Na+,K+‐ATPase trafficking in skeletal muscle: insulin stimulates translocation of both α1‐ and α2‐subunit isoforms
Open Access
- 22 January 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 536 (1-3), 198-202
- https://doi.org/10.1016/s0014-5793(03)00047-4
Abstract
We determined insulin-stimulated Na+,K+-ATPase isoform-specific translocation to the skeletal muscle plasma membrane. When rat muscle plasma membrane fractions were isolated by discontinuous sucrose gradients, insulin-stimulated translocation of α2- but not α1-subunits was detected. However, using cell surface biotinylation techniques, an insulin-induced membrane translocation of both α1 and α2-subunits in rat epitrochlearis muscle and cultured human skeletal muscle cells was noted. Na+,K+-ATPase α-subunit translocation was abolished by the phosphatidylinositol (PI) 3-kinase inhibitor wortmannin, as well as by the protein kinase C inhibitor GF109203X. Thus, insulin mediates Na+,K+-ATPase α1- and α2-subunit translocation to the skeletal muscle plasma membrane via a PI 3-kinase-dependent mechanism.Keywords
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