메뉴 건너뛰기




Volumn 137, Issue 1-2, 2002, Pages 184-193

Towards a complete atomic structure of spectrin family proteins

Author keywords

Actin binding; CH domain; Coiled coil; Dystrophin; EF hands; PH domain; SH3 domain; Structure; Utrophin; WW domain; ZZ domain; actinin; spectrin; spectrin

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA ACTININ; DYSTROPHIN; SPECTRIN;

EID: 0036447290     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2002.4465     Document Type: Conference Paper
Times cited : (50)

References (67)
  • 2
    • 0023632004 scopus 로고
    • The sequence of chick α-actinin reveals homologies to spectrin and calmodulin
    • Baron, M. D., Davison, M. D., Jones, P., and Critchley, D. R. (1987) The sequence of chick α-actinin reveals homologies to spectrin and calmodulin. J. Biol. Chem. 262, 17623-17629.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17623-17629
    • Baron, M.D.1    Davison, M.D.2    Jones, P.3    Critchley, D.R.4
  • 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., Smith, B. O., Uhrin, D., Barlow, P. N., and Winder, S. J. (2002) Solution structure of the calponin CH domain and fitting to the 3D helical reconstruction of F-actin:calponin. Struct. Fold. Design 10, 249-258.
    • (2002) Struct. Fold. Design , vol.10 , pp. 249-258
    • Bramham, J.1    Hodgkinson, J.2    Smith, B.O.3    Uhrin, D.4    Barlow, P.N.5    Winder, S.J.6
  • 5
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana, J., and Saraste, M. (1995) Does Vav bind to F-actin through a CH domain? FEBS Lett. 374, 149-151.
    • (1995) FEBS Lett. , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 6
    • 0030795572 scopus 로고    scopus 로고
    • In vitro expressed dystrophin fragments do not associate with each other
    • Chan, Y.-M., and Kunkel, L. (1997) In vitro expressed dystrophin fragments do not associate with each other. FEBS Lett. 410, 153-159.
    • (1997) FEBS Lett. , vol.410 , pp. 153-159
    • Chan, Y.-M.1    Kunkel, L.2
  • 7
    • 0025234309 scopus 로고
    • Structural predictions for the central domain of dystrophin
    • Cross, R. A., Stewart, M., and Kendrick-Jones, J. (1990) Structural predictions for the central domain of dystrophin. FEBS Lett. 262, 87-92.
    • (1990) FEBS Lett. , vol.262 , pp. 87-92
    • Cross, R.A.1    Stewart, M.2    Kendrick-Jones, J.3
  • 8
    • 0024299114 scopus 로고
    • Alpha-actinins and the DMD protein contain spectrin-like repeats
    • Davison, M. D., and Critchley, D. R. (1988) Alpha-actinins and the DMD protein contain spectrin-like repeats. Cell 52, 159-160.
    • (1988) Cell , vol.52 , pp. 159-160
    • Davison, M.D.1    Critchley, D.R.2
  • 9
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • deArruda, M. V., Watson, S., Lin, C.-S., Levitt, J., and Matsudaira, P. (1990) Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111, 1069-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • DeArruda, M.V.1    Watson, S.2    Lin, C.-S.3    Levitt, J.4    Matsudaira, P.5
  • 11
    • 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., and Saraste, M. (1999) Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments. Cell 98, 537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 12
    • 0026165749 scopus 로고
    • Structure and evolution of the actin crosslinking proteins
    • Dubreuil, R. (1992) Structure and evolution of the actin crosslinking proteins. BioEssays 13, 219-226.
    • (1992) BioEssays , vol.13 , pp. 219-226
    • Dubreuil, R.1
  • 13
    • 0025886649 scopus 로고
    • Structure, calmodulin-binding, and calcium-binding properties of recombinant alpha-spectrin polypeptides
    • Dubreuil, R., Brandin, E., Reisberg, J., Goldstein, L., and Branton, D. (1991) Structure, calmodulin-binding, and calcium-binding properties of recombinant alpha-spectrin polypeptides. J. Biol. Chem. 266, 7189-7193.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7189-7193
