Protein arginine methylation regulates insulin signaling in L6 skeletal muscle cells

摘要: Protein N-arginine methyltransferase (PRMT)1 catalyzes arginine methylation in a variety of substrates, although the potential role PRMT1 insulin action has not been defined. We therefore investigated effect PRMT1-mediated on signaling and glucose uptake skeletal L6 myotubes. Exposure myotubes to rapidly induced translocation increased its catalytic activity membrane fraction. Several proteins fraction were arginine-methylated after treatment, which inhibited by pretreatment with an inhibitor methyltransferase, 5'-deoxy-5'-(methylthio)adenosine (MTA), or small interfering RNA against (PRMT1-siRNA). Inhibition MTA PRMT1-siRNA diminished later phase insulin-stimulated tyrosine phosphorylation receptor (IR) beta IRS-1, association IRS-1 p85alpha subunit PI3-K, uptake. Our results suggest that serves as positive modulator IR/IRS-1/PI3-K pathway subsequent muscle cells.