%2BD1MXntFantL0%3D 10.1242/jcs.043042
    • Bhattacharya R, Gonzalez AM, Debiase PJ, Trejo HE, Goldman RD, Flitney FW, Jones JC (2009) Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength. J Cell Sci 122:1390-1400
    • (2009) J Cell Sci , vol.122 , pp. 1390-1400
    • Bhattacharya, R.1    Gonzalez, A.M.2    Debiase, P.J.3    Trejo, H.E.4    Goldman, R.D.5    Flitney, F.W.6    Jones, J.C.7
  • 14
    • 0035879352 scopus 로고    scopus 로고
    • Cutting edge: Integration of human T lymphocyte cytoskeleton by the cytolinker plectin
    • 11441066 1:CAS:528:DC%2BD3MXotFWksLo%3D
    • Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S (2001) Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin. J Immunol 167:641-645
    • (2001) J Immunol , vol.167 , pp. 641-645
    • Brown, M.J.1    Hallam, J.A.2    Liu, Y.3    Yamada, K.M.4    Shaw, S.5
  • 15
    • 77958038961 scopus 로고    scopus 로고
    • Keeping the vimentin network under control: Cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts
    • 20702585 1:CAS:528:DC%2BC3cXhtlGlt7zL 10.1091/mbc.E10-02-0094
    • Burgstaller G, Gregor M, Winter L, Wiche G (2010) Keeping the vimentin network under control: cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts. Mol Biol Cell 21:3362-3375
    • (2010) Mol Biol Cell , vol.21 , pp. 3362-3375
    • Burgstaller, G.1    Gregor, M.2    Winter, L.3    Wiche, G.4
  • 16
    • 0346363880 scopus 로고    scopus 로고
    • Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin
    • 14675180 1:CAS:528:DC%2BD2cXhtValtw%3D%3D 10.1111/j.1523-1747.2003.12639. x
    • Charlesworth A, Gagnoux-Palacios L, Bonduelle M, Ortonne JP, De Raeve L, Meneguzzi G (2003) Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin. J Invest Dermatol 121:1344-1348
    • (2003) J Invest Dermatol , vol.121 , pp. 1344-1348
    • Charlesworth, A.1    Gagnoux-Palacios, L.2    Bonduelle, M.3    Ortonne, J.P.4    De Raeve, L.5    Meneguzzi, G.6
  • 18
    • 0029811246 scopus 로고    scopus 로고
    • A homozygous nonsense mutation in the PLEC1 gene in patients with epidermolysis bullosa simplex with muscular dystrophy
    • 8941634 1:CAS:528:DyaK28XntVOhs7k%3D 10.1172/JCI119028
    • Chavanas S, Pulkkinen L, Gache Y, Smith FJ, McLean WH, Uitto J, Ortonne JP, Meneguzzi G (1996) A homozygous nonsense mutation in the PLEC1 gene in patients with epidermolysis bullosa simplex with muscular dystrophy. J Clin Invest 98:2196-2200
    • (1996) J Clin Invest , vol.98 , pp. 2196-2200
    • Chavanas, S.1    Pulkkinen, L.2    Gache, Y.3    Smith, F.J.4    McLean, W.H.5    Uitto, J.6    Ortonne, J.P.7    Meneguzzi, G.8
  • 19
    • 33748289988 scopus 로고    scopus 로고
    • Interaction of zonula occludens-1 (ZO-1) with alpha-actinin-4: Application of functional proteomics for identification of PDZ domain-associated proteins
    • 16944923 1:CAS:528:DC%2BD28XotV2lu7g%3D 10.1021/pr060216l
    • Chen VC, Li X, Perreault H, Nagy JI (2006) Interaction of zonula occludens-1 (ZO-1) with alpha-actinin-4: application of functional proteomics for identification of PDZ domain-associated proteins. J Proteome Res 5:2123-2134
    • (2006) J Proteome Res , vol.5 , pp. 2123-2134
    • Chen, V.C.1    Li, X.2    Perreault, H.3    Nagy, J.I.4
  • 20
    • 0034709651 scopus 로고    scopus 로고
    • The 300-kDa intermediate filament-associated protein (IFAP300) is a hamster plectin ortholog
    • 10873583 1:CAS:528:DC%2BD3cXkt1Kmsrw%3D 10.1006/bbrc.2000.2916
    • Clubb BH, Chou YH, Herrmann H, Svitkina TM, Borisy GG, Goldman RD (2000) The 300-kDa intermediate filament-associated protein (IFAP300) is a hamster plectin ortholog. Biochem Biophys Res Commun 273:183-187
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 183-187
    • Clubb, B.H.1    Chou, Y.H.2    Herrmann, H.3    Svitkina, T.M.4    Borisy, G.G.5    Goldman, R.D.6
  • 22
    • 67349092209 scopus 로고    scopus 로고
    • Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes
    • 19242489 10.1038/emboj.2009.48 1:CAS:528:DC%2BD1MXitlGltLc%3D
    • de Pereda JM, Lillo MP, Sonnenberg A (2009) Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes. EMBO J 28:1180-1190
    • (2009) EMBO J , vol.28 , pp. 1180-1190
    • De Pereda, J.M.1    Lillo, M.P.2    Sonnenberg, A.3
  • 23
    • 77957267604 scopus 로고    scopus 로고
    • The cardiac desmosome and arrhythmogenic cardiomyopathies: From gene to disease
    • 20847325 1:CAS:528:DC%2BC3cXhtFOktrvI 10.1161/CIRCRESAHA.110.223412
    • Delmar M, McKenna WJ (2010) The cardiac desmosome and arrhythmogenic cardiomyopathies: from gene to disease. Circ Res 107:700-714
    • (2010) Circ Res , vol.107 , pp. 700-714
    • Delmar, M.1    McKenna, W.J.2
  • 24
    • 38349025530 scopus 로고    scopus 로고
    • Plectin regulates the signaling and trafficking of the HIV-1 co-receptor CXCR4 and plays a role in HIV-1 infection
    • 18155192 1:CAS:528:DC%2BD1cXpsFOquw%3D%3D 10.1016/j.yexcr.2007.10.032
    • Ding Y, Zhang L, Goodwin JS, Wang Z, Liu B, Zhang J, Fan GH (2008) Plectin regulates the signaling and trafficking of the HIV-1 co-receptor CXCR4 and plays a role in HIV-1 infection. Exp Cell Res 314:590-602
    • (2008) Exp Cell Res , vol.314 , pp. 590-602
    • Ding, Y.1    Zhang, L.2    Goodwin, J.S.3    Wang, Z.4    Liu, B.5    Zhang, J.6    Fan, G.H.7
  • 25
    • 0029666420 scopus 로고    scopus 로고
    • Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • 8707838 1:CAS:528:DyaK28XktlKju7c%3D 10.1083/jcb.134.2.559
    • Dowling J, Yu QC, Fuchs E (1996) Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J Cell Biol 134:559-572
    • (1996) J Cell Biol , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 26
    • 0030906239 scopus 로고    scopus 로고
    • Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells
    • 9202391 1:CAS:528:DyaK2sXktF2mtbk%3D
    • Eger A, Stockinger A, Wiche G, Foisner R (1997) Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells. J Cell Sci 110:1307-1316
    • (1997) J Cell Sci , vol.110 , pp. 1307-1316
    • Eger, A.1    Stockinger, A.2    Wiche, G.3    Foisner, R.4
  • 27
    • 0031570308 scopus 로고    scopus 로고
    • Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms
    • 9177781 1:CAS:528:DyaK2sXjt12ktLY%3D 10.1006/geno.1997.4724
