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Chemical Biology Laboratory
The Chemical Biology Laboratory deploys cellular and molecular biology approaches to explore the pathogenesis of cancer and other neurodegenerative diseases. Given the interest in neuronal death, it is no wonder that this lab team is interested in E3 ubiquitin ligases essential for quality control events in neuronal survival. Protein ubiquitylation is highly versatile, ordered, the multistep post translation modification enzymatic process that regulates numerous aspects of cell physiology. This lab team has been studying the role of such E3 ligases to find out the role of quality control E3 ubiquitin ligases in maintenance of proteostasis and hence playing a role in cellular survival and death. Such important biochemical findings may contribute to innovative therapeutic approaches for the diseases associated with misfolded proteins.
Organisms at the cellular level possess a well-established protein quality control mechanism which the lab team is trying to understand at present. The role of E3 ubiquitin ligases was reported in such mechanisms so far. Our laboratory is dedicated to a qualitative research in the field of protein quality control mechanisms. We have recently found that a HECT domain containing E3 ubiquitin ligase E6-AP helps in Amyotrophic Lateral Sclerosis diseases suppression through its association with the misfolded protein aggregates formed by SOD1 mutants. Such findings support that an E3 ligase can have a capability to clear the misfolded protein aggregation. However, while appreciating the incredible efficiency of cellular systems, we must recognize the crucial role of chaperones which are supposed to work preferentially compared to E3 ubiquitin ligases in order to refold the misfolded proteins, and hence conserving the energy utilized during the translation of those proteins. Various examples made us think that we could explore the role of both the chaperones and E3 ubiquitin ligases in the clearance of misfolded proteins. Therefore, now we are working not only with E3 ubiquitin ligases but also with the chaperones and even in their functional association to confer an efficient quality control mechanism to the cell.

 

 

 
 
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