Protein phosphorylation is a signalling mechanism that regulates most aspects of cellular life, and protein kinases, which carry out this post-translational modification, constitute the largest family of enzymes encoded by the human genome. Defects in signal transduction is a mechanism contributing to the development of both cancer and diabetes. Increased knowledge about protein kinase signalling is thus needed to prevent and treat these diseases.

An overall aim of our research is to study the regulation and function of protein phosphorylation cascades with relevance to type 2 diabetes, with a particular focus on adipose tissue, since this tissue is involved in the pathogenesis of diabetes. Presently, our main project evolves around the amp-activated protein kinase (ampk) family, which consists of ampk and another 12 related kinases, of which we are particularly interested in the salt-inducible kinases (1-3). We have shown that sik2 is down-regulated in adipose tissue from obese individuals and are currently investigating the role of sik2 in the development of diabetes. Ampk is a target for new and existing diabetes therapy, and our research will predict effects of such therapy in adipose tissue.