Dr. Amanjot Singh
India Alliance Wellcome-DBT Intermediate Fellow
Dr. Amanjot Singh is a DBT-Wellcome Trust India Alliance Intermediate Fellow in Manipal Institute of Regenerative Medicine, MAHE, Bengaluru.
Manipal Institute of Regenerative Medicine
Qualification: PhD
CURRENT ACADEMIC ROLE & RESPONSIBILITIES
DBT-Wellcome Trust India Alliance Intermediate Fellow in Manipal Institute of Regenerative Medicine, MAHE, Bengaluru
ACADEMIC QUALIFICATIONS
| Degree | Specialisation | Institute | Year of passing |
|---|---|---|---|
| Ph. D | Molecular Biology | University of Delhi South Campus, New Delhi | 2009 |
Experience
| Institution / Organisation | Designation | Role | Tenure |
|---|---|---|---|
| Manipal Institute of Regenerative Medicine | Faculty Fellow/India Alliance DBT-Wellcome Trust Fellow | Teaching and Research | March 2024-current |
| Institute of Bioinformatics and Applied Biotechnology, Bengaluru | Faculty | Teaching and Research | September 2023-February 2024 |
| National Centre for Biological Sciences (TIFR), Bengaluru | INSA Young Scientist | Research | October 2017-August 2023 |
| University of California San Diego, USA | Post-Doctoral Employee | Research | September 2011-January 2016 |
| The Scripps Research Institute, La Jolla, USA | Research Associate | Research | February 2010-September 2011 |
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.
AREAS OF INTEREST, EXPERTISE AND RESEARCH
Area of Interest
Protein quality control (PQC) system, which include chaperones and components of proteasome, ubiquitin, autophagy and lysosomal systems play important roles in almost all aspects of biology. Recent research has revealed new roles for PQC in dynamics of biological condensates (such as stress granules (SGs)) which are rapidly reversible assemblies formed via quinary interactions (which are both transient and multivalent) among the component RNAs and proteins. Such condensates sequester proteins involved in specific biological pathways or serve as an environment for the management of misfolded proteins. High concentration of misfolded and disordered proteins in condensates makes them prone to support formation of pathogenic protein aggregates of an irreversible nature. Work in the lab involves elucidating how the PQC 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.
Area of Expertise
Molecular Biology, Biochemistry, Cell Biology
Area of Research
My research interest broadly involves understanding how cellular homeostasis is maintained under stress, aging and neurodegeneration
Professional Affiliations & Contributions
Member of the following societies:
- Biochemical Society, UK
Singh A*, Kandi AR#, Jayaprakashappa D#, Thuery G, Purohit DJ, Huelsmeier J, Singh R, Pothapragada SS, Ramaswami M* and Bakthavachalu B* (2022) The transcriptional response to oxidative stress is independent of stress granule formation. Molecular Biology of the Cell 33:ar25, 1-16. (*Co-corresponding authors, # equal contribution)
Singh A*, Huelsmeier J*, Kandi AR, Pothapragada SS, Hillebrand J, Petrauskas A, Agarwal K, Krishnan RT, Thiagarajan D, Jayaprakashappa D, VijayRaghavan K, Ramaswami M and Bakthavachalu B (2021) Antagonistic roles for Ataxin-2 structured and disordered domains in RNP condensation. eLife 10:e60326 (*Equal contribution)
Singh A*, Vashistha N, Heck J, Tang X, Wipf P, Brodsky J, Hampton RY* (2020) Direct involvement of HSP70 ATP hydrolysis in Ubr1-dependent quality control. Molecular Biology of the Cell 31 (24) 2669-2686 (* Corresponding authors) “A Highlights from MBoC Selection”
Bakthavachalu B, Huelsmeier J, Sudhakaran I, Hillebrand J, Singh A, Petrauskas A, Thiagarajan D, Sankaranarayanan M, Mizoe L, Anderson E, Pandey UB, Ross E, VijayRaghavan K, Parker R and Ramaswami M (2018) RNP-granule assembly via Ataxin-2 disordered domains is required for long-term memory and neurodegeneration. Neuron 98: 754-766.
Vashistha N, Neal S, Singh A, Caroll S and Hampton RY (2016) Direct and essential function for Hrd3 in ER-associated degradation. Proceedings of the National Academy of Sciences USA 113: 5934-5939.
Google Scholar Link:- Dr. Amanjot Singh Google Scholar
Scoups : https://www.scopus.com/authid/detail.uri?authorId=57209902346