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Regulation of Insulin Sensitivity by Skeletal Muscle Specific Modulation Of p21‐Activated Kinase 1 (PAK1)

Impaired skeletal muscle (skm) insulin signaling results in insulin resistance and the development of type 2 diabetes (T2D). Insulin binding to its receptors on skm cells leads to an intracellular signaling cascade resulting in glucose transporter type 4 (GLUT4) translocation to the plasma membrane (PM) and glucose uptake. The p21–activated kinase 1 (PAK1) is a required element for skm insulin sensitivity. It has been shown that whole body PAK1−/− knock‐out (KO) mice exhibit glucose intolerance and insulin resistance. In clonal skm cells (L6‐GLUT4myc) PAK1 inhibition was shown to impair insulin‐induced filamentous actin (F‐actin) remodeling and GLUT4 translocation; coupled with a loss of normal insulin‐stimulated cofilin dephosphorylation (i.e. activation). Recently, we have shown that PAK1 is essential in the process of actin polymerization via p41‐ARC (Actin‐related protein 2/3 complex subunit 1B). However, the effect of skm specific PAK1 modulations on in vivo glucose homeostasis, and downstream effectors of PAK1 are yet to be fully determined.