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

Published

Journal Article

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 β subunits, is associated with diversity in cell shape and membrane architecture. Here we describe a spectrin isoform from Drosophila that consists of a conventional α spectrin subunit complexed with a novel high molecular weight β subunit (430 kD) that we term β H . The native αβ 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 β H subunit, β H is encoded by a different gene than the previously described Drosophila β-spectrin subunit but shows sequence similarity to β-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 β-spectrin isoform (β H ) than to other members of the spectrin gene family such as α-spectrin and α-actinin.

Full Text

Duke Authors

Cited Authors

  • Dubreuil, RR; Byers, TJ; Stewart, CT; Kiehart, DP

Published Date

  • January 1, 1990

Published In

Volume / Issue

  • 111 / 5

Start / End Page

  • 1849 - 1858

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.111.5.1849

Citation Source

  • Scopus