메뉴 건너뛰기




Volumn 11, Issue 6, 2003, Pages 615-625

Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin β4

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA6 INTEGRIN; BETA4 INTEGRIN; F ACTIN; PLECTIN; PROTEIN SUBUNIT;

EID: 0141631492     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00090-X     Document Type: Article
Times cited : (83)

References (66)
  • 1
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andra 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. 11:1997;3143-3156.
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassler, R.5    Propst, F.6    Wiche, G.7
  • 2
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: Plectin regulates actin dynamics in cultured cells
    • Andra K., Nikolic B., Stocher M., Drenckhahn D., Wiche G. Not just scaffolding. plectin regulates actin dynamics in cultured cells Genes Dev. 12:1998;3442-3451.
    • (1998) Genes Dev. , vol.12 , pp. 3442-3451
    • Andra, K.1    Nikolic, B.2    Stocher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 3
    • 0032533444 scopus 로고    scopus 로고
    • Structural comparisons of calponin homology domains: Implications for actin binding
    • Banuelos S., Saraste M., Carugo K.D. Structural comparisons of calponin homology domains. implications for actin binding Structure. 6:1998;1419-1431.
    • (1998) Structure , vol.6 , pp. 1419-1431
    • Banuelos, S.1    Saraste, M.2    Carugo, K.D.3
  • 4
    • 0036180282 scopus 로고    scopus 로고
    • Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin
    • Bramham J., Hodgkinson J.L., Smith B.O., Uhrin D., Barlow P.N., Winder S.J. Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin. Structure. 10:2002;249-258.
    • (2002) Structure , vol.10 , pp. 249-258
    • Bramham, J.1    Hodgkinson, J.L.2    Smith, B.O.3    Uhrin, D.4    Barlow, P.N.5    Winder, S.J.6
  • 5
    • 0025293017 scopus 로고
    • Identification of a short sequence essential for actin binding by Dictyostelium ABP-120
    • Bresnick A.R., Warren V., Condeelis J. Identification of a short sequence essential for actin binding by Dictyostelium ABP-120. J. Biol. Chem. 265:1990;9236-9240.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9236-9240
    • Bresnick, A.R.1    Warren, V.2    Condeelis, J.3
  • 8
    • 0034705330 scopus 로고    scopus 로고
    • Reconstruction of protein form with X-ray solution scattering and a genetic algorithm
    • Chacon P., Diaz J.F., Moran F., Andreu J.M. Reconstruction of protein form with X-ray solution scattering and a genetic algorithm. J. Mol. Biol. 299:2000;1289-1302.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1289-1302
    • Chacon, P.1    Diaz, J.F.2    Moran, F.3    Andreu, J.M.4
  • 9
    • 0036316492 scopus 로고    scopus 로고
    • Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure
    • Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I. Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure. Nat. Struct. Biol. 9:2002;612-620.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 612-620
    • Choi, H.J.1    Park-Snyder, S.2    Pascoe, L.T.3    Green, K.J.4    Weis, W.I.5
  • 11
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • de Arruda M.V., Watson S., Lin C.S., Leavitt J., Matsudaira P. Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111:1990;1069-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • De Arruda, M.V.1    Watson, S.2    Lin, C.S.3    Leavitt, J.4    Matsudaira, P.5
  • 12
    • 0033517122 scopus 로고    scopus 로고
    • Crystal structure of a tandem pair of fibronectin type III domains from the cytoplasmic tail of integrin alpha6beta4
    • de Pereda J.M., Wiche G., Liddington R.C. Crystal structure of a tandem pair of fibronectin type III domains from the cytoplasmic tail of integrin alpha6beta4. EMBO J. 18:1999;4087-4095.
    • (1999) EMBO J. , vol.18 , pp. 4087-4095
    • De Pereda, J.M.1    Wiche, G.2    Liddington, R.C.3
  • 13
    • 0026291627 scopus 로고
    • Creation of a T7 autogene. Cloning and expression of the gene for bacteriophage T7 RNA polymerase under control of its cognate promoter
    • Dubendorff J.W., Studier F.W. Creation of a T7 autogene. Cloning and expression of the gene for bacteriophage T7 RNA polymerase under control of its cognate promoter. J. Mol. Biol. 219:1991;61-68.
    • (1991) J. Mol. Biol. , vol.219 , pp. 61-68
    • Dubendorff, J.W.1    Studier, F.W.2
  • 14
    • 0030906239 scopus 로고    scopus 로고
    • Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells
    • Eger A., Stockinger A., Wiche G., Foisner R. Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells. J. Cell Sci. 110:1997;1307-1316.
    • (1997) J. Cell Sci. , vol.110 , pp. 1307-1316
    • Eger, A.1    Stockinger, A.2    Wiche, G.3    Foisner, R.4
  • 15
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner R., Wiche G. Structure and hydrodynamic properties of plectin molecules. J. Mol. Biol. 198:1987;515-531.
    • (1987) J. Mol. Biol. , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 16
    • 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. 106:1988;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
  • 17
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner R., Traub P., Wiche G. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. USA. 88:1991;3812-3816.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 18
    • 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. 7:1996;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
  • 19
    • 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
