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Don Blumenthal

associate Professor of Pharmacology and Toxicology and of Biochemistry and of Biomedical Informatics

B.A. University of California, San Diego

Ph.D. University of California, San Diego

 

Research

References

Don.Blumenthal{at}pharm.utah.edu

 

Research

My laboratory is broadly interested in the enzymes known as protein kinases and their roles in cell function and disease. Protein kinases catalyze the phosphorylation of proteins on serine, threonine, and tyrosine residues, which is the most widespread mechanism for the reversible covalent modification of protein structure and function. Protein kinases are the largest enzyme superfamily in eukaryotes, with more 8,000 unique protein kinase genes currently identified. In humans, the protein kinase superfamily consists of more than 500 genes, many of which are directly or indirectly involved in a variety of disease processes including cancer, diabetes, and heart disease. A better understanding of the role of specific protein kinases in disease processes is key to developing drugs that target protein kinases and improved therapies for these diseases.

The specific protein kinases being studied in my laboratory include the cAMP-dependent protein kinase (also known as protein kinase A or PKA), myosin light chain kinase (MLCK), and phosphorylase kinase (PhK). These protein kinases have very different subunit structures and are regulated in very different ways, even though their catalytic domains are homologous. Our research ranges from biochemical and biophysical studies of protein kinase structure and function, to studies of protein kinase activity in different disease states. One of our primary goals is to understand, at the molecular level, how different protein kinases are regulated so that we might better understand disease states in which protein kinase activities are dysregulated.

Much of our current research efforts are directed towards biophysical studies of protein kinases using fluorescence, circular dichroism, and small-angle x-ray and neutron scattering. Many of these studies involve the use of synthetic and expressed peptides that correspond to protein kinase regulatory domains. In the case of the calmodulin-regulated protein kinases, MLCK and PhK, we have shown that such peptides exhibit many of the properties of the whole protein, such as their affinity for calmodulin. Because of their small size compared to the intact protein kinase, they are often ideal for biophysical studies aimed at identifying key amino acids important for kinase function.

References