Disease relevance of dyb-1

• 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 [1].

High impact information on dyb-1

• These findings suggest that: (1) dystrobrevin and dystrophin are functionally related and (2) their disruption impairs cholinergic signalling [2].
• Dystrobrevin- and dystrophin-like mutants display similar phenotypes in the nematode Caenorhabditis elegans [2].

Biological context of dyb-1

• Mutations of dyb-1 and dys-1 lead to similar phenotypes, comprising hyperactivity and a tendency to hypercontract, which suggest that these proteins may participate in a common function [3].
• Dystrophin, dystrobrevin, dystroglycans and several sarcoglycans have conserved homologues in the genome of C. elegans [4].

Physical interactions of dyb-1

• These results are consistent with a model according to which dystrobrevin must bind to dystrophin to be able to function properly [5].

Analytical, diagnostic and therapeutic context of dyb-1

• The deletions affecting the second helix of the Dyb-1 coiled-coil domain abolished the binding of dystrobrevin to dystrophin both in vitro and in the two-hybrid assay [5].

References