Institute welcomes new group leader Rahul Samant

Institute welcomes new group leader Rahul Samant

Institute welcomes new group leader Rahul Samant

Key points:

  • Institute welcomes Dr Rahul Samant as a new group leader appointment to the Signalling research programme
  • Dr Samant joins the Institute from Stanford University, California, USA
  • Dr Samant’s research investigates how cells manage misfolded proteins, which has relevance to understanding ageing-related diseases such as Alzheimer’s and the development of treatments.

 
The Institute is delighted to announce that Dr Rahul Samant has joined the Institute as a group leader within the Signalling research programme. Dr Samant joins the Institute from his position as a research associate in Professor Judith Frydman’s lab at Stanford University, in California, USA.
 
Dr Samant’s research focuses on understanding protein misfolding (where a protein assumes an incorrect three-dimensional shape), which not only renders the misfolded protein non-functional, but can also lead to its accumulation into clumps—thereby interfering with critical biological processes. The formation of such misfolded protein aggregates is linked to the pathology of several ageing-related disorders, including Alzheimer’s and Parkinson’s.
 
Institute Director, Professor Michael Wakelam, who is also a group leader within the Signalling programme, said: “On behalf of the whole Institute, I offer the warmest welcome to Rahul as he joins us. Rahul’s work adds an exciting new dimension to our research portfolio. Given that loss of robustness of protein quality control is a major hallmark of ageing and disease, extending our understanding of the processes that govern this is likely to have important outcomes for improving health in later life.”
 
Dr Samant’s work specifically explores the relationship between molecular chaperones (proteins that assist the folding of other proteins) and the system by which proteins are tagged for degradation (‘ubiquitination’). His recent work in yeast, published in Nature last year, has identified that distinct chaperone and ubiquitin systems collaborate to clear misfolded proteins depending on whether they’re located in the cell nucleus or cytoplasm.
 
Dr Samant’s research brings together conventional biochemistry and cell biology techniques with super-resolution fluorescence microscopy and cutting-edge proteomics approaches.
 
After obtaining a BA in Natural Sciences (Biochemistry) from the University of Cambridge, Dr Samant undertook his PhD with Professor Paul Workman at the Institute of Cancer Research, UK, where he characterised the mechanisms of ubiquitin-mediated degradation in the context of a key cancer-associated chaperone, Heat Shock Protein 90. During his time there, he was also involved in a drug discovery programme in collaboration with Merck Serono that discovered a novel class of cyclin-dependent kinase inhibitors. He then moved to join Judith Frydman’s lab at Stanford University to expand the scope of his research to a more global proteome-wide scale, with relevance to a wide range of protein misfolding diseases.
 
Dr Samant said: “I’m genuinely delighted to be starting at the Babraham Institute. I’ve heard nothing but praise for all aspects of the Institute—the people, the science, the facilities, the ethos. My research so far has focused on ubiquitination biology and stress signalling pathways related to misfolded protein degradation. The Signalling programme’s highly complementary strengths in autophagy (the other major degradation pathway) and healthy ageing was definitely a big draw for me. Its cutting-edge core facilities—especially in terms of proteomics and imaging—are also going to be critical for the work we’re doing.
 
“On a more personal level, it’s pretty emotional to be able to start my own research group in the city where I spent some of the happiest years of my life. I’m going to do my best to instil the same passion into the next generation of budding scientists—although given the top-notch research that goes on here, I don’t think it’s going to be too tough a task!”
 
Head of the Signalling Research Programme, Dr Len Stephens FRS, said: "Rahul's research at the Institute will take great momentum from his past work on the chaperone Hsp90 and on how specific ubiquitination mechanisms label proteins and instruct how they will be cleared. Building on these successes, his group will be addressing the exciting and strategically important question of how protein clearance mechanisms respond to stress in healthy and diseased cell contexts."
 

 

Notes to Editors

 
Press contact
Dr Louisa Wood, Communications Manager, louisa.wood@babraham.ac.uk, 01223 496230
 
 
About the Babraham Institute
The Babraham Institute undertakes world-class life sciences research to generate new knowledge of biological mechanisms underpinning ageing, development and the maintenance of health. Our research focuses on cellular signalling, gene regulation and the impact of epigenetic regulation at different stages of life. By determining how the body reacts to dietary and environmental stimuli and manages microbial and viral interactions, we aim to improve wellbeing and support healthier ageing. The Institute is strategically funded by the Biotechnology and Biological Sciences Research Council (BBSRC), part of UK Research and Innovation, through an Institute Core Capability Grant and also receives funding from other UK research councils, charitable foundations, the EU and medical charities.