| First Author | Ijuin T | Year | 2015 |
| Journal | Biochem Biophys Res Commun | Volume | 456 |
| Issue | 1 | Pages | 41-6 |
| PubMed ID | 25446075 | Mgi Jnum | J:220289 |
| Mgi Id | MGI:5634073 | Doi | 10.1016/j.bbrc.2014.11.031 |
| Citation | Ijuin T, et al. (2015) Improvement of insulin signaling in myoblast cells by an addition of SKIP-binding peptide within Pak1 kinase domain. Biochem Biophys Res Commun 456(1):41-6 |
| abstractText | Abnormalities in insulin-induced glucose incorporation in skeletal muscle were observed in Type 2 diabetes. Our previous studies revealed that the binding between skeletal muscle and kidney-enriched inositol polyphosphate phosphatase (SKIP) and p21-activated protein kinase (Pak1) at the plasma membrane is induced insulin-dependently and that this binding mediated a rapid and efficient termination of insulin signaling and a subsequent glucose uptake into skeletal muscle cells. Here, we identified 11-amino-acids peptide within kinase domain of Pak1, necessary and sufficient for SKIP binding. Expression of this region in C2C12 cells resulted in an increase in insulin signaling. Supplementation of a synthetic peptide of this sequence increased insulin signaling and insulin-induced glucose uptake into skeletal muscle cell lines. These findings suggest the physiological role of Pak1-SKIP binding in the regulation of insulin signaling in skeletal muscle. |
