Dystrophin as a focal adhesion protein. Collocalization with talin and the Mr 48,000 sarcolemmal protein in cultured Xenopus muscle.
Monoclonal antibodies against dystrophin and the postsynaptic 58 kDa protein from Torpedo electric organ were used to localize homologs of these proteins in cultured skeletal muscle (Xenopus laevis). The Xenopus homolog is an Mr 48,000 protein and, like dystrophin, is a sarcolemmal protein. Both proteins localized precisely to talin-positive sites, hence with each other, on the substrate-apposed sarcolemma. Therefore, the first sites of appearance of dystrophin on cultured muscle cells are focal adhesions, i.e. specific sites of cytoskeleton/extracellular matrix interaction. These data also add to evidence that dystrophin and the 58 kDa act together.
Kramarcy
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NR
Department of Physiology, University of North Carolina, Chapel Hill 27599.
Sealock
R
R
D000818:Animals; D000906:Antibodies; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000032:analysis*; D016189:Dystrophin / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D008565:Membrane Proteins / Q000032:analysis; D008970:Molecular Weight; D009132:Muscles / Q000166:cytology / Q000648:ultrastructure*; D012508:Sarcolemma / Q000648:ultrastructure*; D016608:Talin; D014982:Xenopus laevis
D000906:Antibodies; D003598:Cytoskeletal Proteins; D016189:Dystrophin; D008565:Membrane Proteins; D016608:Talin