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A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin.

Publication ,  Journal Article
Dubreuil, RR; Byers, TJ; Stewart, CT; Kiehart, DP
Published in: The Journal of cell biology
November 1990

Spectrins are a major component of the membrane skeleton in many cell types where they are thought to contribute to cell form and membrane organization. Diversity among spectrin isoforms, especially their beta subunits, is associated with diversity in cell shape and membrane architecture. Here we describe a spectrin isoform from Drosophila that consists of a conventional alpha spectrin subunit complexed with a novel high molecular weight beta subunit (430 kD) that we term beta H. The native alpha beta H molecule binds actin filaments with high affinity and has a typical spectrin morphology except that it is longer than most other spectrin isoforms and includes two knoblike structures that are attributed to a unique domain of the beta H subunit. Beta H is encoded by a different gene than the previously described Drosophila beta-spectrin subunit but shows sequence similarity to beta-spectrin as well as vertebrate dystrophin, a component of the membrane skeleton in muscle. By size and sequence similarity, dystrophin is more similar to this newly described beta-spectrin isoform (beta H) than to other members of the spectrin gene family such as alpha-spectrin and alpha-actinin.

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Published In

The Journal of cell biology

DOI

EISSN

1540-8140

ISSN

0021-9525

Publication Date

November 1990

Volume

111

Issue

5 Pt 1

Start / End Page

1849 / 1858

Related Subject Headings

  • Spectrin
  • Sequence Homology, Nucleic Acid
  • Molecular Weight
  • Molecular Sequence Data
  • Dystrophin
  • Drosophila
  • Developmental Biology
  • Cloning, Molecular
  • Cell Membrane
  • Animals
 

Citation

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Dubreuil, R. R., Byers, T. J., Stewart, C. T., & Kiehart, D. P. (1990). A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin. The Journal of Cell Biology, 111(5 Pt 1), 1849–1858. https://doi.org/10.1083/jcb.111.5.1849
Dubreuil, R. R., T. J. Byers, C. T. Stewart, and D. P. Kiehart. “A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin.The Journal of Cell Biology 111, no. 5 Pt 1 (November 1990): 1849–58. https://doi.org/10.1083/jcb.111.5.1849.
Dubreuil RR, Byers TJ, Stewart CT, Kiehart DP. A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin. The Journal of cell biology. 1990 Nov;111(5 Pt 1):1849–58.
Dubreuil, R. R., et al. “A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin.The Journal of Cell Biology, vol. 111, no. 5 Pt 1, Nov. 1990, pp. 1849–58. Epmc, doi:10.1083/jcb.111.5.1849.
Dubreuil RR, Byers TJ, Stewart CT, Kiehart DP. A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin. The Journal of cell biology. 1990 Nov;111(5 Pt 1):1849–1858.

Published In

The Journal of cell biology

DOI

EISSN

1540-8140

ISSN

0021-9525

Publication Date

November 1990

Volume

111

Issue

5 Pt 1

Start / End Page

1849 / 1858

Related Subject Headings

  • Spectrin
  • Sequence Homology, Nucleic Acid
  • Molecular Weight
  • Molecular Sequence Data
  • Dystrophin
  • Drosophila
  • Developmental Biology
  • Cloning, Molecular
  • Cell Membrane
  • Animals