    • Elliott CE, Becker B, Oehler S, Castañón MJ, Hauptmann R, Wiche G (1997) Plectin transcript diversity: identification and tissue distribution of variants with distinct first coding exons and rodless isoforms. Genomics 42:115-125
    • (1997) Genomics , vol.42 , pp. 115-125
    • Elliott, C.E.1    Becker, B.2    Oehler, S.3    Castañón, M.J.4    Hauptmann, R.5    Wiche, G.6
  • 29
    • 0028326917 scopus 로고
    • Distribution of plectin, an intermediate filament-associated protein, in the adult rat central nervous system
    • 8021973 1:CAS:528:DyaK2cXitFegsbc%3D 10.1002/jnr.490370411
    • Errante LD, Wiche G, Shaw G (1994) Distribution of plectin, an intermediate filament-associated protein, in the adult rat central nervous system. J Neurosci Res 37:515-528
    • (1994) J Neurosci Res , vol.37 , pp. 515-528
    • Errante, L.D.1    Wiche, G.2    Shaw, G.3
  • 31
    • 51349145767 scopus 로고    scopus 로고
    • Molecular pathology of myofibrillar myopathies
    • 18764962 10.1017/S1462399408000793
    • Ferrer I, Olive M (2008) Molecular pathology of myofibrillar myopathies. Expert Rev Mol Med 10:e25
    • (2008) Expert Rev Mol Med , vol.10 , pp. 25
    • Ferrer, I.1    Olive, M.2
  • 32
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • 3430617 1:CAS:528:DyaL1cXovF2rsA%3D%3D 10.1016/0022-2836(87)90297-X
    • Foisner R, Wiche G (1987) Structure and hydrodynamic properties of plectin molecules. J Mol Biol 198:515-531
    • (1987) J Mol Biol , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 33
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • 3346324 1:CAS:528:DyaL1cXhs1emsbs%3D 10.1083/jcb.106.3.723
    • Foisner R, Leichtfried FE, Herrmann H, Small JV, Lawson D, Wiche G (1988) Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J Cell Biol 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
  • 34
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • 2023931 1:CAS:528:DyaK3MXisVGisLk%3D 10.1073/pnas.88.9.3812
    • Foisner R, Traub P, Wiche G (1991) Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc Natl Acad Sci USA 88:3812-3816
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 35
    • 0029620499 scopus 로고
    • Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression
    • 8573472 1:CAS:528:DyaK28XhtVyit7k%3D 10.1006/jsbi.1995.1055
    • Foisner R, Bohn W, Mannweiler K, Wiche G (1995) Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression. J Struct Biol 115:304-317
    • (1995) J Struct Biol , vol.115 , pp. 304-317
    • Foisner, R.1    Bohn, W.2    Mannweiler, K.3    Wiche, G.4
  • 36
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • 8688558 1:CAS:528:DyaK28Xht1akt7g%3D
    • Foisner R, Malecz N, Dressel N, Stadler C, Wiche G (1996) M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol Biol Cell 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
  • 37
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • 11493642 1:CAS:528:DC%2BD3MXkslWktb4%3D
    • Fontao L, Geerts D, Kuikman I, Koster J, Kramer D, Sonnenberg A (2001) The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J Cell Sci 114:2065-2076
    • (2001) J Cell Sci , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 39
    • 84859726094 scopus 로고    scopus 로고
    • Phosphorylation of threonine 1736 in the C-terminal tail of integrin beta4 contributes to hemidesmosome disassembly
    • 22357621 1:CAS:528:DC%2BC38XlvFSqurs%3D 10.1091/mbc.E11-11-0957
    • Frijns E, Kuikman I, Litjens S, Raspe M, Jalink K, Ports M, Wilhelmsen K, Sonnenberg A (2012) Phosphorylation of threonine 1736 in the C-terminal tail of integrin beta4 contributes to hemidesmosome disassembly. Mol Biol Cell 23:1475-1485
    • (2012) Mol Biol Cell , vol.23 , pp. 1475-1485
    • Frijns, E.1    Kuikman, I.2    Litjens, S.3    Raspe, M.4    Jalink, K.5    Ports, M.6    Wilhelmsen, K.7    Sonnenberg, A.8
  • 40
    • 0344462732 scopus 로고    scopus 로고
    • Unusual 5' transcript complexity of plectin isoforms: Novel tissue-specific exons modulate actin binding activity
    • 10556294 1:CAS:528:DyaK1MXnvFKrur8%3D 10.1093/hmg/8.13.2461
    • Fuchs P, Zörer M, Rezniczek GA, Spazierer D, Oehler S, Castañón MJ, Hauptmann R, Wiche G (1999) Unusual 5' transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity. Hum Mol Genet 8:2461-2472
    • (1999) Hum Mol Genet , vol.8 , pp. 2461-2472
    • Fuchs, P.1    Zörer, M.2    Rezniczek, G.A.3    Spazierer, D.4    Oehler, S.5    Castañón, M.J.6    Hauptmann, R.7    Wiche, G.8
  • 41
    • 29944439230 scopus 로고    scopus 로고
    • Plectin rodless isoform expression and its detection in mouse brain
    • 16392042 1:CAS:528:DC%2BD28Xps1ak 10.1007/s10571-005-7826-1
    • Fuchs P, Spazierer D, Wiche G (2005) Plectin rodless isoform expression and its detection in mouse brain. Cell Mol Neurobiol 25:1141-1150
    • (2005) Cell Mol Neurobiol , vol.25 , pp. 1141-1150
    • Fuchs, P.1    Spazierer, D.2    Wiche, G.3
  • 43
    • 0029970098 scopus 로고    scopus 로고
    • Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy
    • 8636409 1:CAS:528:DyaK28XjtFChtrc%3D 10.1172/JCI118671
    • Gache Y, Chavanas S, Lacour JP, Wiche G, Owaribe K, Meneguzzi G, Ortonne JP (1996) Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy. J Clin Invest 97:2289-2298
    • (1996) J Clin Invest , vol.97 , pp. 2289-2298
    • Gache, Y.1    Chavanas, S.2    Lacour, J.P.3    Wiche, G.4    Owaribe, K.5    Meneguzzi, G.6    Ortonne, J.P.7
  • 45
    • 0141631492 scopus 로고    scopus 로고
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4
    • 12791251 10.1016/S0969-2126(03)00090-X
    • García-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM (2003) Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Structure 11:615-625
    • (2003) Structure , vol.11 , pp. 615-625
    • García-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    De Pereda, J.M.4
  • 47
    • 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
    • 10525545 1:CAS:528:DyaK1MXmslCqsL8%3D 10.1083/jcb.147.2.417
    • Geerts D, Fontao L, Nievers MG, Schaapveld RQ, Purkis PE, Wheeler GN, Lane EB, Leigh IM, Sonnenberg A (1999) Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J Cell Biol 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
  • 48
