Suresh Mishra, Assistant Professor (Adjunct)

Posttranslational modifications (PTMs) of proteins expand nature’s repertoire by increasing the inventory of side chains available to proteins. The purpose of controlled PTMs is to increase the diversity of functional groups beyond those in the side chains of the 20 proteinogenic amino acids incorporated into nascent proteins. With the completion of the human genome and rapid progress in understanding the proteome, it now is clear that the next phase of molecular bioscience largely will focus on PTMs and their regulation of protein functions. Given the relatively small number of genes and proteins in complex organisms, PTMs (and also RNA splicing) create the enormous and highly dynamic structural and functional diversity required to regulate essential cellular functions. This diversity enables new chemistry; new recognition patterns for partner molecules, turns on and off enzyme activity, and controls the lifetime and location of such proteins in cells.

Academic Achievements:

• Assistant Professor (Internal Medicine & Physiology) University of Manitoba, 2007-present
• Reader (Endocrinology), University of Delhi, India 2004-05
• Research Associate (Physiology), University of Manitoba, Canada
• Postdoctoral Fellow (Ob/Gyn), University of Louisville, USA
• Ph.D. (Biochemistry & Endocrinology), University of Delhi, India
• M.Phil. (Biochemistry & Endocrinology), University of Delhi, India
• M.Sc. (Reproductive Endocrinology), University of Delhi, India

 

Research Interests

We are exploring changes in PTMs in insulin signaling intermediates and mitochondrial proteins in relation to insulin resistance and mitochondrial dysfunction, modification mediated changes in protein function and protein-protein interactions. A number of established pathways/factors known to contribute to the development of type 2 diabetes are interconnected with each other and PTM of proteins play a critical role in this process. Therefore, key to developing improved pharmacological interventions is an understanding of the integration of pathways known to be involved in the pathophysiology of diabetes. Targeting key points of integration of these pathways should provide a novel and more effective strategy for prevention or treatment of type 2 diabetes.
We have recently discovered that tyrosine phosphorylation plays a regulatory role in the crosstalk between serine/threonine phosphorylation and O-GlcNAc modification (enzymatic protein modification by β-N-acetylglucosamine) in cell signaling proteins. Although this discovery was made while working on a pleiotropic protein prohibitin, implication this novel finding extends beyond protein specific function and may represent a general regulatory mechanism involved in receptor tyrosine kinase and immune receptor signaling which is open for direct experimental examination.

 

Search PubMed for publications by Mishra S