메뉴 건너뛰기




Volumn 329, Issue 1, 2003, Pages 15-33

An atomic model for actin binding by the CH domains and spectrin-repeat modules of utrophin and dystrophin

Author keywords

Actin; Calponin homology domain; Dystrophin; Spectrin repeat; Utrophin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; AMINO ACID; CALPONIN; DIMER; DYSTROPHIN; F ACTIN; MONOMER; SPECTRIN; TROPOMYOSIN; UTROPHIN;

EID: 0038554286     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00422-4     Document Type: Article
Times cited : (62)

References (63)
  • 1
    • 0034280902 scopus 로고    scopus 로고
    • An attempt of gene therapy in Duchenne muscular dystrophy: Overexpression of utrophin in transgenic mdx mice
    • Gillis J.-M. An attempt of gene therapy in Duchenne muscular dystrophy: overexpression of utrophin in transgenic mdx mice. Acta Neurol. Belg. 100:2000;146-200.
    • (2000) Acta Neurol. Belg. , vol.100 , pp. 146-200
    • Gillis, J.-M.1
  • 2
    • 0034574069 scopus 로고    scopus 로고
    • Structural comparison of actin binding in utrophin and dystrophin
    • Keep N.H. Structural comparison of actin binding in utrophin and dystrophin. Neurol. Sci. 21:2000;S929-S937.
    • (2000) Neurol. Sci. , vol.21
    • Keep, N.H.1
  • 3
    • 0036087342 scopus 로고    scopus 로고
    • Function and genetics of dystrophin and dystrophin-related proteins in muscle
    • Blake D.J., Weir A., Newey S.E., Davies K.E. Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol. Rev. 82:2002;291-329.
    • (2002) Physiol. Rev. , vol.82 , pp. 291-329
    • Blake, D.J.1    Weir, A.2    Newey, S.E.3    Davies, K.E.4
  • 5
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122:1993;809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 7
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana J., Saraste M. Does Vav bind to F-actin through a CH domain? FEBS Letters. 374:1995;149-151.
    • (1995) FEBS Letters , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 9
    • 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
  • 11
    • 0028306603 scopus 로고
    • Deletion analysis of the dystrophin-actin binding domain
    • Corrado K., Mills P.L., Chamberlain J.S. Deletion analysis of the dystrophin-actin binding domain. FEBS Letters. 344:1994;255-260.
    • (1994) FEBS Letters , vol.344 , pp. 255-260
    • Corrado, K.1    Mills, P.L.2    Chamberlain, J.S.3
  • 13
    • 0026655006 scopus 로고
    • The identification and characterisation of an actin-binding site in α-actinin by mutagenesis
    • Kuhlman P.A., Hemmings L., Critchley D.R. The identification and characterisation of an actin-binding site in α-actinin by mutagenesis. FEBS Letters. 304:1992;201-206.
    • (1992) FEBS Letters , vol.304 , pp. 201-206
    • Kuhlman, P.A.1    Hemmings, L.2    Critchley, D.R.3
  • 14
    • 0026596306 scopus 로고
    • Analysis of the actin-binding domain of α-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 α-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
  • 15
    • 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
  • 16
    • 0026595121 scopus 로고
    • Binding sites involved in the interaction of actin with the N-terminal region of dystrophin
    • Levine B.A., Moir A.J.G., Patchell V.B., Perry S.V. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Letters. 298:1992;44-48.
    • (1992) FEBS Letters , vol.298 , pp. 44-48
    • Levine, B.A.1    Moir, A.J.G.2    Patchell, V.B.3    Perry, S.V.4
  • 17
    • 0032930086 scopus 로고    scopus 로고
    • Disruption of the utrophin-actin interaction by monoclonal antibodies and prediction of an actin-binding surface of utrophin
    • Morris G.E., Man N.T., Huyen N.T.N., Pereboev A., Kendrick-Jones J., Winder S.J. Disruption of the utrophin-actin interaction by monoclonal antibodies and prediction of an actin-binding surface of utrophin. Biochem. J. 337:1999;119-123.
    • (1999) Biochem. J. , vol.337 , pp. 119-123
    • Morris, G.E.1    Man, N.T.2    Huyen, N.T.N.3    Pereboev, A.4    Kendrick-Jones, J.5    Winder, S.J.6
  • 18
    • 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.M., 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. Structure. 8:2000;481-491.
    • (2000) Structure , vol.8 , pp. 481-491
    • Norwood, F.L.M.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 21
    • 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. J. Cell Motil. Cytoskeleton. 46:2000;116-128.
    • (2000) J. Cell Motil. Cytoskeleton , vol.46 , pp. 116-128