    • 0029908558 scopus 로고    scopus 로고
    • Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice
    • 8673141 1:STN:280:DyaK283lvFGksg%3D%3D 10.1038/ng0796-370
    • Georges-Labouesse E, Messaddeq N, Yehia G, Cadalbert L, Dierich A, Le Meur M (1996) Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice. Nat Genet 13:370-373
    • (1996) Nat Genet , vol.13 , pp. 370-373
    • Georges-Labouesse, E.1    Messaddeq, N.2    Yehia, G.3    Cadalbert, L.4    Dierich, A.5    Le Meur, M.6
  • 49
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the alpha6beta4 integrin in keratinocytes
    • 12429829 1:CAS:528:DC%2BD38XpsVaitL8%3D 10.1091/mbc.02-01-0601
    • Geuijen CA, Sonnenberg A (2002) Dynamics of the alpha6beta4 integrin in keratinocytes. Mol Biol Cell 13:3845-3858
    • (2002) Mol Biol Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 50
    • 35348927451 scopus 로고    scopus 로고
    • Desmosomes: New perspectives on a classic
    • 17934502 1:CAS:528:DC%2BD2sXhtFKisbvE 10.1038/sj.jid.5701015
    • Green KJ, Simpson CL (2007) Desmosomes: new perspectives on a classic. J Invest Dermatol 127:2499-2510
    • (2007) J Invest Dermatol , vol.127 , pp. 2499-2510
    • Green, K.J.1    Simpson, C.L.2
  • 51
    • 33744541891 scopus 로고    scopus 로고
    • Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres
    • 16608880 1:CAS:528:DC%2BD28XlsVOms78%3D 10.1242/jcs.02891
    • Gregor M, Zeöld A, Oehler S, Marobela KA, Fuchs P, Weigel G, Hardie DG, Wiche G (2006) Plectin scaffolds recruit energy-controlling AMP-activated protein kinase (AMPK) in differentiated myofibres. J Cell Sci 119:1864-1875
    • (2006) J Cell Sci , vol.119 , pp. 1864-1875
    • Gregor, M.1    Zeöld, A.2    Oehler, S.3    Marobela, K.A.4    Fuchs, P.5    Weigel, G.6    Hardie, D.G.7    Wiche, G.8
  • 52
    • 78649796969 scopus 로고    scopus 로고
    • Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy
    • 21109228 1:CAS:528:DC%2BC3cXhsFags7bE 10.1016/j.ajhg.2010.10.017
    • Gundesli H, Talim B, Korkusuz P, Balci-Hayta B, Cirak S, Akarsu NA, Topaloglu H, Dincer P (2010) Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy. Am J Hum Genet 87:834-841
    • (2010) Am J Hum Genet , vol.87 , pp. 834-841
    • Gundesli, H.1    Talim, B.2    Korkusuz, P.3    Balci-Hayta, B.4    Cirak, S.5    Akarsu, N.A.6    Topaloglu, H.7    Dincer, P.8
  • 53
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • 7736575 1:CAS:528:DyaK2MXlt1Kisrs%3D 10.1016/0092-8674(95)90333-X
    • Guo L, Degenstein L, Dowling J, Yu QC, Wollmann R, Perman B, Fuchs E (1995) Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell 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    Fuchs, E.7
  • 54
    • 0021053192 scopus 로고
    • Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells
    • 6358225 1:CAS:528:DyaL3sXlvFSisLk%3D
    • Herrmann H, Wiche G (1983) Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells. J Biol Chem 258:14610-14618
    • (1983) J Biol Chem , vol.258 , pp. 14610-14618
    • Herrmann, H.1    Wiche, G.2
  • 55
    • 0023126564 scopus 로고
    • Plectin and IFAP-300 K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • 3027087 1:CAS:528:DyaL2sXpvVejsA%3D%3D
    • Herrmann H, Wiche G (1987) Plectin and IFAP-300 K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J Biol Chem 262:1320-1325
    • (1987) J Biol Chem , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 56
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • 1541639 1:CAS:528:DyaK38Xks1Ois70%3D 10.1083/jcb.116.6.1497
    • Hieda Y, Nishizawa Y, Uematsu J, Owaribe K (1992) Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J Cell Biol 116:1497-1506
    • (1992) J Cell Biol , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 57
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • 10036236 1:CAS:528:DyaK1MXisFWrs74%3D
    • Hijikata T, Murakami T, Imamura M, Fujimaki N, Ishikawa H (1999) Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J Cell Sci 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
  • 58
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • 12610730 1:CAS:528:DC%2BD3sXhsF2itrw%3D
    • Hijikata T, Murakami T, Ishikawa H, Yorifuji H (2003) Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem Cell Biol 119:109-123
    • (2003) Histochem Cell Biol , vol.119 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 59
    • 47649083199 scopus 로고    scopus 로고
    • Plectin 1 links intermediate filaments to costameric sarcolemma through beta-synemin, alpha-dystrobrevin and actin
    • 18505798 1:CAS:528:DC%2BD1cXovFakt7s%3D 10.1242/jcs.021634
    • Hijikata T, Nakamura A, Isokawa K, Imamura M, Yuasa K, Ishikawa R, Kohama K, Takeda S, Yorifuji H (2008) Plectin 1 links intermediate filaments to costameric sarcolemma through beta-synemin, alpha-dystrobrevin and actin. J Cell Sci 121:2062-2074
    • (2008) J Cell Sci , vol.121 , pp. 2062-2074
    • Hijikata, T.1    Nakamura, A.2    Isokawa, K.3    Imamura, M.4    Yuasa, K.5    Ishikawa, R.6    Kohama, K.7    Takeda, S.8    Yorifuji, H.9
  • 60
    • 0033973133 scopus 로고    scopus 로고
    • The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome
    • 10637308 1:CAS:528:DC%2BD3cXosFyisQ%3D%3D
    • Hopkinson SB, Jones JC (2000) The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome. Mol Biol Cell 11:277-286
    • (2000) Mol Biol Cell , vol.11 , pp. 277-286
    • Hopkinson, S.B.1    Jones, J.C.2
  • 62
    • 79955960232 scopus 로고    scopus 로고
    • Characterization of cytoskeleton-enriched protein fraction of the trabecular meshwork and ciliary muscle cells
    • 20631233 10.1167/iovs.10-5318
    • Inoue T, Pecen P, Maddala R, Skiba NP, Pattabiraman PP, Epstein DL, Rao PV (2010) Characterization of cytoskeleton-enriched protein fraction of the trabecular meshwork and ciliary muscle cells. Invest Ophthalmol Vis Sci 51:6461-6471
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 6461-6471
    • Inoue, T.1    Pecen, P.2    Maddala, R.3    Skiba, N.P.4    Pattabiraman, P.P.5    Epstein, D.L.6    Rao, P.V.7
  • 63
    • 0035197616 scopus 로고    scopus 로고
    • Plectin repeats and modules: Strategic cysteines and their presumed impact on cytolinker functions
    • 11746222 1:CAS:528:DC%2BD38XksFyjtQ%3D%3D 10.1002/bies.1151
