메뉴 건너뛰기




Volumn 19, Issue 9, 1997, Pages 811-817

Evolution of the spectrin repeat

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0031239149     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190911     Document Type: Review
Times cited : (64)

References (57)
  • 1
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle, R. (1995). The multiplicity of domains in proteins. Annu. Rev. Biochem. 64, 287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.1
  • 3
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies
    • Shotton, D.M., Burke, B.E. and Branton, D. (1979). The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. J. Mol. Biol. 131, 303-29.
    • (1979) J. Mol. Biol. , vol.131 , pp. 303-329
    • Shotton, D.M.1    Burke, B.E.2    Branton, D.3
  • 4
    • 0026671203 scopus 로고
    • Conformation and elasticity of the isolated red blod cell membrane skeleton
    • Svoboda, K., Schmidt, C.F., Branton, D. and Block, S.M. (1992). Conformation and elasticity of the isolated red blod cell membrane skeleton. Biophys. J. 63, 784-793.
    • (1992) Biophys. J. , vol.63 , pp. 784-793
    • Svoboda, K.1    Schmidt, C.F.2    Branton, D.3    Block, S.M.4
  • 5
    • 0025284142 scopus 로고
    • On the structure of erythrocyte spectrin in partially expanded membrane skeletons
    • McGough, A.M. and Josephs, R. (1990). On the structure of erythrocyte spectrin in partially expanded membrane skeletons. Proc. Natl Acad. Sci. USA 87, 5208-12.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5208-5212
    • McGough, A.M.1    Josephs, R.2
  • 6
    • 0024561407 scopus 로고
    • Elasticity of the human red cell membrane skeleton
    • Vertessy, B. and Steck, T. (1989). Elasticity of the human red cell membrane skeleton. Biophys. J. 55, 255-262.
    • (1989) Biophys. J. , vol.55 , pp. 255-262
    • Vertessy, B.1    Steck, T.2
  • 7
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • Hitt, A. and Luna, E. (1994). Membrane interactions with the actin cytoskeleton. Curr. Opin. Cell Biol. 6, 120-130.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 120-130
    • Hitt, A.1    Luna, E.2
  • 8
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett, V. and Gilligan, D.M. (1993). The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9, 27-66.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 9
    • 0026754234 scopus 로고
    • The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments
    • Byers, T.J., Brandin, E., Lue, R.A., Winograd, E. and Branton, D. (1992). The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments. Proc. Natl Acad. Sci. USA 89, 6187-91.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6187-6191
    • Byers, T.J.1    Brandin, E.2    Lue, R.A.3    Winograd, E.4    Branton, D.5
  • 10
    • 0024449311 scopus 로고
    • The complete sequence of Drosophila alpha-spectrin: Conservation of structural domains between alpha-spectrins and alpha-actinin
    • Dubreuil, R.R. et al. (1989). The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin. J. Cell Biol. 109, 2197-205.
    • (1989) J. Cell Biol. , vol.109 , pp. 2197-2205
    • Dubreuil, R.R.1
  • 11
    • 0021705094 scopus 로고
    • Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins
    • Pollard, T. (1984). Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. J. Cell Biol. 99, 1970-1980.
    • (1984) J. Cell Biol. , vol.99 , pp. 1970-1980
    • Pollard, T.1
  • 12
    • 0024242826 scopus 로고
    • Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae
    • Bennett, H. and Condeelis, J. (1988). Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae. Cell. Motil. Cytoskel. 11, 303-17.
    • (1988) Cell. Motil. Cytoskel. , vol.11 , pp. 303-317
    • Bennett, H.1    Condeelis, J.2
  • 13
    • 0027416935 scopus 로고
    • Transient, localized accumulation of alpha-spectrin during sea urchin morphogenesis
    • Wessel, G.M. and Chen, S.W. (1993). Transient, localized accumulation of alpha-spectrin during sea urchin morphogenesis. Dev. Biol. 155, 161-71.
    • (1993) Dev. Biol. , vol.155 , pp. 161-171
    • Wessel, G.M.1    Chen, S.W.2
  • 14
    • 0025933220 scopus 로고
    • Identification of a 220 kDa membrane-associated plant cell protein immunologically related to human β-spectrin
    • Maude, D., Guillett, G., Rogers, P. and Charest, P. (1991). Identification of a 220 kDa membrane-associated plant cell protein immunologically related to human β-spectrin. FEBS Lett. 294, 77-80.