    • Moores, C.A.1    Kendrick-Jones, J.2
  • 23
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo K., Gautel M., Ylanne J., Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Letters. 513:2002;119-123.
    • (2002) FEBS Letters , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 24
    • 0029906168 scopus 로고    scopus 로고
    • Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene
    • Tinsley J.M., Potter A.C., Phelps S.R., Fisher R., Trickett J.I., Davies K.E. Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene. Nature. 384:1996;349-353.
    • (1996) Nature , vol.384 , pp. 349-353
    • Tinsley, J.M.1    Potter, A.C.2    Phelps, S.R.3    Fisher, R.4    Trickett, J.I.5    Davies, K.E.6
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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
  • 29
    • 0031694478 scopus 로고    scopus 로고
    • An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation
    • Hanein D., Volkmann N., Goldsmith S., Michon A.M., Lehman W., Craig R., et al. An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation. Nature Struct. Biol. 5:1998;787-792.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 787-792
    • Hanein, D.1    Volkmann, N.2    Goldsmith, S.3    Michon, A.M.4    Lehman, W.5    Craig, R.6
  • 30
  • 31
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W., Hatch V., Korman V., Rosol M., Thomas L., Maytum R., et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J. Mol. Biol. 302:2000;593-606.
    • (2000) J. Mol. Biol. , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 32
    • 0026593808 scopus 로고
    • Expression of the N-terminal domain of dystrophin in E. coli and demonstration of binding to F-actin
    • Way M., Pope B., Cross R.A., Kendrick-Jones J., Weeds A.G. Expression of the N-terminal domain of dystrophin in E. coli and demonstration of binding to F-actin. FEBS Letters. 301:1992;243-245.
    • (1992) FEBS Letters , vol.301 , pp. 243-245
    • Way, M.1    Pope, B.2    Cross, R.A.3    Kendrick-Jones, J.4    Weeds, A.G.5
  • 34
    • 0029967315 scopus 로고    scopus 로고
    • Structure-function relationships in dystrophin and utrophin
    • Winder S.J. Structure-function relationships in dystrophin and utrophin. Biochem. Soc. Trans. 24:1996;497-501.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 497-501
    • Winder, S.J.1
  • 35
    • 0032561199 scopus 로고    scopus 로고
    • A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction
    • Amann K.J., Renley B.A., Ervasti J.M. A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J. Biol. Chem. 273:1998;28419-28423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28419-28423
    • Amann, K.J.1    Renley, B.A.2    Ervasti, J.M.3
  • 37
    • 0035999982 scopus 로고    scopus 로고
    • Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle
    • Rybakova I.N., Patel J.R., Davies K.E., Yurchenco P.D., Ervasti J.M. Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle. Mol. Biol. Cell. 13:2002;1512-1521.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1512-1521
    • Rybakova, I.N.1    Patel, J.R.2    Davies, K.E.3    Yurchenco, P.D.4    Ervasti, J.M.5
  • 38
    • 0035069182 scopus 로고    scopus 로고
    • Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure
    • Orlova A., Rybakova I.N., Prochniewicz E., Thomas D.D., Ervasti J.M., Egelman E.H. Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure. Biophys. J. 80:2001;1926-1931.
    • (2001) Biophys. J. , vol.80 , pp. 1926-1931
    • Orlova, A.1    Rybakova, I.N.2    Prochniewicz, E.3    Thomas, D.D.4    Ervasti, J.M.5    Egelman, E.H.6
  • 39
    • 0028176006 scopus 로고
    • Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough A., Way M., DeRosier D. Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126:1994;433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 40
    • 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
  • 42
    • 12544250909 scopus 로고    scopus 로고
    • Actin and actin binding proteins
    • Chapt. 36, Saunders, Philadelphia
    • Pollard, T. D. & Earnshaw, W. C. (2002). Actin and actin binding proteins. In Cell Biology, Chapt. 36, Saunders, Philadelphia pp. 566-567.
    • (2002) Cell Biology , pp. 566-567
    • Pollard, T.D.1    Earnshaw, W.C.2
  • 43
    • 0026472782 scopus 로고
    • Assembly of the intestinal brush border cytoskeleton
    • Heintzelman M.B., Mooseker M.S. Assembly of the intestinal brush border cytoskeleton. Curr. Top. Dev. Biol. 26:1992;93-122.
