CSIR - Centre for Cellular & Molecular Biology
Council of Scientific and Industrial Research
Ministry of Science & Technology, Govt. of India
Senior Principal Scientist
Email: janesh@ccmb.res.in
Phone: 040-27192588
Research Interests:
Ionotropic glutamate receptors (iGluRs) mediate 60% of excitatory neurotransmission in the central nervous system (CNS). They are encoded by 18 genes in vertebrates that assemble as tetrameric cation channels with distinct functional properties into four groups, namely; AMPA (?-amino-3-hydroxy-5-methyl-4-isoxalolepropionic acid), NMDA (N-methyl-D-aspartic acid), Kainate and Delta families. Their dysfunction is linked to a number of neurological disorders such as autism, epilepsy, schizophrenia, psychiatric disorders, and pain. Our group primarily focuses on the kainate and delta receptor families. On the one hand, we intend to elucidate the molecular underpinnings of receptor assembly, gating, and modulation; on the other hand, we are interested in deciphering the architecture of native, heteromeric receptors and their complexes with auxiliary proteins.
We employ a multipronged approach that includes single-particle cryo-electron microscopy, X-ray crystallography, electrophysiology, and a host of biophysical and biochemical techniques to gain insights into how iGluRs work and are modulated by their cognate auxiliary proteins to affect synaptic neurotransmission and plasticity.
Selected Publications
Dhingra S, Chopade PM, Vinnakota R, Kumar J. Functional Implications of the Exon 9 Splice Insert in GluK1 Kainate Receptors. eLife 2023 12: RP89755, https://doi.org/10.7554/eLife.89755.1
Kumar J, Popescu GK, Gantz SC. GluD receptors are functional ion channels. Biophys J. 2023 Jun 20;122(12):2383-2395. doi: 10.1016/j.bpj.2023.05.012.
Vinnakota R, Dhingra S, Kumari J, Ansari MY, Shukla E, Nerkar MD, Kumar J. Role of Neto1 extracellular domain in modulation of kainate receptors. Int J Biol Macromol. 2021 Oct 8;192:525-536. doi: 10.1016/j.ijbiomac.2021.10.001.
George B, Assaiya A, Roy RJ, Kembhavi A, Chauhan R, Paul G, Kumar J*, Ninan SP*. CASSPER is a semantic segmentation-based particle picking algorithm for single-particle cryo-electron microscopy. Commun Biol. 2021 Feb 15;4(1):200. doi:/10.1038/s42003-021-01721-1 (*Corressponding authors)
Kumari J, Bendre AD, Bhosale S, Vinnakota R, Burada AP, Tria G, Ravelli R, Peters PJ, Kumar J. Structural dynamics of the GluK3-kainate receptor neurotransmitter binding domains revealed by cryo-EM. Int J Biol Macromol. 2020 Apr 15; 149:1051–8.
Burada AP, Vinnakota R, Kumar J. Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture. Nat Struct Mol Biol. 2020 Jan;27(1):84-91. doi: 10.1038/s41594-019-0359-y.
Education & Experience
P.G: | M.Sc (Biotechnology) ; Devi Ahilya University, Indore, Madhya Pradesh, India ; 1999-2001 |
Ph.D: | All India Institute of Medical Science,New Delhi, India ; 2002-2007 ; |
Post.Doc: | National Institute of Child Health and Human Development (NICHD), National Institutes of Health (NIH), Bethesda, MD, USA ; 2007-2013 ; |
Experience: |
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Title | Journal | Year |
---|---|---|
Functional Implications of the Exon 9 Splice Insert in GluK1 Kainate Receptors | bioRxiv | 2023 |
GluD receptors are functional ion channels | Biophys J | 2023 |
Structure, Function, and Regulation of the Kainate Receptor | Subcell Biochem. | 2022 |
Ionotropic glutamate delta receptors: The enigma has finally begun to unravel | Neuropharmacology | 2022 |
Role of Neto1 extracellular domain in modulation of kainate receptors. | Int J Biol Macromol | 2021 |
Structural biology of ionotropic glutamate delta receptors and their crosstalk with metabotropic glutamate receptors | Neuropharmacology | 2021 |
An overview of the recent advances in cryo-electron microscopy for life sciences | Emerg Top Life Sci. | 2021 |
CASSPER is a semantic segmentation-based particle picking algorithm for single-particle cryo-electron microscopy | Commun Biol. | 2021 |
Emerging insights into the structure and function of ionotropic glutamate delta receptors | Br J Pharmacol | 2020 |
The architecture of GluD2 ionotropic delta glutamate receptor elucidated by cryo-EM | J Struct Biol. | 2020 |
Structural dynamics of the GluK3-kainate receptor neurotransmitter binding domains revealed by cryo-EM | Int J Biol Macromol. | 2020 |
Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture | Nat Struct Mol Biol. | 2020 |
Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery | Sci Rep. | 2019 |
Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports | Sci Rep | 2014 |
Structural mechanism of glutamate receptor activation and desensitization. | Nature | 2014 |
Functional insights from glutamate receptor ion channel structures. | Annu Rev Physiol. | 2013 |
Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface. | Neuron | 2012 |
Structure and assembly mechanism for heteromeric kainate receptors. | Neuron | 2011 |
A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq. | Nucleic Acids Res. | 2011 |
Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains | J Mol Biol. | 2010 |
Domain organization and function in GluK2 subtype kainate receptors | Proc Natl Acad Sci U S A. | 2010 |
The N-terminal domain of GluR6-subtype glutamate receptor ion channels. | Nat Struct Mol Biol. | 2009 |
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janesh@ccmb.res.in
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shivpratap@ccmb.res.in
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sanjaysuman@ccmb.res.in
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