Hostname: page-component-78c5997874-8bhkd Total loading time: 0 Render date: 2024-11-19T09:24:15.687Z Has data issue: false hasContentIssue false

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

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