    • Janda L, Damborský J, Rezniczek GA, Wiche G (2001) Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions. BioEssays 23:1064-1069
    • (2001) BioEssays , vol.23 , pp. 1064-1069
    • Janda, L.1    Damborský, J.2    Rezniczek, G.A.3    Wiche, G.4
  • 64
    • 0028928013 scopus 로고
    • Alternate binding of actin and calmodulin to multiple sites on dystrophin
    • 7890677 1:CAS:528:DyaK2MXksVSks7s%3D 10.1074/jbc.270.10.5578
    • Jarrett HW, Foster JL (1995) Alternate binding of actin and calmodulin to multiple sites on dystrophin. J Biol Chem 270:5578-5586
    • (1995) J Biol Chem , vol.270 , pp. 5578-5586
    • Jarrett, H.W.1    Foster, J.L.2
  • 65
    • 0041562604 scopus 로고    scopus 로고
    • Immunofluorescence analysis of the basement membrane zone components in human anagen hair follicles
    • 12930291 10.1034/j.1600-0625.2002.120402.x
    • Joubeh S, Mori O, Owaribe K, Hashimoto T (2003) Immunofluorescence analysis of the basement membrane zone components in human anagen hair follicles. Exp Dermatol 12:365-370
    • (2003) Exp Dermatol , vol.12 , pp. 365-370
    • Joubeh, S.1    Mori, O.2    Owaribe, K.3    Hashimoto, T.4
  • 66
    • 84857653875 scopus 로고    scopus 로고
    • Plectin promotes migration and invasion of cancer cells and is a novel prognostic marker for head and neck squamous cell carcinoma
    • 22245045 1:CAS:528:DC%2BC38Xhs1GhtL4%3D 10.1016/j.jprot.2011.12.018
    • Katada K, Tomonaga T, Satoh M, Matsushita K, Tonoike Y, Kodera Y, Hanazawa T, Nomura F, Okamoto Y (2012) Plectin promotes migration and invasion of cancer cells and is a novel prognostic marker for head and neck squamous cell carcinoma. J Proteomics 75:1803-1815
    • (2012) J Proteomics , vol.75 , pp. 1803-1815
    • Katada, K.1    Tomonaga, T.2    Satoh, M.3    Matsushita, K.4    Tonoike, Y.5    Kodera, Y.6    Hanazawa, T.7    Nomura, F.8    Okamoto, Y.9
  • 68
    • 81855220949 scopus 로고    scopus 로고
    • Nesprin-3: A versatile connector between the nucleus and the cytoskeleton
    • 22103514 1:CAS:528:DC%2BC3MXhsFaiurzE 10.1042/BST20110669
    • Ketema M, Sonnenberg A (2011) Nesprin-3: a versatile connector between the nucleus and the cytoskeleton. Biochem Soc Trans 39:1719-1724
    • (2011) Biochem Soc Trans , vol.39 , pp. 1719-1724
    • Ketema, M.1    Sonnenberg, A.2
  • 69
    • 35648937494 scopus 로고    scopus 로고
    • Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin
    • 17881500 1:CAS:528:DC%2BD2sXht1ygur7N 10.1242/jcs.014191
    • Ketema M, Wilhelmsen K, Kuikman I, Janssen H, Hodzic D, Sonnenberg A (2007) Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. J Cell Sci 120:3384-3394
    • (2007) J Cell Sci , vol.120 , pp. 3384-3394
    • Ketema, M.1    Wilhelmsen, K.2    Kuikman, I.3    Janssen, H.4    Hodzic, D.5    Sonnenberg, A.6
  • 71
    • 44149113780 scopus 로고    scopus 로고
    • Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms
    • 18490514 1:CAS:528:DC%2BD1cXmsVWksLc%3D 10.1083/jcb.200711058
    • Konieczny P, Fuchs P, Reipert S, Kunz WS, Zeöld A, Fischer I, Paulin D, Schröder R, Wiche G (2008) Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms. J Cell Biol 181:667-681
    • (2008) J Cell Biol , vol.181 , pp. 667-681
    • Konieczny, P.1    Fuchs, P.2    Reipert, S.3    Kunz, W.S.4    Zeöld, A.5    Fischer, I.6    Paulin, D.7    Schröder, R.8    Wiche, G.9
  • 75
    • 0037439896 scopus 로고    scopus 로고
    • Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly
    • 12482924 1:CAS:528:DC%2BD3sXpvVKmtg%3D%3D 10.1242/jcs.00241
    • Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A (2003) Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly. J Cell Sci 116:387-399
    • (2003) J Cell Sci , vol.116 , pp. 387-399
    • Koster, J.1    Geerts, D.2    Favre, B.3    Borradori, L.4    Sonnenberg, A.5
  • 76
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes
    • 14668477 1:CAS:528:DC%2BD2cXitlGgsrs%3D 10.1091/mbc.E03-09-0697
    • Koster J, van Wilpe S, Kuikman I, Litjens SH, Sonnenberg A (2004) Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes. Mol Biol Cell 15:1211-1223
    • (2004) Mol Biol Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    Van Wilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 77
    • 0021828069 scopus 로고
    • Identification and spatial arrangement of high molecular weight proteins (Mr 300 000-330 000) co-assembling with microtubules from a cultured cell line (rat glioma C6)
    • 2863145 1:CAS:528:DyaL2MXltVSlsb0%3D
    • Koszka C, Leichtfried FE, Wiche G (1985) Identification and spatial arrangement of high molecular weight proteins (Mr 300 000-330 000) co-assembling with microtubules from a cultured cell line (rat glioma C6). Eur J Cell Biol 38:149-156
    • (1985) Eur J Cell Biol , vol.38 , pp. 149-156
    • Koszka, C.1    Leichtfried, F.E.2    Wiche, G.3
  • 78
    • 0034133976 scopus 로고    scopus 로고
    • Mutation reports: Epidermolysis bullosa simplex associated with severe mucous membrane involvement and novel mutations in the plectin gene
    • 10652001 1:CAS:528:DC%2BD3cXktlWgurY%3D 10.1046/j.1523-1747.2000.00856.x
    • Kunz M, Rouan F, Pulkkinen L, Hamm H, Jeschke R, Bruckner-Tuderman L, Brocker EB, Wiche G, Uitto J, Zillikens D (2000) Mutation reports: epidermolysis bullosa simplex associated with severe mucous membrane involvement and novel mutations in the plectin gene. J Invest Dermatol 114:376-380
    • (2000) J Invest Dermatol , vol.114 , pp. 376-380
    • Kunz, M.1    Rouan, F.2    Pulkkinen, L.3    Hamm, H.4    Jeschke, R.5    Bruckner-Tuderman, L.6    Brocker, E.B.7    Wiche, G.8    Uitto, J.9    Zillikens, D.10
  • 79
    • 35348846508 scopus 로고    scopus 로고
    • An early evaluation of malignant tendency with plectin expression in human colorectal adenoma and adenocarcinoma
    • 18084872 1:CAS:528:DC%2BD2sXnt1GmsLY%3D
    • Lee KY, Liu YH, Ho CC, Pei RJ, Yeh KT, Cheng CC, Lai YS (2004) An early evaluation of malignant tendency with plectin expression in human colorectal adenoma and adenocarcinoma. J Med 35:141-149
    • (2004) J Med , vol.35 , pp. 141-149
    • Lee, K.Y.1    Liu, Y.H.2    Ho, C.C.3    Pei, R.J.4    Yeh, K.T.5    Cheng, C.C.6    Lai, Y.S.7
  • 80