    • (1991) FEBS Lett. , vol.294 , pp. 77-80
    • Maude, D.1    Guillett, G.2    Rogers, P.3    Charest, P.4
  • 15
    • 0025215706 scopus 로고
    • The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin
    • Sahr, K.E. et al. (1990). The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin. J. Biol. Chem. 265, 4434-43.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4434-4443
    • Sahr, K.E.1
  • 16
    • 0025254086 scopus 로고
    • Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin
    • Moon, R.T. and McMahon, A.P. (1990). Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin. J. Biol. Chem. 265, 4427-33.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4427-4433
    • Moon, R.T.1    McMahon, A.P.2
  • 17
    • 0024483987 scopus 로고
    • Primary structure of the brain alpha-spectrin
    • published erratum appears in J. Cell Biol. (1989) Mar; 108(3), following 1175.
    • Wasenius, V.M. et al. (1989). Primary structure of the brain alpha-spectrin [published erratum appears in J. Cell Biol. (1989) Mar; 108(3), following 1175]. J. Cell Biol. 108, 79-93.
    • (1989) J. Cell Biol. , vol.108 , pp. 79-93
    • Wasenius, V.M.1
  • 18
    • 0025332977 scopus 로고
    • Full-length sequence of the cDNA for human erythroid beta-spectrin
    • Winkelmann, J.C. et al. (1990). Full-length sequence of the cDNA for human erythroid beta-spectrin. J. Biol. Chem. 265, 11827-32.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11827-11832
    • Winkelmann, J.C.1
  • 19
    • 0026732691 scopus 로고
    • Characterization of human brain cDNA encoding the general isoform of beta-spectrin
    • Hu, R.J., Watanabe, M. and Bennett, V. (1992). Characterization of human brain cDNA encoding the general isoform of beta-spectrin. J. Biol. Chem. 267, 18715-22.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18715-18722
    • Hu, R.J.1    Watanabe, M.2    Bennett, V.3
  • 20
    • 0027371802 scopus 로고
    • Complete nucleotide sequence of the murine erythroid beta-spectrin cDNA and tissue-specific expression in normal and jaundiced mice
    • Bloom, M.L., Birkenmeier, C.S. and Barker, J.E. (1993) Complete nucleotide sequence of the murine erythroid beta-spectrin cDNA and tissue-specific expression in normal and jaundiced mice. Blood 82, 2906-14.
    • (1993) Blood , vol.82 , pp. 2906-2914
    • Bloom, M.L.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 21
    • 0027471370 scopus 로고
    • The complete amino acid sequence for brain beta spectrin (beta fodrin): Relationship to globin sequences
    • published errata appear in Brain Res. Mol. Brain Res. (1993) Oct; 20(1-2), 179 and (1994) Jan; 21 (1-2), 181.
    • Ma, Y. et al. (1993). The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences [published errata appear in Brain Res. Mol. Brain Res. (1993) Oct; 20(1-2), 179 and (1994) Jan; 21 (1-2), 181]. Brain Res. Mol. Brain Res. 18, 87-99.
    • (1993) Brain Res. Mol. Brain Res. , vol.18 , pp. 87-99
    • Ma, Y.1
  • 22
    • 0028679744 scopus 로고
    • Actin binding proteins 1: Spectrin superfamily
    • Hartwig, J.H. (1994). Actin binding proteins 1: Spectrin superfamily. Protein Profile 1, 711-762.
    • (1994) Protein Profile , vol.1 , pp. 711-762
    • Hartwig, J.H.1
  • 24
    • 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
  • 26
    • 0026749753 scopus 로고
    • SH3-an abundant protein domain in search of a function
    • Musacchio, A., Gibson, T., Lehto, V.-P. and Saraste, M. (1992). SH3-an abundant protein domain in search of a function. FEBS Lett. 307, 55-61.
