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Principal Investigator
Principal Investigator
Dr Indrajit Sahu, Phd
My broad research interest is to understand the mechanism of protein degradation by Ubiquitin-Proteasome-System (UPS) in human 3Ds – Disease, Disorders & Development. The UPS is the major protein degradation machinery in all eukaryotes responsible for the timely degradation of the damaged, unused and retired proteins Thereby it regulates almost all cellular signaling pathways during normal and diseased settings. Despite the extensive involvement of Proteasomes in human pathologies and being a potential hotspot for target therapy, we are lacking the deeper understanding on the Proteasome functionality under disease conditions.
Phd Students
Phd Students
Suraj Kumar, CSIR-JRF
Having a hypoxic microenvironment is a common and salient feature of most solid tumours which severely affect the cancer prognosis, diagnosis and the modern therapeutic modalities. Understanding the synergistic relationship between hypoxia and cancer has become an emergent demand. Since proteasome activity and integrity is highly dynamic in hypoxia and can deregulate the cancer cell physiology, we would like to investigate how hypoxic cancer cells manipulate the proteasome function for survival. If we could understand these proteasome impairments, a better therapeutic strategy can be developed to tackle solid tumours
Madhuparna Karmakar, UGC-JRF
Activating Ubiquitin-mediated Proteasomal System for the treatment of Alzheimer's disease
Ravish Javed, UGC-JRF
Understanding the alteration in structural and functional dynamics of host macromolecular complexes upon virus infection is crucial in understanding disease mechanism. My doctoral research is centered on investigating how one of the most vital proteases of SARS-CoV2 influence the human Ubiquitin-Proteasome System (UPS) and alter host protein homeostasis.
Adarsh Mala, JRF
The 26S proteasome is the primary ubiquitin-dependent degradation machinery in eukaryotic cells. In contrast, the 20S proteasome, which constitutes ~50% of cellular proteasomes, acts as an emergency system under hypoxic stress and can degrade both unstructured and globular proteins despite lacking defined substrate-binding sites and unfoldase activity.
My project aims to understand how the 20S proteasome recognizes and unfolds its substrates for proteolysis.
Project Students
Project Students
Lipika Sahu
My study focuses on the interaction between one of the vital Deubiquitinating Enzymes (DUBs) of USP family via the UBL domain and the 26S Proteasome complex. The work highlights the structural aspects underlying their binding interface. This will provide insight into the molecular basis of DUB–proteasome interaction.
Understanding how ubiquitin chain topology is dynamically regulated is essential to decoding cellular proteostasis. My project investigates how deubiquitinases (DUBs) sculpt ubiquitin architecture under basal conditions. I aim to identify constitutively edited substrates and define how disruption of DUB function reshapes the cellular ubiquitin landscape.
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