    • 0031686709 scopus 로고    scopus 로고
    • Plectin in the human central nervous system: Predominant expression at pia/glia and endothelia/glia interfaces
    • 9754951 1:CAS:528:DyaK1cXkvFSgtrs%3D 10.1007/s004010050885
    • Lie AA, Schröder R, Blümcke I, Magin TM, Wiestler OD, Elger CE (1998) Plectin in the human central nervous system: predominant expression at pia/glia and endothelia/glia interfaces. Acta Neuropathol 96:215-221
    • (1998) Acta Neuropathol , vol.96 , pp. 215-221
    • Lie, A.A.1    Schröder, R.2    Blümcke, I.3    Magin, T.M.4    Wiestler, O.D.5    Elger, C.E.6
  • 81
    • 0022245790 scopus 로고
    • Purification of the 300 K intermediate filament-associated protein and its in vitro recombination with intermediate filaments
    • 3897249 1:CAS:528:DyaL2MXltlOgtbc%3D 10.1083/jcb.101.3.802
    • Lieska N, Yang HY, Goldman RD (1985) Purification of the 300 K intermediate filament-associated protein and its in vitro recombination with intermediate filaments. J Cell Biol 101:802-813
    • (1985) J Cell Biol , vol.101 , pp. 802-813
    • Lieska, N.1    Yang, H.Y.2    Goldman, R.D.3
  • 82
    • 0141764796 scopus 로고    scopus 로고
    • Specificity of binding of the plectin actin-binding domain to beta4 integrin
    • 14517317 1:CAS:528:DC%2BD3sXnvVyjtLs%3D 10.1091/mbc.E03-05-0268
    • Litjens SH, Koster J, Kuikman I, van Wilpe S, de Pereda JM, Sonnenberg A (2003) Specificity of binding of the plectin actin-binding domain to beta4 integrin. Mol Biol Cell 14:4039-4050
    • (2003) Mol Biol Cell , vol.14 , pp. 4039-4050
    • Litjens, S.H.1    Koster, J.2    Kuikman, I.3    Van Wilpe, S.4    De Pereda, J.M.5    Sonnenberg, A.6
  • 83
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • 16757171 1:CAS:528:DC%2BD28XntFWrtLo%3D 10.1016/j.tcb.2006.05.004
    • Litjens SH, de Pereda JM, Sonnenberg A (2006) Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol 16:376-383
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    De Pereda, J.M.2    Sonnenberg, A.3
  • 84
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24)
    • 8633055 1:CAS:528:DyaK28XivVKqsb8%3D 10.1073/pnas.93.9.4278
    • Liu CG, Maercker C, Castañon MJ, Hauptmann R, Wiche G (1996) Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24). Proc Natl Acad Sci USA 93:4278-4283
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4278-4283
    • Liu, C.G.1    Maercker, C.2    Castañon, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 85
    • 0000488695 scopus 로고
    • Interactions of tensin with actin and identification of its three distinct actin-binding domains
    • 8195290 1:CAS:528:DyaK2cXivFagtbY%3D 10.1083/jcb.125.5.1067
    • Lo SH, Janmey PA, Hartwig JH, Chen LB (1994) Interactions of tensin with actin and identification of its three distinct actin-binding domains. J Cell Biol 125:1067-1075
    • (1994) J Cell Biol , vol.125 , pp. 1067-1075
    • Lo, S.H.1    Janmey, P.A.2    Hartwig, J.H.3    Chen, L.B.4
  • 86
    • 0036385851 scopus 로고    scopus 로고
    • Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity
    • 12200133 1:CAS:528:DC%2BD38XmsV2ku7g%3D 10.1016/S0006-291X(02)02007-7
    • Lunter PC, Wiche G (2002) Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity. Biochem Biophys Res Commun 296:904-910
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 904-910
    • Lunter, P.C.1    Wiche, G.2
  • 87
    • 0035807883 scopus 로고    scopus 로고
    • Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein
    • 11724960 1:CAS:528:DC%2BD3MXptFCltb0%3D 10.1073/pnas.261371298
    • Mack GJ, Compton DA (2001) Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein. Proc Natl Acad Sci USA 98:14434-14439
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14434-14439
    • Mack, G.J.1    Compton, D.A.2
  • 88
    • 79952196493 scopus 로고    scopus 로고
    • Novel interactions of ankyrins-G at the costameres: The muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C
    • 21223964 1:CAS:528:DC%2BC3MXjsFWnur8%3D 10.1016/j.yexcr.2011.01.002
    • Maiweilidan Y, Klauza I, Kordeli E (2011) Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C. Exp Cell Res 317:724-736
    • (2011) Exp Cell Res , vol.317 , pp. 724-736
    • Maiweilidan, Y.1    Klauza, I.2    Kordeli, E.3
  • 89
    • 0029873478 scopus 로고    scopus 로고
    • Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site
    • 8626512 1:CAS:528:DyaK28XitFartLc%3D 10.1074/jbc.271.14.8203
    • Malecz N, Foisner R, Stadler C, Wiche G (1996) Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. J Biol Chem 271:8203-8208
    • (1996) J Biol Chem , vol.271 , pp. 8203-8208
    • Malecz, N.1    Foisner, R.2    Stadler, C.3    Wiche, G.4
  • 90
    • 50849108513 scopus 로고    scopus 로고
    • Regulation of hemidesmosome disassembly by growth factor receptors
    • 18583123 1:CAS:528:DC%2BD1cXhtVyks7vI 10.1016/j.ceb.2008.05.001
    • Margadant C, Frijns E, Wilhelmsen K, Sonnenberg A (2008) Regulation of hemidesmosome disassembly by growth factor receptors. Curr Opin Cell Biol 20:589-596
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 589-596
    • Margadant, C.1    Frijns, E.2    Wilhelmsen, K.3    Sonnenberg, A.4
  • 92
    • 80052636155 scopus 로고    scopus 로고
    • Plectin regulates invasiveness of SW480 colon carcinoma cells and is targeted to podosome-like adhesions in an isoform-specific manner
    • 21821021 1:CAS:528:DC%2BC3MXhtFGlsbvO 10.1016/j.yexcr.2011.07.013
    • McInroy L, Määttä A (2011) Plectin regulates invasiveness of SW480 colon carcinoma cells and is targeted to podosome-like adhesions in an isoform-specific manner. Exp Cell Res 317:2468-2478
    • (2011) Exp Cell Res , vol.317 , pp. 2468-2478
    • McInroy, L.1    Määttä, A.2
  • 95
    • 14644402383 scopus 로고    scopus 로고
    • Epidermolysis bullosa simplex associated with pyloric atresia is a novel clinical subtype caused by mutations in the plectin gene (PLEC1)
    • 15681471 1:CAS:528:DC%2BD2MXhvFKrtrw%3D 10.1016/S1525-1578(10)60005-0
    • Nakamura H, Sawamura D, Goto M, McMillan JR, Park S, Kono S, Hasegawa S, Paku S, Nakamura T, Ogiso Y, Shimizu H (2005) Epidermolysis bullosa simplex associated with pyloric atresia is a novel clinical subtype caused by mutations in the plectin gene (PLEC1). J Mol Diagn 7:28-35