    • Fontao L., Geerts D., Kuikman I., Koster J., Kramer D., Sonnenberg A. 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. 114:2001;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
  • 21
    • 0033520387 scopus 로고    scopus 로고
    • Crossroads on cytoskeletal highways
    • Fuchs E., Yang Y. Crossroads on cytoskeletal highways. Cell. 98:1999;547-550.
    • (1999) Cell , vol.98 , pp. 547-550
    • Fuchs, E.1    Yang, Y.2
  • 23
    • 0037092046 scopus 로고    scopus 로고
    • The utrophin actin-binding domain binds F-actin in two different modes: Implications for the spectrin superfamily of proteins
    • Galkin V.E., Orlova A., VanLoock M.S., Rybakova I.N., Ervasti J.M., Egelman E.H. The utrophin actin-binding domain binds F-actin in two different modes. implications for the spectrin superfamily of proteins J. Cell Biol. 157:2002;243-251.
    • (2002) J. Cell Biol. , vol.157 , pp. 243-251
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Rybakova, I.N.4    Ervasti, J.M.5    Egelman, E.H.6
  • 24
    • 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. 147:1999;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
  • 26
    • 0030727339 scopus 로고    scopus 로고
    • Evidence for a conformational change in actin induced by fimbrin (N375) binding
    • Hanein D., Matsudaira P., DeRosier D.J. Evidence for a conformational change in actin induced by fimbrin (N375) binding. J. Cell Biol. 139:1997;387-396.
    • (1997) J. Cell Biol. , vol.139 , pp. 387-396
    • Hanein, D.1    Matsudaira, P.2    DeRosier, D.J.3
  • 28
    • 0024046835 scopus 로고
    • Model building of disulfide bonds in proteins with known three-dimensional structure
    • Hazes B., Dijkstra B.W. Model building of disulfide bonds in proteins with known three-dimensional structure. Protein Eng. 2:1988;119-125.
    • (1988) Protein Eng. , vol.2 , pp. 119-125
    • Hazes, B.1    Dijkstra, B.W.2
  • 29
    • 0026596306 scopus 로고
    • Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain
    • Hemmings L., Kuhlman P.A., Critchley D.R. Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J. Cell Biol. 116:1992;1369-1380.
    • (1992) J. Cell Biol. , vol.116 , pp. 1369-1380
    • Hemmings, L.1    Kuhlman, P.A.2    Critchley, D.R.3
  • 30
    • 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. 262:1987;1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 31
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda Y., Nishizawa Y., Uematsu J., Owaribe K. Identification of a new hemidesmosomal protein, HD1. a major, high molecular mass component of isolated hemidesmosomes J. Cell Biol. 116:1992;1497-1506.
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 32
    • 0031576324 scopus 로고    scopus 로고
    • 3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin: Visualization of interactions between F-actin and calponin
    • Hodgkinson J.L., el-Mezgueldi M., Craig R., Vibert P., Marston S.B., Lehman W. 3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin. visualization of interactions between F-actin and calponin J. Mol. Biol. 273:1997;150-159.
    • (1997) J. Mol. Biol. , vol.273 , pp. 150-159
    • Hodgkinson, J.L.1    El-Mezgueldi, M.2    Craig, R.3    Vibert, P.4    Marston, S.B.5    Lehman, W.6
  • 33
    • 0033593116 scopus 로고    scopus 로고
    • The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin
    • a
    • Keep N.H., Norwood F.L., Moores C.A., Winder S.J., Kendrick-Jones J. The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. J. Mol. Biol. 285:1999;1257-1264. a.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1257-1264
    • Keep, N.H.1    Norwood, F.L.2    Moores, C.A.3    Winder, S.J.4    Kendrick-Jones, J.5
  • 35
    • 0035670672 scopus 로고    scopus 로고
    • Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin
    • Koster J., Kuikman I., Kreft M., Sonnenberg A. Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin. J. Invest. Dermatol. 117:2001;1405-1411.
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 1405-1411
    • Koster, J.1    Kuikman, I.2    Kreft, M.3    Sonnenberg, A.4
  • 36
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 38
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg
    • Lee G.F., Burrows G.G., Lebert M.R., Dutton D.P., Hazelbauer G.L. Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg. J. Biol. Chem. 269:1994;29920-29927.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 39
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: A family of versatile cytolinker proteins
    • Leung C.L., Green K.J., Liem R.K. Plakins. a family of versatile cytolinker proteins Trends Cell Biol. 12:2002;37-45.
    • (2002) Trends Cell Biol. , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.3
  • 40
    • 0026595121 scopus 로고
    • Binding sites involved in the interaction of actin with the N-terminal region of dystrophin
    • Levine B.A., Moir A.J., Patchell V.B., Perry S.V. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Lett. 298:1992;44-48.
    • (1992) FEBS Lett. , vol.298 , pp. 44-48
    • Levine, B.A.1    Moir, A.J.2    Patchell, V.B.3    Perry, S.V.4
  • 43
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y., Eisenberg D. 3D domain swapping. As domains continue to swap Protein Sci. 11:2002;1285-1299.
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 44
    • 0029873478 scopus 로고    scopus 로고
    • Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site
    • Malecz N., Foisner R., Stadler C., Wiche G. Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. J. Biol. Chem. 271:1996;8203-8208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8203-8208
