Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Oct 1;90(19):9115–9119. doi: 10.1073/pnas.90.19.9115

Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.

J Bryan 1, R Edwards 1, P Matsudaira 1, J Otto 1, J Wulfkuhle 1
PMCID: PMC47512  PMID: 8415664

Abstract

A cDNA for fascin, an actin-bundling protein in echinoderms, has been cloned, sequenced, and expressed. The predicted mass of the protein is approximately 55 kDa, similar to that observed for fascin purified from sea urchin eggs. Bacterially expressed fascin reacts with antibodies prepared against sea urchin egg fascin. Fascin has a strong sequence similarity to the singed gene (sn) product in Drosophila and has similarities with a 55-kDa human actin-bundling protein. No extensive similarities were found with other known actin-binding/bundling proteins, indicating that this is a separate gene family.

Full text

PDF
9115

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arpin M., Pringault E., Finidori J., Garcia A., Jeltsch J. M., Vandekerckhove J., Louvard D. Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity. J Cell Biol. 1988 Nov;107(5):1759–1766. doi: 10.1083/jcb.107.5.1759. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bazari W. L., Matsudaira P., Wallek M., Smeal T., Jakes R., Ahmed Y. Villin sequence and peptide map identify six homologous domains. Proc Natl Acad Sci U S A. 1988 Jul;85(14):4986–4990. doi: 10.1073/pnas.85.14.4986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bryan J., Kane R. E. Separation and interaction of the major components of sea urchin actin gel. J Mol Biol. 1978 Oct 25;125(2):207–224. doi: 10.1016/0022-2836(78)90345-5. [DOI] [PubMed] [Google Scholar]
  4. Burgess D. R., Schroeder T. E. Polarized bundles of actin filaments within microvilli of fertilized sea urchin eggs. J Cell Biol. 1977 Sep;74(3):1032–1037. doi: 10.1083/jcb.74.3.1032. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cooley L., Verheyen E., Ayers K. chickadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis. Cell. 1992 Apr 3;69(1):173–184. doi: 10.1016/0092-8674(92)90128-y. [DOI] [PubMed] [Google Scholar]
  6. DeRosier D. J., Censullo R. Structure of F-actin needles from extracts of sea urchin oocytes. J Mol Biol. 1981 Feb 15;146(1):77–99. doi: 10.1016/0022-2836(81)90367-3. [DOI] [PubMed] [Google Scholar]
  7. DeRosier D., Mandelkow E., Silliman A. Structure of actin-containing filaments from two types of non-muscle cells. J Mol Biol. 1977 Jul 15;113(4):679–695. doi: 10.1016/0022-2836(77)90230-3. [DOI] [PubMed] [Google Scholar]
  8. Fechheimer M., Murdock D., Carney M., Glover C. V. Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000-dalton actin-bundling protein. J Biol Chem. 1991 Feb 15;266(5):2883–2889. [PubMed] [Google Scholar]
  9. Gorlin J. B., Yamin R., Egan S., Stewart M., Stossel T. P., Kwiatkowski D. J., Hartwig J. H. Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J Cell Biol. 1990 Sep;111(3):1089–1105. doi: 10.1083/jcb.111.3.1089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gutzeit H. O. The role of microfilaments in cytoplasmic streaming in Drosophila follicles. J Cell Sci. 1986 Feb;80:159–169. doi: 10.1242/jcs.80.1.159. [DOI] [PubMed] [Google Scholar]
  11. Kane R. E. Preparation and purification of polymerized actin from sea urchin egg extracts. J Cell Biol. 1975 Aug;66(2):305–315. doi: 10.1083/jcb.66.2.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Maekawa S., Endo S., Sakai H. A protein in starfish sperm head which bundles actin filaments in vitro: purification and characterization. J Biochem. 1982 Dec;92(6):1959–1972. doi: 10.1093/oxfordjournals.jbchem.a134127. [DOI] [PubMed] [Google Scholar]
  14. Matsudaira P. Modular organization of actin crosslinking proteins. Trends Biochem Sci. 1991 Mar;16(3):87–92. doi: 10.1016/0968-0004(91)90039-x. [DOI] [PubMed] [Google Scholar]
  15. Otto J. J., Kane R. E., Bryan J. Formation of filopodia in coelomocytes: localization of fascin, a 58,000 dalton actin cross-linking protein. Cell. 1979 Jun;17(2):285–293. doi: 10.1016/0092-8674(79)90154-5. [DOI] [PubMed] [Google Scholar]
  16. Otto J. J., Kane R. E., Bryan J. Redistribution of actin and fascin in sea urchin eggs after fertilization. Cell Motil. 1980;1(1):31–40. doi: 10.1002/cm.970010104. [DOI] [PubMed] [Google Scholar]
  17. Otto J. J., Schroeder T. E. Assembly-disassembly of actin bundles in starfish oocytes: an analysis of actin-associated proteins in the isolated cortex. Dev Biol. 1984 Feb;101(2):263–273. doi: 10.1016/0012-1606(84)90140-4. [DOI] [PubMed] [Google Scholar]
  18. Overton J. The fine structure of developing bristles in wild type and mutant Drosophila melanogaster. J Morphol. 1967 Aug;122(4):367–379. doi: 10.1002/jmor.1051220406. [DOI] [PubMed] [Google Scholar]
  19. Paterson J., O'Hare K. Structure and transcription of the singed locus of Drosophila melanogaster. Genetics. 1991 Dec;129(4):1073–1084. doi: 10.1093/genetics/129.4.1073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Roiha H., Rubin G. M., O'Hare K. P element insertions and rearrangements at the singed locus of Drosophila melanogaster. Genetics. 1988 May;119(1):75–83. doi: 10.1093/genetics/119.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Scheel J., Ziegelbauer K., Kupke T., Humbel B. M., Noegel A. A., Gerisch G., Schleicher M. Hisactophilin, a histidine-rich actin-binding protein from Dictyostelium discoideum. J Biol Chem. 1989 Feb 15;264(5):2832–2839. [PubMed] [Google Scholar]
  22. Smith R. F., Smith T. F. Automatic generation of primary sequence patterns from sets of related protein sequences. Proc Natl Acad Sci U S A. 1990 Jan;87(1):118–122. doi: 10.1073/pnas.87.1.118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Spudich J. A., Amos L. A. Structure of actin filament bundles from microvilli of sea urchin eggs. J Mol Biol. 1979 Apr 5;129(2):319–331. doi: 10.1016/0022-2836(79)90285-7. [DOI] [PubMed] [Google Scholar]
  24. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986 May 5;189(1):113–130. doi: 10.1016/0022-2836(86)90385-2. [DOI] [PubMed] [Google Scholar]
  25. Xue F., Cooley L. kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell. 1993 Mar 12;72(5):681–693. doi: 10.1016/0092-8674(93)90397-9. [DOI] [PubMed] [Google Scholar]
  26. Yamashiro-Matsumura S., Matsumura F. Intracellular localization of the 55-kD actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin. J Cell Biol. 1986 Aug;103(2):631–640. doi: 10.1083/jcb.103.2.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Yamashiro-Matsumura S., Matsumura F. Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. J Biol Chem. 1985 Apr 25;260(8):5087–5097. [PubMed] [Google Scholar]
  28. 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. 1990 Sep;111(3):1069–1079. doi: 10.1083/jcb.111.3.1069. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES