A microscopy image showing layers in different colors and a network of neurons

Department of
Biology

Photo of Siddhesh  S. Kamat

Siddhesh S. Kamat

Associate Professor

Biology

Chemical biology, metabolomics, chemoproteomics, lipid metabolism, protein biochemistry

+91-20-25908433

siddhesh@iiserpune.ac.in

Siddhesh Kamat is currently an Associate Professor, a SwarnaJayanti Fellow, and an EMBO Young Investigator, in the Department of Biology at IISER Pune. Dr. Kamat completed his BTech from the Institute of Chemical Technology (former UDCT) in 2007, and a PhD from the Department of Chemistry at Texas A&M University in 2012. Dr Kamat was the 9th Irving S. Sigal Postdoctoral Fellow of the American Chemical Society at the Department of Chemical Physiology, The Scripps Research Institute. He joined IISER Pune in 2016.

Research

Chemical biology of mammalian lipid signalling pathways

Dr. Siddhesh Kamat's group is interested in studying the biological mechanisms of lipid signaling pathways in the mammalian nervous and immune system. To achieve their goals, the group integrates aspects of chemical biology, biochemistry, molecular and cell biology, immunology, animal and/or cellular models, in conjunction with advanced mass spectrometry (LC-MS) based metabolomics and proteomics techniques. The long term goal is to identify and understand as-of-yet uncharacterized lipid signaling pathways in vivo, annotate enzymes and receptors that regulate their biology and provide new insights and therapeutic paradigms for orphan and/or emerging human neurological and immunological diseases.

Selected Publications

Mondal, S., Kinatukara, P., Singh, S., Shambhavi, S., Patil, G. S., Dubey, N., Singh, S. M., Pal, B., Shekar, P. C., Kamat, S. S., Sankarnarayanan, R. (2022) Dip2 is a unique regulator of diacylglycerol lipid homeostasis in eukaryotes, eLife 11, e77665.

Rajendran, A., Soory, A., Khandelwal, N., Ratnaparkhi, G. S., Kamat, S. S.* (2022) A multi-omics analysis reveals that the lysine deacetylase ABHD14B influences glucose metabolism in mammals, J. Biological Chemistry 298 (7), 102128, 1- 14. 

Mehdiratta, K., Singh, S., Sharma, S., Bhosale, R. S., Choudhary, R., Masal, D. P., Manocha, A., Dhamale, B. D., Khan, N., Vivekanand, A., Sharma, P., Ikeh, M., Brown A. C., Parish, T., Ojha, A., Michael, J. S., Faruq, M., Medigeshi, G. R., Mohanty, D., Reddy, D. S., Natarajan, V. T., Kamat, S. S.*, Gokhale, R. S.* (2022) Kupyaphores are zinc homeostatic metallophores required for colonization of Mycobacterium tuberculosis, PNAS 119(8), e2110293119. 

Mehendale, N., Mallik, R. M., Kamat, S. S.* (2021) Mapping sphingolipid metabolism pathways during phagosomal maturation, ACS Chemical Biology 16(12), 2757-2765. 

Khandelwal, N., Shaikh, M., Mhetre, A., Singh, S., Sajeevan, T., Joshi, A., Balaji, K. N., Chakrapani, H., Kamat, S. S.* (2021) Fatty acid chain length drives lysophosphatidylserine dependent immunological outputs, Cell Chemical Biology 28, 1169-1179. 

Singh, S., Joshi, A., Kamat, S. S.* (2020) Mapping the neuroanatomy of ABHD16A-ABHD12 & lysophosphatidylserines provides new insights into the pathophysiology of the human neurological disorder PHARC, Biochemistry 59 (24), 2299-2311. 

Rajendran, A., Vaidya, K., Mendoza, J., Bridwell-Rabb, J., Kamat, S. S.* (2020) Functional annotation of ABHD14B, an orphan serine hydrolase enzyme, Biochemistry 59 (2), 183-196 

Kelkar, D. S., Ravikumar, G., Mehendale, N., Singh, S., Joshi, A., Sharma, A. K., Mhetre, A., Rajendan, A., Chakrapani, H., Kamat, S. S.* (2019) A chemical genetic screen identifies ABHD12 as an oxidized phosphatidylserine lipase, Nature Chemical Biology 15, 169-178. 

Joshi, A., Shaikh, M., Singh, S., Rajendran, A., Mhetre, A., Kamat, S. S.* (2018) Biochemical characterization of the PHARC associated serine hydrolase ABHD12 reveals its preference for long chain lipids, J. Biological Chemistry 293, 16953-16963. 

Pathak, D., Mehendale, N., Singh, S., Mallik, R. M., Kamat, S. S.* (2018) Lipidomics suggests a new role for ceramide synthase in phagocytosis, ACS Chemical Biology 13, 2280-2287.