    • Malecz, N.1    Foisner, R.2    Stadler, C.3    Wiche, G.4
  • 45
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster 3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 46
    • 0033918661 scopus 로고    scopus 로고
    • Biochemical characterisation of the actin-binding properties of utrophin
    • Moores C.A., Kendrick-Jones J. Biochemical characterisation of the actin-binding properties of utrophin. Cell Motil. Cytoskeleton. 46:2000;116-128.
    • (2000) Cell Motil. Cytoskeleton , vol.46 , pp. 116-128
    • Moores, C.A.1    Kendrick-Jones, J.2
  • 47
    • 0034708341 scopus 로고    scopus 로고
    • Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism
    • Moores C.A., Keep N.H., Kendrick-Jones J. Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism. J. Mol. Biol. 297:2000;465-480.
    • (2000) J. Mol. Biol. , vol.297 , pp. 465-480
    • Moores, C.A.1    Keep, N.H.2    Kendrick-Jones, J.3
  • 48
    • 0030820604 scopus 로고    scopus 로고
    • A minimal region on the integrin beta4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells
    • a
    • Niessen C.M., Hulsman E.H., Oomen L.C., Kuikman I., Sonnenberg A. A minimal region on the integrin beta4 subunit that is critical to its localization in hemidesmosomes regulates the distribution of HD1/plectin in COS-7 cells. J. Cell Sci. 110:1997;1705-1716. a.
    • (1997) J. Cell Sci. , vol.110 , pp. 1705-1716
    • Niessen, C.M.1    Hulsman, E.H.2    Oomen, L.C.3    Kuikman, I.4    Sonnenberg, A.5
  • 49
    • 0030975508 scopus 로고    scopus 로고
    • Integrin alpha 6 beta 4 forms a complex with the cytoskeletal protein HD1 and induces its redistribution in transfected COS-7 cells
    • b
    • Niessen C.M., Hulsman E.H., Rots E.S., Sanchez-Aparicio P., Sonnenberg A. Integrin alpha 6 beta 4 forms a complex with the cytoskeletal protein HD1 and induces its redistribution in transfected COS-7 cells. Mol. Biol. Cell. 8:1997;555-566. b.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 555-566
    • Niessen, C.M.1    Hulsman, E.H.2    Rots, E.S.3    Sanchez-Aparicio, P.4    Sonnenberg, A.5
  • 50
    • 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. 134:1996;1455-1467.
    • (1996) J. Cell Biol. , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 51
    • 0034657791 scopus 로고    scopus 로고
    • The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
    • Norwood F.L., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Struct. Fold. Des. 8:2000;481-491.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 481-491
    • Norwood, F.L.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 52
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 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
    • Pytela R., Wiche G. 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. 77:1980;4808-4812.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 55
    • 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
    • Rezniczek G.A., de Pereda J.M., Reipert S., Wiche G. 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. 141:1998;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
  • 57
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: Versatile organizers of cytoskeletal architecture
    • Ruhrberg C., Watt F.M. The plakin family. versatile organizers of cytoskeletal architecture Curr. Opin. Genet. Dev. 7:1997;392-397.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, F.M.2
  • 58
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert G.J., Lawson D., Wiche G. Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell Biol. 59:1992;138-147.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 138-147
    • Seifert, G.J.1    Lawson, D.2    Wiche, G.3
  • 59
    • 0033053121 scopus 로고    scopus 로고
    • Plectin: A cytolinker by design
    • Steinbock F.A., Wiche G. Plectin. a cytolinker by design Biol. Chem. 380:1999;151-158.
    • (1999) Biol. Chem. , vol.380 , pp. 151-158
    • Steinbock, F.A.1    Wiche, G.2
  • 60
    • 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. 113:2000;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
  • 62
    • 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. 135:1996;991-1007.
    • (1996) J. Cell Biol. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 63
    • 0029829634 scopus 로고    scopus 로고
    • Plectin and human genetic disorders of the skin and muscle. The paradigm of epidermolysis bullosa with muscular dystrophy
    • Uitto J., Pulkkinen L., Smith F.J., McLean W.H. Plectin and human genetic disorders of the skin and muscle. The paradigm of epidermolysis bullosa with muscular dystrophy. Exp. Dermatol. 5:1996;237-246.
    • (1996) Exp. Dermatol. , vol.5 , pp. 237-246
    • Uitto, J.1    Pulkkinen, L.2    Smith, F.J.3    McLean, W.H.4
  • 64
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • Volkmann N., DeRosier D., Matsudaira P., Hanein D. An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 153:2001;947-956.
    • (2001) J. Cell Biol. , vol.153 , pp. 947-956
    • Volkmann, N.1    DeRosier, D.2    Matsudaira, P.3    Hanein, D.4
  • 65
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: Implications for the requirements of severing and capping
    • Way M., Pope B., Weeds A.G. Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin. implications for the requirements of severing and capping J. Cell Biol. 119:1992;835-842.
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.