Saranga MV

Parkinson's disease (PD) is the second most prevalent neurodegenerative disease. Neurodegeneration accompanied with neuroinflammation, protein degradation dysfunction and mitochondrial dysfunction is commonly associated with the pathogenesis of PD. Although the exact pathogenic mechanism is still not well understood evidence has suggested the role of impaired ubiquitin/proteasome pathway (UPP), lysosome pathway and autophagy machinery in α-synuclein accumulation and degeneration of dopaminergic neurons. The Tripartite Motif (TRIM) family proteins typically have E3 ubiquitin ligase activities and play crucial roles in the degradation of target proteins. TRIM family proteins are known to play important role in various cellular processes like autophagy, innate immune response and inflammation. TRIM proteins having RNA/miRNA binding NHL domain (TRIM2, TRIM3, TRIM32, TRIM 71) are known to regulate neurons. I am currently interested to understand the role of these TRIM-NHL proteins in TNF driven neuroinflammatory stress condition in the cellular model and its implication in mitochondrial dysfunction. This study will provide a better insight into the mitochondrial functions regulated by TRIM proteins which can modulate neuronal health further.