Cell Biology
Cell Death and Signaling Group
Indian Institute of Advanced Research (Gandhinagar, India)
Proteins degradation system is a process which is essential for removal of defective and useless proteins from cytoplasm and maintenance of amino acid homeostasis. There are two major pathways accomplish regulated protein catabolism: the ubiquitin-proteasome system (UPS) and the autophagy-lysosomal system. The UPS serves as the primary route for degradation of short-lived proteins and provides the specificity and temporal control needed for fine-tuning the steady-state levels of many regulatory proteins. While autophagy is primarily responsible for degradation of long-lived proteins and protein aggregates and cell organelles. Process of ubiquitination completed in three steps: through the sequential action of the ubiquitin activating enzyme E1, conjugating E2, and ligases E3. Ubiquitin E3 ligases are the most diverse component in this process and mediate the attachment of ubiquitin to the target protein, thus are responsible for the target specificity. Several important proteins of autophagy pathways also act as ubiquitin E3 ligases (ATG-5, ATG-12) and these proteins are important regulatory points of autophagy process. Autophagy is a dynamic, multistep process involving vesicle formation from double layered membrane and subsequently their delivery to lysosome in mammals. To monitor dynamics of autophagy we have established LC3-GFP marker assay using fluorescence microscopy and LC3-immunoblot assay. Present study involves studying the dynamics of Autophagosome formation using high-throughput microscopy and their regulation by ubiquitin proteasome system. My research work also involves elucidation of protein-protein interactions in ubiquitin proteasome system and autophagy pathway using proteomics and high-throughput screening methods.
2008-present CSIR- Junior Research Fellowship
2010-2011 UGC- Junior Research Fellowship
2009-2010 UGC- Junior Research Fellowship


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Sripada L, Tomar D, Prajapati P, Singh R, Singh AK, Singh R.
Tomar D, Singh R, Singh AK, Singh R.
Tomar D, Singh R, Sripada L, Prajapati P, Singh AK, Singh R.
Tomar D, Singh R, Pandya C, Singh AK, Singh, R.
Singh AK, Singh R, Tomar D, Pandya C, Singh R.
Tomar D, Singh AK, Singh R.