Dystrophin and functionally related proteins in the nematode Caenorhabditis elegans.
We investigated the function of dystrophin in the nematode Caenorhabditis elegans. Although nematodes and mammals diverged early in evolution, their muscles share many structural and molecular features, thus rendering C. elegans relevant as a model to study muscle function. Dystrophin, dystrobrevin, dystroglycans and several sarcoglycans have conserved homologues in the genome of C. elegans. The major strength of the model comes from its genetic tractability, which allows the quick and easy manipulation of gene expression, either to inactivate genes, or to create transgenic animals. Over the last 2 years, work on C. elegans dystrophin has led to the identification of a putative new member of the dystrophin-glycoprotein complex, and has brought additional data suggesting that dystrophin mutations affect ion channel function.
Ségalat
Laurent
L
CGMC, CNRS-UMR 5534, Université Lyon 1, 43 bld du 11 Novembre, 69622 Villeurbanne cedex, France. segalat@maccgmc.univ.-lyonl.fr
D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism*; D015220:Calcium Channels / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism; D049030:Dystroglycans; D016189:Dystrophin / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D016678:Genome; D008562:Membrane Glycoproteins / Q000378:metabolism; D009154:Mutation
D015220:Calcium Channels; D003598:Cytoskeletal Proteins; D016189:Dystrophin; D008562:Membrane Glycoproteins; D049030:Dystroglycans