    • (1992) Curr. Top. Dev. Biol. , vol.26 , pp. 93-122
    • Heintzelman, M.B.1    Mooseker, M.S.2
  • 44
    • 0026685853 scopus 로고
    • The differentiating intestinal epithelial cell: Establishment and maintenance of functions through interactions between cellular structures
    • Louvard D., Kedinger M., Hauri H.P. The differentiating intestinal epithelial cell: establishment and maintenance of functions through interactions between cellular structures. Annu. Rev. Cell Biol. 8:1992;157-195.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 157-195
    • Louvard, D.1    Kedinger, M.2    Hauri, H.P.3
  • 45
    • 0032561199 scopus 로고    scopus 로고
    • A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction
    • Amann K.J., Renley B.A., Ervasti J.M. A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J. Biol. Chem. 273:1998;28419-28423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28419-28423
    • Amann, K.J.1    Renley, B.A.2    Ervasti, J.M.3
  • 46
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 47
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 48
    • 0025308841 scopus 로고
    • Caldesmon and the structure of vertebrate smooth muscle thin filaments: Electron microscopy of isolated thin filaments
    • Moody C., Lehman W., Craig R. Caldesmon and the structure of vertebrate smooth muscle thin filaments: electron microscopy of isolated thin filaments. J. Muscle Res. Cell Motil. 11:1990;176-185.
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 176-185
    • Moody, C.1    Lehman, W.2    Craig, R.3
  • 49
    • 0022928662 scopus 로고
    • An algorithm for straightening images of curved filamentous structures
    • Egelman E.H. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy. 19:1986;367-374.
    • (1986) Ultramicroscopy , vol.19 , pp. 367-374
    • Egelman, E.H.1
  • 50
    • 0029916489 scopus 로고    scopus 로고
    • Image analysis of helical objects: The Brandeis helical package
    • Owen C., Morgan D.G., DeRosier D.J. Image analysis of helical objects: the Brandeis helical package. J. Struct. Biol. 116:1996;167-175.
    • (1996) J. Struct. Biol. , vol.116 , pp. 167-175
    • Owen, C.1    Morgan, D.G.2    DeRosier, D.J.3
  • 51
    • 0027514929 scopus 로고
    • Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments
    • Vibert P., Craig R., Lehman W. Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments. J. Cell Biol. 123:1993;313-321.
    • (1993) J. Cell Biol. , vol.123 , pp. 313-321
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 52
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin and tropomyosin revealed by cryo-electron microscopy
    • Milligan R.A., Flicker P.F. Structural relationships of actin, myosin and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105:1987;29-39.
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 53
    • 0023644892 scopus 로고
    • Three-dimensional structure of frozen hydrated flagellar filament of Salmonella typhimurium
    • Trachtenberg S., DeRosier D.J. Three-dimensional structure of frozen hydrated flagellar filament of Salmonella typhimurium. J. Mol. Biol. 195:1987;581-601.
    • (1987) J. Mol. Biol. , vol.195 , pp. 581-601
    • Trachtenberg, S.1    DeRosier, D.J.2
  • 54
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by use of a directed mutation algorithm
    • Lorenz M., Popp D., Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by use of a directed mutation algorithm. J. Mol. Biol. 234:1993;826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 55
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 56
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125:1999;185-195.
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 57
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacon P., Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317:2002;375-384.
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacon, P.1    Wriggers, W.2
  • 61
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum V.L., Li D., MacDonald R.I., Mondragon A. Structures of two repeats of spectrin suggest models of flexibility. Cell. 98:1999;523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 62
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo K., Young P., Gautel M., Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell. 98:1999;537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.