Reduction of caveolin-3 expression does not inhibit stretch-induced phosphorylation of ERK2 in skeletal muscle myotubes.

Mechanotransduction is critical to the maintenance and growth of skeletal muscle, but the mechanism by which cellular deformations are converted to biochemical signals remains unclear. Among the earliest and most ubiquitous responses to mechanical stimulation is the phosphorylation and activation of mitogen-activated protein kinases, in particular ERK2. Caveolin-3 (CAV-3) binds ERK2 and its upstream activators in inactive states on the caveolae of resting muscle.