    • (2005) J Mol Diagn , vol.7 , pp. 28-35
    • Nakamura, H.1    Sawamura, D.2    Goto, M.3    McMillan, J.R.4    Park, S.5    Kono, S.6    Hasegawa, S.7    Paku, S.8    Nakamura, T.9    Ogiso, Y.10    Shimizu, H.11
  • 99
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • 8830774 1:CAS:528:DyaK28Xls1yktLo%3D 10.1083/jcb.134.6.1455
    • Nikolic B, Mac Nulty E, Mir B, Wiche G (1996) Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J Cell Biol 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
  • 100
    • 71049185569 scopus 로고    scopus 로고
    • BRCA2 interacts with the cytoskeletal linker protein plectin to form a complex controlling centrosome localization
    • 19709076 1:CAS:528:DC%2BD1MXhsVSktLfM 10.1111/j.1349-7006.2009.01282.x
    • Niwa T, Saito H, Imajoh-ohmi S, Kaminishi M, Seto Y, Miki Y, Nakanishi A (2009) BRCA2 interacts with the cytoskeletal linker protein plectin to form a complex controlling centrosome localization. Cancer Sci 100:2115-2125
    • (2009) Cancer Sci , vol.100 , pp. 2115-2125
    • Niwa, T.1    Saito, H.2    Imajoh-Ohmi, S.3    Kaminishi, M.4    Seto, Y.5    Miki, Y.6    Nakanishi, A.7
  • 102
    • 0033395566 scopus 로고    scopus 로고
    • Identification of the hemidesmosomal 500 kDa protein (HD1) as plectin
    • 10578067 1:CAS:528:DC%2BD3cXmt1aksw%3D%3D 10.1093/oxfordjournals.jbchem. a022560
    • Okumura M, Uematsu J, Hirako Y, Nishizawa Y, Shimizu H, Kido N, Owaribe K (1999) Identification of the hemidesmosomal 500 kDa protein (HD1) as plectin. J Biochem 126:1144-1150
    • (1999) J Biochem , vol.126 , pp. 1144-1150
    • Okumura, M.1    Uematsu, J.2    Hirako, Y.3    Nishizawa, Y.4    Shimizu, H.5    Kido, N.6    Owaribe, K.7
  • 103
    • 2442605590 scopus 로고    scopus 로고
    • Plectin-RACK1 (receptor for activated C kinase 1) scaffolding: A novel mechanism to regulate protein kinase C activity
    • 14966116 1:CAS:528:DC%2BD2cXjsVKmsL4%3D 10.1074/jbc.M312382200
    • Osmanagic-Myers S, Wiche G (2004) Plectin-RACK1 (receptor for activated C kinase 1) scaffolding: a novel mechanism to regulate protein kinase C activity. J Biol Chem 279:18701-18710
    • (2004) J Biol Chem , vol.279 , pp. 18701-18710
    • Osmanagic-Myers, S.1    Wiche, G.2
  • 104
    • 33747163300 scopus 로고    scopus 로고
    • Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration
    • 16908671 1:CAS:528:DC%2BD28XosVKgt7Y%3D 10.1083/jcb.200605172
    • Osmanagic-Myers S, Gregor M, Walko G, Burgstaller G, Reipert S, Wiche G (2006) Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration. J Cell Biol 174:557-568
    • (2006) J Cell Biol , vol.174 , pp. 557-568
    • Osmanagic-Myers, S.1    Gregor, M.2    Walko, G.3    Burgstaller, G.4    Reipert, S.5    Wiche, G.6
  • 106
    • 80052855504 scopus 로고    scopus 로고
    • Quantitative tissue proteomics of esophageal squamous cell carcinoma for novel biomarker discovery
    • 21743296 1:CAS:528:DC%2BC38XitlGlt7Y%3D 10.4161/cbt.12.6.16833
    • Pawar H, Kashyap MK, Sahasrabuddhe NA, Renuse S, Harsha HC, Kumar P, Sharma J, Kandasamy K et al (2011) Quantitative tissue proteomics of esophageal squamous cell carcinoma for novel biomarker discovery. Cancer Biol Ther 12:510-522
    • (2011) Cancer Biol Ther , vol.12 , pp. 510-522
    • Pawar, H.1    Kashyap, M.K.2    Sahasrabuddhe, N.A.3    Renuse, S.4    Harsha, H.C.5    Kumar, P.6    Sharma, J.7    Kandasamy, K.8
  • 107
    • 11944249876 scopus 로고    scopus 로고
    • Plectin gene mutations can cause epidermolysis bullosa with pyloric atresia
    • 15654962 1:CAS:528:DC%2BD2MXnvFCksQ%3D%3D 10.1111/j.0022-202X.2004.23564. x
    • Pfendner E, Uitto J (2005) Plectin gene mutations can cause epidermolysis bullosa with pyloric atresia. J Invest Dermatol 124:111-115
    • (2005) J Invest Dermatol , vol.124 , pp. 111-115
    • Pfendner, E.1    Uitto, J.2
  • 108
    • 0029798270 scopus 로고    scopus 로고
    • Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy
    • 8894687 1:CAS:528:DyaK28Xmt1ansL0%3D 10.1093/hmg/5.10.1539
    • Pulkkinen L, Smith FJ, Shimizu H, Murata S, Yaoita H, Hachisuka H, Nishikawa T, McLean WH, Uitto J (1996) Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. Hum Mol Genet 5:1539-1546
    • (1996) Hum Mol Genet , vol.5 , pp. 1539-1546
    • Pulkkinen, L.1    Smith, F.J.2    Shimizu, H.3    Murata, S.4    Yaoita, H.5    Hachisuka, H.6    Nishikawa, T.7    McLean, W.H.8    Uitto, J.9
  • 109
    • 0019051839 scopus 로고
    • High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments
    • 6933530 1:CAS:528:DyaL3cXlvVWgur0%3D 10.1073/pnas.77.8.4808
    • Pytela R, Wiche G (1980) High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc Natl Acad Sci USA 77:4808-4812
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 110
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes
    • 15121854 1:CAS:528:DC%2BD2cXjvFChtLo%3D 10.1128/MCB.24.10.4351-4360.2004
    • Rabinovitz I, Tsomo L, Mercurio AM (2004) Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes. Mol Cell Biol 24:4351-4360
    • (2004) Mol Cell Biol , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 111
    • 84878814938 scopus 로고    scopus 로고
    • Linking cytoarchitecture to metabolism: Sarcolemma-associated plectin affects glucose uptake by destabilizing microtubule networks in mdx myofibers
    • (in press)
    • Raith M, Valencia RG, Fischer I, Orthofer M, Penninger JM, Spuler S, Rezniczek GA, Wiche G (2013) Linking cytoarchitecture to metabolism: sarcolemma-associated plectin affects glucose uptake by destabilizing microtubule networks in mdx myofibers. Skeletal muscle (in press)
    • (2013) Skeletal Muscle
    • Raith, M.1    Valencia, R.G.2    Fischer, I.3    Orthofer, M.4    Penninger, J.M.5    Spuler, S.6    Rezniczek, G.A.7    Wiche, G.8
  • 112
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • 10527638 1:CAS:528:DyaK1MXms1ygs7o%3D 10.1006/excr.1999.4626
    • Reipert S, Steinböck F, Fischer I, Bittner RE, Zeöld A, Wiche G (1999) Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp Cell Res 252:479-491
    • (1999) Exp Cell Res , vol.252 , pp. 479-491
    • Reipert, S.1    Steinböck, F.2    Fischer, I.3    Bittner, R.E.4    Zeöld, A.5    Wiche, G.6