    • Dubreuil, R.1    Brandin, E.2    Reisberg, J.3    Goldstein, L.4    Branton, D.5
  • 14
    • 0024449311 scopus 로고
    • The complete sequence of Drosophila alpha-spectrin: Conservation of structural domains between alpha-spectrins and alpha-actinin
    • Dubreuil, R., Byers, T., Sillman, A., Bar-Zvi, D., Goldstein, L., and Branton, D. (1989) The complete sequence of Drosophila alpha-spectrin: Conservation of structural domains between alpha-spectrins and alpha-actinin. J. Cell Biol. 109, 2197-2205.
    • (1989) J. Cell Biol. , vol.109 , pp. 2197-2205
    • Dubreuil, R.1    Byers, T.2    Sillman, A.3    Bar-Zvi, D.4    Goldstein, L.5    Branton, D.6
  • 15
    • 0023082024 scopus 로고
    • Isolation and characterisation of sea urchin spectrin: Calcium modulation of the spectrin-actin interaction
    • Fishkind, D. J., Bonder, E. M., and Begg, D. A. (1987) Isolation and characterisation of sea urchin spectrin: Calcium modulation of the spectrin-actin interaction. Cell Motil. Cytoskel. 7, 304-314.
    • (1987) Cell Motil. Cytoskel. , vol.7 , pp. 304-314
    • Fishkind, D.J.1    Bonder, E.M.2    Begg, D.A.3
  • 18
    • 0032563965 scopus 로고    scopus 로고
    • Single calponin homology domains are not actin binding domains
    • Gimona, M., and Winder, S. J. (1998) Single calponin homology domains are not actin binding domains. Curr. Biol. 8, R674-675.
    • (1998) Curr. Biol. , vol.8
    • Gimona, M.1    Winder, S.J.2
  • 20
    • 0020023993 scopus 로고
    • Preparation of spectrin
    • Gratzer, W. (1985) Preparation of spectrin. Methods Enzymol. 85, 475-480.
    • (1985) Methods Enzymol. , vol.85 , pp. 475-480
    • Gratzer, W.1
  • 21
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum, V., Li, D., MacDonald, R., and Mondragon, A. (1999) Structures of two repeats of spectrin suggest models of flexibility. Cell 98, 523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.1    Li, D.2    MacDonald, R.3    Mondragon, A.4
  • 23
    • 0343081091 scopus 로고    scopus 로고
    • Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan
    • Huang, X., Poy, F., Zhang, R., Joachimiak, A., Sudol, M., and Eck, M. J. (2000) Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan. Nat. Struct. Biol. 7, 634-638.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5    Eck, M.J.6
  • 25
    • 0036157980 scopus 로고    scopus 로고
    • The WW domain: Linking cell signalling to the membrane cytoskeleton
    • Ilsley, J. L., Sudol, M., and Winder, S. J. (2002) The WW domain: Linking cell signalling to the membrane cytoskeleton. Cell. Signal. 14, 183-189.
    • (2002) Cell. Signal. , vol.14 , pp. 183-189
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 26
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of β-dystroglycan regulates its interaction with utrophin
    • James, M., Nuttall, A., Ilsley, J. L., Ottersbach, K., Tinsley, J. N., Sudol, M., and Winder, S. J. (2000) Adhesion-dependent tyrosine phosphorylation of β-dystroglycan regulates its interaction with utrophin. J. Cell Sci. 113, 1717-1726.
    • (2000) J. Cell Sci. , vol.113 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.N.5    Sudol, M.6    Winder, S.J.7
  • 27
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signalling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P., and Sudol, M. (2000) The importance of being proline: The interaction of proline-rich motifs in signalling proteins with their cognate domains. FASEB J. 14, 231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 28
    • 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
    • Keep, N. H., Norwood, F. L. M., Moores, C. A., Winder, S. J., and Kendrick-Jones, J. (1998) 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, 1257-1264.
    • (1998) J. Mol. Biol. , vol.285 , pp. 1257-1264
    • Keep, N.H.1    Norwood, F.L.M.2    Moores, C.A.3    Winder, S.J.4    Kendrick-Jones, J.5
  • 31
