This Collection supports and amplifies research related to SDG 3.
Insulin is one of the most potent and pleiotropic hormones in the body, regulating a myriad of physiological processes. However, perhaps none is best studied as its role in regulating glucose transport into skeletal muscle and adipose tissue. Upon binding to its receptor, insulin triggers a signaling cascade via plasma membrane recruitment of the insulin receptor substrate, and activation of phosphoinositide 3-kinase and Akt. In the context of glucose uptake, Akt then phosphorylates AS160 (TBC1D4) to increase plasma membrane abundance of the insulin-responsive glucose transporter (GLUT4/SLC2A4), and members of the glycolytic pathway including hexokinase 2 (HK2) and 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 (PFKFB2) to enhance glycolytic flux. Beyond this, our understanding of insulin-stimulated glucose uptake signal transduction is incomplete. In fact, advances in phosphoproteomic technologies and bioinformatic approaches have revealed a complex signaling network far more dynamic and kinetic than previously appreciated.
In this collection, we aim to profile some of the exciting avenues researchers are exploring in their attempts to deepen our understanding of insulin stimulated glucose uptake. We welcome research that attempts to deepen our understanding of insulin signal transduction, including but not limited to:
- The identification of novel insulin signaling (i.e. Akt) substrates
- The development of new methods to quantify insulin action
- Phosphoproteomic analysis of the insulin signaling network
- Exploration of metabolite/signaling crosstalk
We also welcome review articles and opinion pieces, especially those profiling lesser-studied or overlooked components of the insulin signaling network, or those which seek to define critical gaps in the field.