In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin.

Dystrophin, the product of the gene mutated in Duchenne muscular dystrophy (DMD) is bound by its C-terminus to a protein complex including the related protein dystrobrevin. Both proteins contain a putative coiled-coil domain consisting of two alpha-helices. It has been reported that the two proteins bind to each other by the first one of the two alpha-helices. We have revisited this question using the Caenorhabditis elegans homologs of dystrophin and dystrobrevin. In vitro interaction occurs through the more conserved second helix. We propose a new model of dystrophin interactions with associated proteins.