Assembly of the dystrophin-associated protein complex does not require the dystrophin COOH-terminal domain.

摘要: Dystrophin is a multidomain protein that links the actin cytoskeleton to laminin in extracellular matrix through dystrophin associated (DAP) complex. The COOH-terminal domain of binds two components DAP complex, syntrophin and dystrobrevin. To understand role dystrobrevin, we previously generated series transgenic mouse lines expressing dystrophins with deletions throughout domain. Each these mice had normal muscle function displayed localization Since dystrobrevin bind each other as well dystrophin, have now deleted for entire Unexpectedly, this truncated supported assembly These results demonstrate functionally associate complex absence direct link dystrophin. We also observed complexes different strains were not identical. Instead, contained varying ratios isoforms. suggest alternative splicing gene, which naturally generates may regulate isoform composition