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Regulation of Dishevelled and -catenin in rat skeletal muscle: an alternative exercise-induced GSK-3 signaling pathway

¹The Research Division, Joslin Diabetes Center and Department of Medicine; and ²Division of Endocrinology, Diabetes, and Metabolism, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts

Submitted 27 April 2005 ; accepted in final form 7 February 2006

-catenin is a multifunctional protein involved in cell-cell adhesion and the Wnt signaling pathway. -Catenin is activated upon its dephosphorylation, an event triggered by Dishevelled (Dvl)-mediated phosphorylation and deactivation of glycogen synthase kinase-3 (GSK-3). In skeletal muscle, both insulin and exercise decrease GSK-3 activity, and we tested the hypothesis that these two stimuli regulate -catenin. Immunoblotting demonstrated that Dvl, Axin, GSK-3, and -catenin proteins are expressed in rat red and white gastrocnemius muscles. Treadmill running exercise in vivo significantly decreased -catenin phosphorylation in both muscle types, with complete dephosphorylation being elicited by maximal exercise. -Catenin dephosphorylation was intensity dependent, as dephosphorylation was highly correlated with muscle glycogen depletion during exercise (r² = 0.84, P < 0.001). -Catenin dephosphorylation was accompanied by increases in GSK-3 Ser⁹ phosphorylation and Dvl-GSK-3 association. In contrast to exercise, maximal insulin treatment (1 U/kg body wt) had no effect on skeletal muscle -catenin phosphorylation or Dvl-GSK-3 interaction. In conclusion, exercise in vivo, but not insulin, increases the association between Dvl and GSK-3 in skeletal muscle, an event paralleled by -catenin dephosphorylation.

insulin; Wnt; Akt; protein kinase C; glycogen-synthase kinase-3

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