Intragenic duplication and divergence in the spectrin superfamily of proteins

Molecular Biology and Evolution

Volumn 14, Issue 12, 1997, Pages 1285-1295

  Thomas, Graham H ^a   Newbern, E Claire ^a   Korte, Carol C ^a   Bales, Mark A ^a,c   Muse, Spencer V ^a,d   Clark, Andrew G ^a   Kiehart, Daniel P ^b  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b DUKE UNIVERSITY   (United States)

^c UNIVERSITY OF ARIZONA   (United States)

^d UNIVERSITY OF MISSOURI   (United States)

Author keywords

Concerted evolution; Dystrophin; Membrane skeleton; Repetitive DNA; Spectrin; Actinin

Indexed keywords

SPECTRIN;

ARTICLE; GENE DUPLICATION; GENETIC MODEL; MOLECULAR EVOLUTION; PROTEIN FAMILY; TANDEM REPEAT;

ARTHROPODA; VERTEBRATA;

EID: 0030827612     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.molbev.a025738     Document Type: Article

References (53)

1. BARON, M. D., M. D. DAVISON, P. A. JONES, and D. R. CRITCHLEY. 1991. The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin. J. Biol. Chem. 262:17623-17629.
2. BENNETT, V. 1992. Ankyrins: adapters between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem. 267:8703-8706.
3. BENNETT, V., and D. M. GILLIGAN. 1993. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9:27-66.
4. BIES, R. D., S. F. PHELPS, M. D. CORTEZ, R. ROBERTS, C. T. CASKEY, and J. S. CHAMBERLAIN. 1992. Human and murine dystrophin mRNA transcripts are differentially expressed during skeletal muscle, heart, and brain development. Nucleic Acids Res. 20:1725-1731.
5. BLOOM, M. L., C. S. BIRKENMEIER, and J. E. BARKER. 1993. Complete nucleotide sequence of the murine erythroid β-spectrin cDNA and tissue-specific expression in normal and jaundiced mice. Blood 82:2906-2914.
6. BRISTOW, J., M. K. TEE, S. E. GITELMAN, S. H. MELLON, and W. L. MILLER. 1993. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping p450c21B. J. Cell Biol. 122:265-278.
7. BROWN, N. H., and F. C. KAFATOS. 1988. Functional cDNA libraries from Drosophila embryos. J. Mol. Biol. 203:425-437.
8. BYERS, T. J., E. BRANDIN, R. A. LUE, E. WINOGRAD, and D. BRANTON. 1992. The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments. Proc. Natl. Acad. Sci. USA 89:6187-6191.
9. DE ARRUDA, M. V., S. WATSON, C. S. LIN, J. LEAVITT, and P. MATSUDAIRA. 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.
10. DRUBIN, D. G., and W. J. NELSON. 1996. Origins of cell polarity. Cell 84:335-344.
11. DUBREUIL, R. R. 1991. Structure and evolution of the actin crosslinking proteins. Bioessays 13:219-226.
12. DUBREUIL, R. R., T. J. BYERS, A. L. SILLMAN, D. BAR-ZVI, L. S. B. GOLDSTEIN, and D. BRANTON. 1989. The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin. J. Cell Biol. 109:2197-2205.
13. H) is similar in size to vertebrate dystrophin. J. Cell Biol. 111:1849-1858.
14. FROHMAN, M. A. 1990. RACE: rapid amplification of cDNA ends. Pp. 28-38 in M. A. INNIS, D. H. GELFAND, J. J. SNINSKY and T. J. WHITE, eds. PCR Protocols. Academic Press, San Diego.
15. FYRBERG, E., K. MELISSA, E. BALL, C. FYRBERG, and M. C. REEDY, 1990. Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions. J. Cell Biol. 110:1999-2011.
16. GORLIN, J. B., R. YAMIN, S. EGAN, M. STEWART, T. P. STOSSEL, D. J. KWIATKOWSKI, and J. H. HARTWIG. 1990. Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J. Cell Biol. 111:1089-1105.
17. HARTWIG, J. H., and D. J. KWIATKOWSKI. 1991. Actin-binding proteins. Curr. Opin. Cell Biol. 3:87-97.
18. HU, R.-J., W. MASAYO, and V. BENNETT. 1992. Characterization of human brain cDNA encoding the general isoform of β-spectrin. J. Biol. Chem. 267:18715-18722.
19. KENNEDY, S., S. WARREN, B. FORGET, and J. MORROW. 1991. Ankyrin binds to the 15th repetitive unit of erythroid and non-erythroid beta-spectrin. J. Cell Biol. 115:267-277.
20. KOENIG, M., A. P. MONACO, and L. M. KUNKEL. 1988. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53:219-228.
21. KUMAR, S., K. TAMWA, and M. NEI. 1993. Molecular evolutionary genetic analysis. Version 1.02. Institute of Molecular Evolutionary Genetics, Pennsylvania State University, University Park.
22. LEE, J. K., E. BRANDIN, D. BRANTON, and L. S. B. GOLDSTEIN. 1997. α-Spectrin is required for ovarian follicle monolayer integrity in Drosophila melanogaster. Development 124:353-362.
23. LEMAIRE, C., R. HEILIG, and J. L. MANDEL. 1988. Nucleotide sequence of chicken dystrophin cDNA. Nucleic Acids Res. 16:11815.
24. LUNA, E. J., and A. L. HITT. 1992. Cytoskeleton-plasma membrane interactions. Science 258:955-964.
25. MA, Y., W. E. ZIMMER, B. M. RIEDERER, and S. R. GOODMAN. 1993. The complete amino acid sequence for brain β spectrin (β fodrin): relationship to globin sequences. Mol. Brain Res. 18:87-99.