    • (1992) FEBS Lett. , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.-P.3    Saraste, M.4
  • 27
    • 0028985239 scopus 로고
    • The C-terminal domain of alpha-spectrin is structurally related to calmodulin
    • Trave, G., Pastore, A., Hyvonen, M. and Saraste, M. (1995) The C-terminal domain of alpha-spectrin is structurally related to calmodulin. Eur. J. Biochem. 227, 35-42.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 35-42
    • Trave, G.1    Pastore, A.2    Hyvonen, M.3    Saraste, M.4
  • 29
    • 0028953284 scopus 로고
    • Modulation of erythrocyte membrane mechanical function by b-spectrin phosphorylation and dephosphorylation
    • Manno, S., Takakuwa, Y., Nagao, K. and Mohandas, N. (1995). Modulation of erythrocyte membrane mechanical function by b-spectrin phosphorylation and dephosphorylation. J. Biol. Chem. 270, 5659-5665.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5659-5665
    • Manno, S.1    Takakuwa, Y.2    Nagao, K.3    Mohandas, N.4
  • 30
    • 0029096888 scopus 로고
    • Structure of the binding site for inositol phosphates in a PH domain
    • Hyvonen, M. et al. (1995). Structure of the binding site for inositol phosphates in a PH domain. EMBO J. 14, 4676-4685.
    • (1995) EMBO J. , vol.14 , pp. 4676-4685
    • Hyvonen, M.1
  • 31
    • 0024573939 scopus 로고
    • Characterization of the calmodulin-binding site of nonerythroid alpha-spectrin. Recombinant protein and model peptide studies
    • Leto, T.L., Pleasic, S., Forget, B.G., Benz, E.J. and Marchesi, V.T. (1989). Characterization of the calmodulin-binding site of nonerythroid alpha-spectrin. Recombinant protein and model peptide studies. J. Biol. Chem. 264, 5826-30.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5826-5830
    • Leto, T.L.1    Pleasic, S.2    Forget, B.G.3    Benz, E.J.4    Marchesi, V.T.5
  • 32
    • 0025886649 scopus 로고
    • Structure, calmodulin-binding, and calcium-binding properties of recombinant alpha spectrin polypeptides
    • Dubreuil, R.R., Brandin, E., Reisberg, J.H., Goldstein, L.S. and Branton, D. (1991). Structure, calmodulin-binding, and calcium-binding properties of recombinant alpha spectrin polypeptides. J. Biol. Chem. 266, 7189-93.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7189-7193
    • Dubreuil, R.R.1    Brandin, E.2    Reisberg, J.H.3    Goldstein, L.S.4    Branton, D.5
  • 33
    • 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, 177-80.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 34
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. and Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 35
    • 0027749280 scopus 로고
    • Crystal structure of the repetitive segments of spectrin
    • Yan, Y. et al. (1993). Crystal structure of the repetitive segments of spectrin. Science 262, 2027-30.
    • (1993) Science , vol.262 , pp. 2027-2030
    • Yan, Y.1
  • 36
    • 0026510756 scopus 로고
    • Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins
    • Parry, D.A., Dixon, T.W. and Cohen, C. (1992). Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins. Biophys. J. 61, 858-67.
    • (1992) Biophys. J. , vol.61 , pp. 858-867
    • Parry, D.A.1    Dixon, T.W.2    Cohen, C.3
  • 37
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., van Dyke, M. and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 39
    • 0028011014 scopus 로고
    • Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin
    • MacDonald, R.I., Musacchio, A., Holmgren, R.A. and Saraste, M. (1994). Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin. Proc. Natl Acad. Sci. USA 91, 1299-303.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1299-1303
    • MacDonald, R.I.1    Musacchio, A.2    Holmgren, R.A.3    Saraste, M.4
  • 40
    • 0028172933 scopus 로고
    • The first human alpha-spectrin structural domain begins with serine
    • Lusitani, D.M. et al. (1994). The first human alpha-spectrin structural domain begins with serine. J. Biol. Chem. 269, 25955-8.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25955-25958
    • Lusitani, D.M.1
  • 41
    • 0024993498 scopus 로고
    • Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association
    • Tse, W.T. et al. (1990). Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association. J. Clin. Invest. 86, 909-16.
    • (1990) J. Clin. Invest. , vol.86 , pp. 909-916
    • Tse, W.T.1
  • 42
    • 0027419729 scopus 로고
    • Location of the human red cell spectrin tetramer binding site and detection of a related 'closed' hairpin loop dimer using proteolytic footprinting
    • Speicher, D.W. et al. (1993). Location of the human red cell spectrin tetramer binding site and detection of a related 'closed' hairpin loop dimer using proteolytic footprinting. J. Biol. Chem. 268, 4227-35.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4227-4235
    • Speicher, D.W.1
  • 43
    • 0028245275 scopus 로고
    • A partial structural repeat forms the heterodimer self-association site of all b-spectrins
    • Kennedy, S., Weed, S., Forget, B. and Morrow, J. (1994). A partial structural repeat forms the heterodimer self-association site of all b-spectrins. J. Biol. Chem. 269, 11400-11408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11400-11408
    • Kennedy, S.1    Weed, S.2    Forget, B.3    Morrow, J.4
  • 44
    • 0027438310 scopus 로고
    • Spectrin cagliari. an Ala→Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer
    • Sahr, K.E. et al. (1993). Spectrin cagliari. an Ala→Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. J. Biol. Chem. 268, 22656-62.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22656-22662
    • Sahr, K.E.1
  • 45
    • 0028240888 scopus 로고
    • Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: Further support for a triple-stranded folding unit model of the spectrin heterodimer contact site
    • Parquet, N. et al. (1994). Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: further support for a triple-stranded folding unit model of the spectrin heterodimer contact site. Blood 84, 303-8.
