Principal Investigator
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- Dr. Prasanna Venkatraman
Dr. Prasanna Venkatraman
Principal Investigator
Research Interests
Protein-protein interactions (PPI), typify physical, signalling and regulatory networks that orchestrate cellular responses. PPI are sensitive to levels, mutations, post translational modifications (PTM), and subcellular boundaries. Cancer cells exploit these to rewire networks to maintain mosaic correlations that allow them to survive. The lab tries to understand PPIs at different hierarchical levels with a long term goal is to expose the Achilles heel in cancer.
Current activities include:
- Mapping the molecular details of individual PPIs and characterizing the hot spot sides of interaction
- Exploiting them for the design and evolution of inhibitors
- Structure guided construction of first neighbourhood subnetworks.
- Inferring function and regulation through domain motif interaction
- Expanding the networks by expression analysis and APMS derived PPI
- Deriving context specific pathways that can be described by edge level metrics.
RESEARCH
The lab is interested in the general understanding of the mechanism of cellular homoeostasis both in health and in disease. Synthesis of proteins, their ability to go from a linear polypeptide chain into a final folded structure, the specific functions that they carry out and finally their degradation are tightly and spatio-temporally controlled processes. Any aberration in the above processes is responsible for patho-physiological conditions seen in a multitude of diseases. They believe that dissecting the fundamental mechanism behind these processes will help in better understanding of the global aberrations observed in diseases like cancer and help in the development of new strategies for therapeutic interventions. Along these directions we are currently focusing on the structural, mechanistic and cell biological aspects of protein degradation by a self compartmentalized ubiquitous, ATP dependent regulatory protease called the Proteasomes.
There research now includes a new addition- a molecule from the cell signaling family - 14-3-3 zeta. They have been drawn to this molecule due to its surprising role in functioning as a molecular chaperone. The structural requirement of this protein to function as a chaperone and the identification of a novel ATP binding motif responsible for this function is being investigated. they are keen to explore if this is a unifying principle across the protein family with different isoforms