26. MOON, R. T., and A. P. MCMAHON. 1990. Generation of diversity in nonerythroid spectrins. J. Biol. Chem. 256:4427- 4433.
27. MUSACCHIO, A., T. GIBSON, P. RICE, J. THOMPSON, and M. SARASTE. 1993. The PH domain: a common piece in the structural patchwork of signaling proteins. Trends Biochem. SCi. 18:343-348.
28. MUSACCHIO, A., M. WILMANNS, and M. SARASTE. 1994. Structure and function of the SH3 domain. Prog. Biophys. Mol. Biol. 61:283-297.
29. MUSE, S. V., A. G. CLARK, and G. H. THOMAS. 1997. Comparisons of the nucleotide substitution process among repetitive segments of the α- and β-spectrin genes. J. Mol. Evol. 44:492-500.
30. NOEGEL, A., W. WITKE, and M. SCHLEICHER. 1987. Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions. FEBS Lett. 221:391-396.
31. NOEGEL, A. A., S. RAPP, F. LOTTSPEICH, M. SCHLEICHER, and M. STEWART. 1989. The Dictyostelium gelation factor shares a putative actin-binding site with α-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-β conformation. J. Cell Biol. 109:607-618.
32. PEIFER, M., and E. WEISCHAUS. 1990. The segment polarity gene armadillo encodes a functionally modular protein that is the Drosophila homolog of human plakoglobin. Cell 63:1167-1178.
33. PRASSLER, J., S. STOCKER, G. MARRIOTT, M. HEIDECKER, J. KELLERMAN, and G. GERISCH. 1997. Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes. Mol. Biol. Cell 8:83-95.
34. RIGGLEMAN, B., E. WIESCHAUS, and P. SCHEDL. 1989. Molecular analysis of the armadillo locus: uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene. Genes Dev. 3:96-113.
35. RYBAKOVA, I. N., K. J. AMANN, and J. M. ERVASTI. 1996. A new model for the interaction of dystrophin with F-actin. J. Cell Biol. 135:661-672.
36. SABER, M. A., H. ABDEL-HEMID, M. ROMEIH, H. AHMED, and R. HARISON. 1996. GenBank Accession L33405, Release 98.0.
37. SAHR, K. E., P. LAURILA, L. KOTULA et al. (12 co-authors). 1990. The complete cDNA and polypeptide sequences of human erythroid α-spectrin. J. Biol. Chem. 265:4434-4443.
38. SPEICHER, D. W., T. M. DESILVA, K. D. SPEICHER, J. A. URSITTI, P. HEMBACH, and L. WEGLARZ. 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. 268:4227-4235.
39. SPEICHER, D. W., and V. T. MARCHESI. 1984. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311:177-180.
40. TEPASS, U., C. THERES, and E. KNUST. 1990. crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia. Cell 61:787-799.
41. Heavy-spectrin has a restricted tissue and sub cellular distribution during Drosophila embryogenesis. Development 120:2039-2050.
42. TSE, W. T., M.-C. LECOMTE, F. F. COSTA, M. GARBARZ, C. FEO, P. BOIVIN, D. DHERMY, and B. G. FORGET. 1990. Point mutation in the β-spectrin gene associated with αI/74 hereditary elliptocytosis. J. Clin. Invest. 86:909-916.
43. VEIL, A., and D. BRANTON. 1994. Interchain binding at the tail end of the Drosophila spectrin molecule. Proc. Natl. Acad. Sci. USA 91:10839-10843.
44. _. 1996. Spectrin: on the path from structure to function. Curr. Opin. Cell Biol. 8:49-55.
45. WASENIUS, V.-M., M. SARASTE, P. SALVEN, M. ERÄMAA, L. HOLM, and V.-P. LEHTO. 1989. Primary structure of the brain α-spectrin. J. Cell Biol. 108:79-93.
46. WHARTON, K. A., K. M. JOHANSEN, T. XU, and S. ARTAVANIS-TSAKONAS. 1995. Nucleotide sequence from the neurogenic locus Notch implies a gene product that shares homology with proteins containing EGF-like repeats. Cell 43:567-581.
47. WHARTON, K. A., B. YEDVOBNICK, V. G. FINNERTY, and S. ARTAVANIS-TSAKONAS. 1985. opa: a novel family of transcribed repeats shared by the Notch locus and other developmentally regulated loci in D. melanogaster. Cell 40:55-62.
48. WINKELMAN, J. C., J.-G. CHANG, W. T. TSE, V. T. MARCHESI, and B. G. FORGET. 1990a. Full-length sequence of the cDNA for human erythroid β-spectrin. J. Biol. Chem. 265:11827-11838.
49. WINKELMAN, J. C., F. F. COSTA, B. L. LINZIE, and B. G. FORGET. 1990b. β Spectrin in human skeletal muscle. J. Biol. Chem. 265:20449-20454.
50. WINKELMAN, J. C., and B. G. FORGET. 1993. Erythroid and nonerythroid spectrins. Blood 81:3173-3185.
51. YAN, Y., E. WINOGRAD, A. VEIL, T. CRONIN, S. C. HARRISON, and D. BRANTON. 1993. Crystal structure of the repetitive segments of spectrin. Science 262:2027-2030.
52. YOUSSOUFIAN, H., M. MCAFEE, and D. J. KWIATKOWSKI. 1990. Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene. Am. J. Hum. Genet. 47:62-71.
53. ZIMMER, E. A., S. L. MARTIN, S. M. BEVERLEY, Y. W. KAN, and A. C. WILSON. 1980. Rapid duplication and loss of genes coding for the α-chains of hemoglobin. Proc. Natl. Acad. Sci. USA 77:2158-2162.