    • (1994) Blood , vol.84 , pp. 303-308
    • Parquet, N.1
  • 46
    • 0026073190 scopus 로고
    • The exon-intron organization of the human erythrocyte a-spectrin gene
    • Kotula, L. et al. (1991). The exon-intron organization of the human erythrocyte a-spectrin gene. Genomics 9, 131-40.
    • (1991) Genomics , vol.9 , pp. 131-140
    • Kotula, L.1
  • 47
    • 0027366505 scopus 로고
    • The exon-intron organization of the human erythroid b-spectrin gene
    • Amin, K., Scarpa, A., Winkelmann, J., Curtis, P. and Forget, B. (1993). The exon-intron organization of the human erythroid b-spectrin gene. Genomics 18, 118-125.
    • (1993) Genomics , vol.18 , pp. 118-125
    • Amin, K.1    Scarpa, A.2    Winkelmann, J.3    Curtis, P.4    Forget, B.5
  • 49
    • 0028086431 scopus 로고
    • Analysis of the phasing of four spectrin-like repeats in alpha-actinin
    • Gilmore, A.P., Parr, T., Patel, B., Gratzer, W.B. and Critchley, D.R. (1994). Analysis of the phasing of four spectrin-like repeats in alpha-actinin. Eur J. Biochem. 225, 235-42.
    • (1994) Eur J. Biochem. , vol.225 , pp. 235-242
    • Gilmore, A.P.1    Parr, T.2    Patel, B.3    Gratzer, W.B.4    Critchley, D.R.5
  • 50
    • 0029117231 scopus 로고
    • Dystrophin and utrophin: The missing links!
    • Winder, S., Gibson, T. and Kendrick-Jones, J. (1995) Dystrophin and utrophin: the missing links! FEHS Lett. 369, 27-33.
    • (1995) FEHS Lett. , vol.369 , pp. 27-33
    • Winder, S.1    Gibson, T.2    Kendrick-Jones, J.3
  • 51
    • 0030001020 scopus 로고    scopus 로고
    • Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes
    • Li, X. and Bennett, V. (1996). Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. J. Biol. Chem. 271, 15695-15702.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15695-15702
    • Li, X.1    Bennett, V.2
  • 52
    • 0029804981 scopus 로고    scopus 로고
    • A new model for the interaction of dystrophin with F-actin
    • Rybakova, I., Amann, K. and Ervasti, J. (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.1    Amann, K.2    Ervasti, J.3
  • 53
    • 0028928013 scopus 로고
    • Alternate binding of actin and calmodulin to multiple sites on dystrophin
    • Jarrett, H. and Foster, J. (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.1    Foster, J.2
  • 54
    • 0028306603 scopus 로고
    • Deletion analysis of the dystrophin-actin binding domain
    • Corrado, K., Mills, P.L. and Chamberlain, J.S. (1994). Deletion analysis of the dystrophin-actin binding domain. FEBS Lett. 344, 255-260.
    • (1994) FEBS Lett. , vol.344 , pp. 255-260
    • Corrado, K.1    Mills, P.L.2    Chamberlain, J.S.3
  • 55
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • Kennedy, S.P., Warren, S.L., Forget, B.C. and Morrow, J.S. (1991). Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. J. Cell Biol. 115, 267-77.
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.C.3    Morrow, J.S.4
  • 56
    • 0026165749 scopus 로고
    • Structure and evolution of the actin crosslinking proteins
    • Dubreuil, R. (1991). Structure and evolution of the actin crosslinking proteins. BioEssays 13, 219-226.
    • (1991) BioEssays , vol.13 , pp. 219-226
    • Dubreuil, R.1
  • 57
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.