  • 113
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the beta4 subunit and plectin at multiple molecular sites
    • 9531560 1:CAS:528:DyaK1cXis1ejs7s%3D 10.1083/jcb.141.1.209
    • Rezniczek GA, de Pereda JM, Reipert S, Wiche G (1998) Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites. J Cell Biol 141:209-225
    • (1998) J Cell Biol , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    De Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 114
    • 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
    • 14559777 1:CAS:528:DC%2BD3sXptVSntLs%3D 10.1093/hmg/ddg345
    • Rezniczek GA, Abrahamsberg C, Fuchs P, Spazierer D, Wiche G (2003) Plectin 5-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum Mol Genet 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
  • 115
    • 33947722764 scopus 로고    scopus 로고
    • Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan
    • 17389230 1:CAS:528:DC%2BD2sXjvVSnsb0%3D 10.1083/jcb.200604179
    • Rezniczek GA, Konieczny P, Nikolic B, Reipert S, Schneller D, Abrahamsberg C, Davies KE, Winder SJ, Wiche G (2007) Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan. J Cell Biol 176:965-977
    • (2007) J Cell Biol , vol.176 , pp. 965-977
    • Rezniczek, G.A.1    Konieczny, P.2    Nikolic, B.3    Reipert, S.4    Schneller, D.5    Abrahamsberg, C.6    Davies, K.E.7    Winder, S.J.8    Wiche, G.9
  • 116
    • 70450263531 scopus 로고    scopus 로고
    • Plectin gene defects lead to various forms of epidermolysis bullosa simplex
    • 19945614 1:CAS:528:DC%2BC3cXhsVSgu7o%3D 10.1016/j.det.2009.10.004
    • Rezniczek GA, Walko G, Wiche G (2010) Plectin gene defects lead to various forms of epidermolysis bullosa simplex. Dermatol Clin 28:33-41
    • (2010) Dermatol Clin , vol.28 , pp. 33-41
    • Rezniczek, G.A.1    Walko, G.2    Wiche, G.3
  • 119
    • 66949173652 scopus 로고    scopus 로고
    • Myofibrillar myopathies: A clinical and myopathological guide
    • 19563540 10.1111/j.1750-3639.2009.00289.x 1:CAS:528:DC%2BD1MXos1Ojt7s%3D
    • Schröder R, Schoser B (2009) Myofibrillar myopathies: a clinical and myopathological guide. Brain Pathol 19:483-492
    • (2009) Brain Pathol , vol.19 , pp. 483-492
    • Schröder, R.1    Schoser, B.2
  • 123
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
    • 15128297 10.1111/j.1432-1033.2004.04095.x 1:CAS:528:DC%2BD2cXksVykt7c%3D
    • Sevcík J, Urbániková L, Kostan J, Janda L, Wiche G (2004) Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur J Biochem 271:1873-1884
    • (2004) Eur J Biochem , vol.271 , pp. 1873-1884
    • Sevcík, J.1    Urbániková, L.2    Kostan, J.3    Janda, L.4    Wiche, G.5
  • 124
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • 8138568 1:CAS:528:DyaK2cXis1Kntro%3D 10.1083/jcb.125.1.159
    • Skalli O, Jones JC, Gagescu R, Goldman RD (1994) IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions. J Cell Biol 125:159-170
    • (1994) J Cell Biol , vol.125 , pp. 159-170
    • Skalli, O.1    Jones, J.C.2    Gagescu, R.3    Goldman, R.D.4
  • 126
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • 17499243 1:CAS:528:DC%2BD2sXmtFOit7c%3D 10.1016/j.yexcr.2007.03.039
    • Sonnenberg A, Liem RK (2007) Plakins in development and disease. Exp Cell Res 313:2189-2203
    • (2007) Exp Cell Res , vol.313 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.2
  • 127
    • 34247222123 scopus 로고    scopus 로고
    • The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain
    • 17397861 1:CAS:528:DC%2BD2sXkslCmsL4%3D 10.1016/j.jmb.2007.02.090
    • Sonnenberg A, Rojas AM, de Pereda JM (2007) The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain. J Mol Biol 368:1379-1391
    • (2007) J Mol Biol , vol.368 , pp. 1379-1391
    • Sonnenberg, A.1    Rojas, A.M.2    De Pereda, J.M.3
  • 128
    • 34247238238 scopus 로고    scopus 로고
    • Oxidation and nitrosylation of cysteines proximal to the intermediate filament (IF)-binding site of plectin: Effects on structure and vimentin binding and involvement in if collapse
    • 17224453 1:CAS:528:DC%2BD2sXis1KgtLk%3D 10.1074/jbc.M608473200
    • Spurny R, Abdoulrahman K, Janda L, Rünzler D, Köhler G, Castañón MJ, Wiche G (2007) Oxidation and nitrosylation of cysteines proximal to the intermediate filament (IF)-binding site of plectin: effects on structure and vimentin binding and involvement in IF collapse. J Biol Chem 282:8175-8187
    • (2007) J Biol Chem , vol.282 , pp. 8175-8187
    • Spurny, R.1    Abdoulrahman, K.2    Janda, L.3    Rünzler, D.4    Köhler, G.5    Castañón, M.J.6    Wiche, G.7
  • 129
    • 84954358370 scopus 로고    scopus 로고
    • Plectin deficiency affects precursor formation and dynamics of vimentin networks
    • 18848541 1:CAS:528:DC%2BD1cXhtlGhtL7P 10.1016/j.yexcr.2008.09.012
    • Spurny R, Gregor M, Castañón MJ, Wiche G (2008) Plectin deficiency affects precursor formation and dynamics of vimentin networks. Exp Cell Res 314:3570-3580
    • (2008) Exp Cell Res , vol.314 , pp. 3570-3580
    • Spurny, R.1    Gregor, M.2    Castañón, M.J.3    Wiche, G.4
  • 130
    • 0033927556 scopus 로고    scopus 로고
    • Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis
    • 10891503 1:CAS:528:DC%2BD3cXlt1Snu74%3D 10.1128/MCB.20.15.5665-5679.2000
    • Stegh AH, Herrmann H, Lampel S, Weisenberger D, Andrä K, Seper M, Wiche G, Krammer PH, Peter ME (2000) Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol Cell Biol 20:5665-5679
    • (2000) Mol Cell Biol , vol.20 , pp. 5665-5679
    • Stegh, A.H.1    Herrmann, H.2    Lampel, S.3    Weisenberger, D.4    Andrä, K.5    Seper, M.6    Wiche, G.7    Krammer, P.H.8    Peter, M.E.9
  • 131
    • 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
    • 10639335
    • Steinböck FA, Nikolic B, Coulombe PA, Fuchs E, Traub P, Wiche G (2000) Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain. J Cell Sci 113:483-491
    • (2000) J Cell Sci , vol.113 , pp. 483-491
    • Steinböck, F.A.1    Nikolic, B.2    Coulombe, P.A.3    Fuchs, E.4    Traub, P.5    Wiche, G.6
  • 133
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • 8922382 1:CAS:528:DyaK28XntVarsL0%3D 10.1083/jcb.135.4.991
    • Svitkina TM, Verkhovsky AB, Borisy GG (1996) Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J Cell Biol 135:991-1007
