DBT/Wellcome Trust India Alliance Intermediate Fellow

 

Research Focus:

Protein quality control (PQC) system, which include chaperones and components of the ubiquitin-proteasome system (UPS) play important roles maintain cellular homeostasis. While chaperones are involved in folding of the proteins, UPS is important for the degradation of terminally misfolded/unfolded proteins. Recent research has revealed new roles for these two arms of the PQC system in the dynamics of biological condensates (such as stress granules (SGs)) which are reversible membraneless assemblies formed via promiscuous interactions (that are both transient and multivalent) among the component RNAs and proteins (which may or may not possess disordered regions). Such condensates sequester proteins involved in specific biological pathways or can serve as an environment for the management of misfolded proteins. High concentration of misfolded and disordered proteins in condensates makes them prone to support the formation of pathological protein aggregates of an irreversible nature which are formed naturally in neurons during aging and neurodegeneration.

Work in our lab involves elucidating how the PQC system is involved in the dynamics of condensates/SGs. We also test the molecular basis of such sequestration of other proteins in SGs or pathological aggregates and how this rewires cellular homeostasis during stress, aging and neurodegeneration.
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Publication:  https://scholar.google.com/citations?hl=en&user=u9UXulYAAAAJ

https://www.scopus.com/authid/detail.uri?authorId=57209902346