Protein Phosphorylation

Our research

Protein phosphorylation is a biological process that regulates most aspects of cellular life, and the enzymes that catalyze this reaction – protein kinases – constitute the largest family of enzymes encoded by the human genome.

An overall aim of our research is to study the regulation and function of protein phosphorylation cascades that are important for the maintenance of a normal energy metabolism and that might be involved in the pathophysiological changes that ultimately lead to type 2 diabetes. We have a specific focus on protein kinases that regulate adipose tissue function, since defects in this tissue, for example in its ability to efficiently store fat, is an underlying cause of insulin resistance and diabetes.

We are currently investigating two protein kinases, namely AMP-activated protein kinase (AMPK) and Salt-inducible kinase 2 (SIK2). Our goal is to determine their role in the control of adipocyte metabolism, both in healthy and in diseased states.

Aims

AMPK activation constitutes a strategy for the treatment of insulin resistance. Using AMPK activators and other tools, we aim to determine the role of AMPK in adipose cells.

SIK2 is an AMPK-related kinase with abundant expression in adipose tissue. We have found that SIK2 is markedly downregulated in human obesity and insulin resistance. Our aim is to determine if and how SIK2 affects insulin sensitivity in adipose cells – specifically in humans.

Impact

Our research will evaluate the usefulness of AMPK activation as an approach for treatment, by predicting the effect of AMPK activation in adipose tissue. The physiological relevance of our studies is reinforced using human cells and tissue. 
Our work on SIK2 will address if downregulation of this protein is a causative factor in development of obesity and insulin resistance.
 

Research output

Link to a list of research output by the group in Lund University’s research portal
 

Team members

Link to a list of team members in Lund University’s research portal