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Differential distributions of two adducin-like protein isoforms in the Drosophila ovary and early embryo

Published online by Cambridge University Press:  26 September 2008

Michèle Zaccai
Affiliation:
Division of Biology, California Institute of Technology, Pasadena, California, USA.
Howard D. Lipshitz*
Affiliation:
Division of Biology, California Institute of Technology, Pasadena, California, USA.
*
H.D Lipshitz, Program in Developmental Biology, Division of Endocrinology & Department of Geneties, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, Canada M5G 1X8. Telephone: (+1) 416-813-8179. Fax: (+1) 416-813-7956. e-mail: lipshitz@sickkids.on.ca..

Summary

Adducin is a cytoskeletal protein that can function in vitro to bundle F-actin and to control the assembly of the F-actin/spectrin cytoskeletal network. The Drosophila Adducin-like (Add) locus (also referred to as hu-li tai shao (hts)) encodes a family of proteins of which several are homologous to mammalian adducin (Ding et al., Proc. Natl. Acad. Sci. USA90, 2512–16, 1993; Yue & Spradling, Genes Dev.6, 2443–54, 1992). We report the identification of two novel adducin isoforms: a 95 × 103Mr form (ADD-95) and an 87 × 103Mr form (ADD-87). We present a detailed analysis of the distribution patterns of ADD-95 and ADD-87 during oogenesis and embryogenesis. The isoforms are co-expressed in several cell- and tissuetypes; however, only ADD-87 is present in mid- to late-stage oocytes. ADD-87 is present throughout the oocyte cortex at stages 9 and 10 of oogenesis but is detectable only at the anterior pole from stage 11 onward, correlated with localisation of Add-hts mRNA first to the cortex and then to the anterior pole of the oocyte. ADD-87 co-localises with F-actin and spectrin in the cortex of the oocyte through stage 10 of oogenesis, consistent with a possible role in cytoskeletal assembly or function predicted by mammalian studies.

Type
Article
Copyright
Copyright © Cambridge University Press 1996

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References

Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. & Struhl, K. (eds.)(1994). Current Protocols in Molecular Biology, ed. Janssen, K. vol. 2. New York: Wiley Interscience.Google Scholar
Bennett, V., Gardner, K. & Steiner, J.P. (1988). Brain adducin: a protein kinase C substrate that may mediate site-directed assembly at the spectrin-actin junction. J. Biol. Chem. 263, 5860–9.Google Scholar
Byers, T.J., Dubreuil, R., Branton, D., Kiehart, D.P. & Goldstein, L.S.B. (1987). Drosophila spectrin. II. Conserved features of the alpha-subunit are revealed by analysis of cDNA clones and fusion proteins. J. Cell Biol. 105, 2103–10.CrossRefGoogle ScholarPubMed
Campos-Ortega, J.A. & Hartenstein, V. (1985). The Embryonic Development of Drosophila melanogaster. Berlin:Springer-Verlag.CrossRefGoogle Scholar
Ding, D. & Lipshitz, H.D. (1993). Localized RNAs and their functions. BioEssays 15, 651–8.CrossRefGoogle ScholarPubMed
Ding, D., Parkhurst, S.M. & Lipshitz, H.D. (1993). Different genetic requirements for anterior RNA localization revealed by the distribution of Adducin-like transcripts during Drosophila oogenesis. Proc. Natl. Acad. Sci. USA. 90, 2512–16.CrossRefGoogle ScholarPubMed
Dubreuil, R., Byers, T.J., Branton, D., Goldstein, L.S.B. & Kiehart, D.P. (1987). Drosophila Spectrin. I. Characterization of the purified protein. J. Cell Biol. 105, 2095–102.Google Scholar
Gardner, K. & Bennett, V. (1987). Modulation of spectrinactin assembly by erythrocyte adducin. Nature. 328, 359–62.CrossRefGoogle ScholarPubMed
Harlow, E. & Lane, D. (1988). Antibodies: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.Google Scholar
Joshi, R., Gilligan, D.M., Otto, E., McLaughlin, T. & Bennett, V. (1991). Primary structure and domain organization of human alpha and beta adducin. J. Cell Biol. 115, 665–75.CrossRefGoogle ScholarPubMed
Kaiser, H.W., O'Keefe, E. & Bennett, V. (1989). Adducin:Ca++-dependent association with sites of cell-cell contact.J. Cell Biol. 109, 557–69.CrossRefGoogle ScholarPubMed
King, R.C. (1970). Ovarian Development in Drosophila melanogaster. New York: Academic Press.Google Scholar
Lin, H., Yue, L. & Spradling, A.C. (1994). The Drosophila fusome, a germline-specific organelle, contains membrane skeletal proteins and functions in cyst formation. Development. 120, 947–56.Google Scholar
Mishe, S.M., Mooseker, M.S. & Morrow, J.S. (1987). Erythrocyte adducin: a calmodulin-regulated actin-bunding protein that stimulates spectrin–actin binding. J. Cell Biol. 105, 2847–45.Google Scholar
Pinto-Correia, C., Goldstein, E.G., Bennett, V. & Sobel, J.S. (1991). Immunofluorescence localization of an adducinlike protein in the chromosomes of mouse oocytes. Dev. Biol. 146, 301–11.CrossRefGoogle ScholarPubMed
Robinson, D.N., Cant, K. & Cooley, L. (1994). Morphogenesis of Drosophila ovarian ring canals. Development 120, 2015–25.CrossRefGoogle ScholarPubMed
Smith, D.B. & Johnson, K.S. (1988). Single-step purification of polypeptides expressed in Escherichia coli as fusion with glutathione S-transferase. Gene 67, 3140.CrossRefGoogle ScholarPubMed
Whittaker, K.L. & Lipshitz, H.D. (1995). Mechanisms and functions of RNA localization to the anterior pole of the Drosophila oocyte and early embryo. In Localized RNAs, ed. H.D., Lipshitz, 4161. Austin, Texas:R.G. Landes.Google Scholar
Yue, L. (1992). Genetic and molecular characterization of huli tai shas (hts), a gene required for ring canal formation during Drosophila oogenesis. PhD thesis, Johns Hopkins University, Baltimore, Maryland.Google Scholar
Yue, L. & Spradling, A.C. (1992). hu-li tai shao, a gene required for ring canal formation during Drosophila oogenesis, encodes a homolog of adducin. Genes Dev. 6, 2443–54.CrossRefGoogle Scholar