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig, M., Monaco, A. P., and Kunkel, L. M. (1988) The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53, 219-226.
    • (1988) Cell , vol.53 , pp. 219-226
    • Koenig, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 34
    • 0028176006 scopus 로고
    • Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough, A., Way, M., and DeRosier, D. (1994) Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126, 433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 35
    • 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., and Kendrick-Jones, J. (2000) Structure of the utrophin actin-binding domain bound to F-actin reveals binding by an induced fit mechanism. J. Mol. Biol. 297, 465-480.
    • (2000) J. Mol. Biol. , vol.297 , pp. 465-480
    • Moores, C.A.1    Keep, N.H.2    Kendrick-Jones, J.3
  • 36
  • 38
    • 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., and Kendrick-Jones, J. (2000) 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. Design 8, 481-491.
    • (2000) Struct. Fold. Design , vol.8 , pp. 481-491
    • Norwood, F.L.M.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 39
    • 0026510756 scopus 로고
    • Analysis of the three-α-helix motif in the spectrin superfamily of proteins
    • Parry, D. A. D., Dixon, T. W., and Cohen, C. (1992) Analysis of the three-α-helix motif in the spectrin superfamily of proteins. Biophys. J. 61, 858-867.
    • (1992) Biophys. J. , vol.61 , pp. 858-867
    • Parry, D.A.D.1    Dixon, T.W.2    Cohen, C.3
  • 40
    • 0031239149 scopus 로고    scopus 로고
    • Evolution of the spectrin repeat
    • Pascual, J., Castresana, J., and Saraste, M. (1997) Evolution of the spectrin repeat. BioEssays 19, 811-817.
    • (1997) BioEssays , vol.19 , pp. 811-817
    • Pascual, J.1    Castresana, J.2    Saraste, M.3
  • 41
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual, J., Pfuhl, M., Rivas, G., Pastore, A., and Saraste, M. (1996) The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 383, 201-207.
    • (1996) FEBS Lett. , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 43
    • 0032915455 scopus 로고    scopus 로고
    • The WW domain of dystrophin requires EF-hands region to interact with β-dystroglycan
    • Rentschler, S., Linn, H., Deininger, K., Bedford, M. T., Espanel, X., and Sudol, M. (1999) The WW domain of dystrophin requires EF-hands region to interact with β-dystroglycan. Biol. Chem. 380, 431-442.
    • (1999) Biol. Chem. , vol.380 , pp. 431-442
    • Rentschler, S.1    Linn, H.2    Deininger, K.3    Bedford, M.T.4    Espanel, X.5    Sudol, M.6
  • 44
    • 0029804981 scopus 로고    scopus 로고
    • A new model for the interaction of dystrophin with F-actin
    • Rybakova, I. N., Amman, K. J., and Ervasti, J. M. (1996) A new model for the interaction of dystrophin with F-actin. J. Cell Biol. 135, 661-672.
    • (1996) J. Cell Biol. , vol.135 , pp. 661-672
    • Rybakova, I.N.1    Amman, K.J.2    Ervasti, J.M.3
  • 45
    • 0030695947 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through a lateral association
    • Rybakova, I. N., and Ervasti, J. M. (1997) Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through a lateral association. J. Biol. Chem. 272, 28771-28778.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28771-28778
    • Rybakova, I.N.1    Ervasti, J.M.2
  • 47
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher, D. W., and Marchesi, V. T. (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311, 177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 50
    • 0027474019 scopus 로고
    • Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers
    • Taylor, K. A., and Taylor, D. W. (1993) Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J. Mol. Biol. 230, 196-205.
    • (1993) J. Mol. Biol. , vol.230 , pp. 196-205
    • Taylor, K.A.1    Taylor, D.W.2
  • 51
  • 52
    • 0028785099 scopus 로고
    • Molecular mechanism of the calcium-induced change in the spectrin EF-hands
    • Trave, G., Lacombe, P.-J., Pfuhl, M., Saraste, M., and Pastore, A. (1995) Molecular mechanism of the calcium-induced change in the spectrin EF-hands. EMBO J. 14, 4922-4931.
    • (1995) EMBO J. , vol.14 , pp. 4922-4931
    • Trave, G.1    Lacombe, P.-J.2    Pfuhl, M.3    Saraste, M.4    Pastore, A.5
  • 53
    • 0016627986 scopus 로고
    • Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme
    • Tufty, R. M., and Kretsinger, R. H. (1975) Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 187, 167-169.
    • (1975) Science , vol.187 , pp. 167-169
    • Tufty, R.M.1    Kretsinger, R.H.2
  • 54
    • 0026732937 scopus 로고
    • Characterization of calcium-binding to brain spectrin
    • Wallis, C., Wenegieme, E., and Babitch, J. (1992) Characterization of calcium-binding to brain spectrin. J. Biol. Chem. 267, 4333-4337.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4333-4337
    • Wallis, C.1    Wenegieme, E.2    Babitch, J.3
  • 56
    • 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., and Weeds, A. G. (1992) 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, 835-842.
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 57
    • 0030668762 scopus 로고    scopus 로고
    • The membrane-cytoskeleton interface: The role of dystrophin and utrophin
    • Winder, S. J. (1997) The membrane-cytoskeleton interface: The role of dystrophin and utrophin. J. Muscle Res. Cell Motil. 18, 617-629.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 617-629
    • Winder, S.J.1
  • 58
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder, S. J. (2001) The complexities of dystroglycan. Trends Biochem. Sci. 26, 118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 59
    • 0029117231 scopus 로고
    • Dystrophin and utrophin: The missing links
    • Winder, S. J., Gibson, T. J., and Kendrick-Jones, J. (1995a) Dystrophin and utrophin: The missing links. FEBS Lett. 369, 27-33.
    • (1995) FEBS Lett. , vol.369 , pp. 27-33
    • Winder, S.J.1    Gibson, T.J.2    Kendrick-Jones, J.3
  • 60
    • 0029934409 scopus 로고    scopus 로고
    • Low probability of dystrophin and utrophin coiled coil regions forming dimers
    • Winder, S. J., Gibson, T. J., and Kendrick-Jones, J. (1996) Low probability of dystrophin and utrophin coiled coil regions forming dimers. Biochem. Soc. Trans. 24, 280S.
    • (1996) Biochem. Soc. Trans. , vol.24
    • Winder, S.J.1    Gibson, T.J.2    Kendrick-Jones, J.3
  • 63
    • 0025348420 scopus 로고
    • Smooth muscle calponin: Inhibition of the actomyosin MgATPase and regulation by phosphorylation
    • Winder, S. J., and Walsh, M. P. (1990) Smooth muscle calponin: Inhibition of the actomyosin MgATPase and regulation by phosphorylation. J. Biol. Chem. 265, 10148-10155.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10148-10155
    • Winder, S.J.1    Walsh, M.P.2
  • 64
    • 0027301038 scopus 로고
    • Erythroid and non-erythroid spectrins
    • Winkelmann, J., and Forget, B. (1993) Erythroid and non-erythroid spectrins. Blood 81, 3173-3185.
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.1    Forget, B.2
  • 66
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the α-actinin rod reveals an extensive torsional twist
    • Ylanne, J., Scheffzek, K., Young, P., and Saraste, M. (2001) Crystal structure of the α-actinin rod reveals an extensive torsional twist. Struct. Fold. Design 9, 597-604.
    • (2001) Struct. Fold. Design , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 67
    • 0029645869 scopus 로고
    • Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin
    • Zhang, P., Talluri, S., Deng, H., Branton, D., and Wagner, G. (1995) Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin. Struct. Fold. Design 15, 1185-1195.
    • (1995) Struct. Fold. Design , vol.15 , pp. 1185-1195
    • Zhang, P.1    Talluri, S.2    Deng, H.3    Branton, D.4    Wagner, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.