Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 456, Issue 1, Pages 41-46Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2014.11.031
Keywords
SKIP; Pak1; Insulin signaling; Skeletal muscle
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Funding
- Japan Society for the Promotion of Science (JSPS) KAKENHI Grant [25460365]
- Novo Nordisk Pharma Research Foundation
- Japan Diabetes Foundation
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT) KAKENHI Grant, Japan [23227005]
- Grants-in-Aid for Scientific Research [25460365, 23227005] Funding Source: KAKEN
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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. (C) 2014 Elsevier Inc. All rights reserved.
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