    • (1996) J Cell Biol , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 134
    • 84857037909 scopus 로고    scopus 로고
    • Fused in sarcoma (FUS) interacts with the cytolinker protein plectin: Implications for FUS subcellular localization and function
    • 22240165 1:CAS:528:DC%2BC38XjtVOqsbg%3D 10.1016/j.yexcr.2011.12.019
    • Thomsen C, Udhane S, Runnberg R, Wiche G, Ståhlberg A, Aman P (2012) Fused in sarcoma (FUS) interacts with the cytolinker protein plectin: implications for FUS subcellular localization and function. Exp Cell Res 318:653-661
    • (2012) Exp Cell Res , vol.318 , pp. 653-661
    • Thomsen, C.1    Udhane, S.2    Runnberg, R.3    Wiche, G.4    Ståhlberg, A.5    Aman, P.6
  • 135
    • 33644642950 scopus 로고    scopus 로고
    • Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease
    • 16507904 1:CAS:528:DC%2BD28XislGgtbk%3D 10.2353/ajpath.2006.051028
    • Tian R, Gregor M, Wiche G, Goldman JE (2006) Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease. Am J Pathol 168:888-897
    • (2006) Am J Pathol , vol.168 , pp. 888-897
    • Tian, R.1    Gregor, M.2    Wiche, G.3    Goldman, J.E.4
  • 136
  • 137
    • 0030015434 scopus 로고    scopus 로고
    • Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice
    • 8673140 10.1038/ng0796-366
    • van der Neut R, Krimpenfort P, Calafat J, Niessen CM, Sonnenberg A (1996) Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice. Nat Genet 13:366-369
    • (1996) Nat Genet , vol.13 , pp. 366-369
    • Van Der Neut, R.1    Krimpenfort, P.2    Calafat, J.3    Niessen, C.M.4    Sonnenberg, A.5
  • 139
    • 84880689857 scopus 로고    scopus 로고
    • Stabilization of the dystroglycan complex in Cajal bands of myelinating Schwann cells through plectin-mediated anchorage of vimentin filaments
    • (in press)
    • Walko G, Wögenstein K, Winter L, Fischer I, Feltri L, Wiche G (2013) Stabilization of the dystroglycan complex in Cajal bands of myelinating Schwann cells through plectin-mediated anchorage of vimentin filaments. Glia (in press)
    • (2013) Glia
    • Walko G, W.1
  • 140
    • 84992236576 scopus 로고    scopus 로고
    • Plectin isoforms as organizers of intermediate filament cytoarchitecture
    • 21866256 10.4161/bioa.1.1.14630
    • Wiche G, Winter L (2011) Plectin isoforms as organizers of intermediate filament cytoarchitecture. Bioarchitecture 1:14-20
    • (2011) Bioarchitecture , vol.1 , pp. 14-20
    • Wiche, G.1    Winter, L.2
  • 141
    • 0020612365 scopus 로고
    • Occurrence and immunolocalization of plectin in tissues
    • 6350322 1:CAS:528:DyaL3sXltlOht7g%3D 10.1083/jcb.97.3.887
    • Wiche G, Krepler R, Artlieb U, Pytela R, Denk H (1983) Occurrence and immunolocalization of plectin in tissues. J Cell Biol 97:887-901
    • (1983) J Cell Biol , vol.97 , pp. 887-901
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Denk, H.5
  • 142
    • 0021749865 scopus 로고
    • Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes
    • 6386498 1:CAS:528:DyaL2cXmt1Onurc%3D 10.1016/0014-4827(84)90766-3
    • Wiche G, Krepler R, Artlieb U, Pytela R, Aberer W (1984) Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp Cell Res 155:43-49
    • (1984) Exp Cell Res , vol.155 , pp. 43-49
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Aberer, W.5
  • 143
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil
    • 2050743 1:CAS:528:DyaK38Xht1entLw%3D 10.1083/jcb.114.1.83
    • Wiche G, Becker B, Luber K, Weitzer G, Castañón MJ, Hauptmann R, Stratowa C, Stewart M (1991) Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil. J Cell Biol 114:83-99
    • (1991) J Cell Biol , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castañón, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 144
  • 145
    • 84872350268 scopus 로고    scopus 로고
    • The many faces of plectin and plectinopathies: Pathology and mechanisms
    • 22864774 1:CAS:528:DC%2BC3sXktVyrtg%3D%3D 10.1007/s00401-012-1026-0
    • Winter L, Wiche G (2013) The many faces of plectin and plectinopathies: pathology and mechanisms. Acta Neuropathol 125:77-93
    • (2013) Acta Neuropathol , vol.125 , pp. 77-93
    • Winter, L.1    Wiche, G.2
  • 146
    • 45349095416 scopus 로고    scopus 로고
    • Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape
    • 18541706 1:CAS:528:DC%2BD1cXns1yms7Y%3D 10.1083/jcb.200710151
    • Winter L, Abrahamsberg C, Wiche G (2008) Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape. J Cell Biol 181:903-911
    • (2008) J Cell Biol , vol.181 , pp. 903-911
    • Winter, L.1    Abrahamsberg, C.2    Wiche, G.3
  • 147
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • 8752219 1:CAS:528:DyaK28XltleqtL4%3D 10.1016/S0092-8674(00)80138-5
    • Yang Y, Dowling J, Yu QC, Kouklis P, Cleveland DW, Fuchs E (1996) An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. Cell 86:655-665
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6
  • 148
    • 0029982832 scopus 로고    scopus 로고
    • Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli
    • 8686756 1:CAS:528:DyaK28XkslKhtr0%3D
    • Yaoita E, Wiche G, Yamamoto T, Kawasaki K, Kihara I (1996) Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli. Am J Pathol 149:319-327
    • (1996) Am J Pathol , vol.149 , pp. 319-327
    • Yaoita, E.1    Wiche, G.2    Yamamoto, T.3    Kawasaki, K.4    Kihara, I.5
  • 150
    • 0021828068 scopus 로고
    • Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: Immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin
    • 2992982 1:STN:280:DyaL2M3osFWgtw%3D%3D
    • Zernig G, Wiche G (1985) Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin. Eur J Cell Biol 38:113-122
    • (1985) Eur J Cell Biol , vol.38 , pp. 113-122
    • Zernig, G.1    Wiche, G.2
  • 151
    • 0345874728 scopus 로고    scopus 로고
    • Multiple variable first exons: A mechanism for cell- and tissue-specific gene regulation
    • 14672974 1:CAS:528:DC%2BD2cXlvVGmsQ%3D%3D 10.1101/gr.1225204
    • Zhang T, Haws P, Wu Q (2004) Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res 14:79-89
    • (2004) Genome Res , vol.14 , pp. 79-89
    • Zhang, T.1    Haws, P.2    Wu, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.