A β-spectrin isoform from Drosophila (β H ) is similar in size to vertebrate dystrophin
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.
Dubreuil, RR; Byers, TJ; Stewart, CT; Kiehart, DP
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