Peroxisome proliferator-activated receptor- coactivator-1 (PGC-1) participates in the control of expression of genes involved in adaptive thermogenesis, muscle fiber type differentiation and fuel homeostasis. The objective of the present study was to evaluate the participation of cold-induced PGC-1 expression on the muscle fiber-type specific activity of proteins that belong to the insulin-signaling pathway. Rats were exposed to +4^°C for four days and acutely treated with insulin in the presence, or absence, of an antisense oligonucleotide to PGC-1. Cold exposure promoted a significant increase of PGC-1 and UCP-3 protein expression in type I and type II fibers of the gastrocnemius muscle. In addition, cold exposure led to higher glucose uptake during a hyperinsulinemic clamp, which was accompanied by higher expression and membrane localization of GLUT-4 in both muscle fiber types. Conversely, cold exposure promoted significantly lower insulin-induced tyrosine phosphorylation of the insulin receptor and [Ser⁴⁷³]-phosphorylation of Akt, and an insulin-independent increase of [Thr¹⁷²]-phosphorylation of AMPK. The inhibition of PGC-1 expression in cold-exposed rats, by antisense oligonucleotide treatment, diminished glucose clearance rates during a hyperinsulinemic clamp and reduced the expression and membrane localization of GLUT-4. Furthermore, the reduction of PGC-1 expression resulted in no modification of the insulin-induced tyrosine phosphorylation of the insulin receptor and [Ser⁴⁷³]-phosphorylation of Akt. Finally, reduction of PGC-1 resulted in lower [Thr¹⁷²]-phosphorylation of AMPK. Thus, cold-induced hyperexpression of PGC-1 participates in the control of skeletal muscle glucose uptake through a mechanism that controls GLUT-4 expression and sub-cellular localization, independently of the insulin receptor and Akt activities, but dependent on AMPK.