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Na + ,K + ‐ATPase trafficking in skeletal muscle: insulin stimulates translocation of both α 1 ‐ and α 2 ‐subunit isoforms
Author(s) -
Al-Khalili Lubna,
Yu Mei,
Chibalin Alexander V
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00047-4
Subject(s) - skeletal muscle , chromosomal translocation , phosphatidylinositol , wortmannin , g alpha subunit , protein kinase c , protein subunit , protein kinase a , insulin , chemistry , microbiology and biotechnology , biology , medicine , endocrinology , biochemistry , kinase , gene
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 α 2 ‐ but not α 1 ‐subunits was detected. However, using cell surface biotinylation techniques, an insulin‐induced membrane translocation of both α 1 and α 2 ‐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 α 1 ‐ and α 2 ‐subunit translocation to the skeletal muscle plasma membrane via a PI 3‐kinase‐dependent mechanism.