Moitrayee Bhattacharyya, PhD
Associate Professor of PharmacologyCards
About
Titles
Associate Professor of Pharmacology
Biography
The Bhattacharyya Lab studies molecular mechanism of kinase signaling, especially in the context of learning, memory and neuropathological conditions. Dr. Bhattacharyya received her PhD in Computational Biophysics at the Indian Institute of Science, Bangalore where she used molecular dynamics simulations and graph theory to study allosteric communication in proteins and its complexes with RNA/DNA. She made a transition into experimental biology during her postdoctoral studies at the University of California Berkeley as a Human Frontier Science Program Long Term Fellow. She used structural biology, single-molecule microscopy, and native mass spectrometry along with computational techniques to study the molecular mechanism of regulation in a calcium/calmodulin-dependent protein kinase that is critical for learning and memory. The Bhattacharyya Lab takes an integrative approach to understand the molecular mechanism of cellular signaling using both experimental and computational techniques.
Appointments
Pharmacology
Associate Professor on TermPrimary
Other Departments & Organizations
- Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS)
- Interdepartmental Neuroscience Program
- Janeway Society
- Molecular Medicine, Pharmacology, and Physiology
- Neural Disorders
- Neuroscience Track
- Pharmacology
- Primary Faculty
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Education & Training
- PhD
- Indian Institute of Science (2012)
Research
Publications
2026
PI3K Regulates Wild-type RAS Signaling to Confer Resistance to KRAS Inhibition
Ge X, Singh J, Li W, Markham C, Ruiz C, Stites E, Bhattacharyya M, Liu Y, Muzumdar M. PI3K Regulates Wild-type RAS Signaling to Confer Resistance to KRAS Inhibition. Cancer Research 2026, 10.1158/0008-5472.can-25-3625. PMID: 42095550, PMCID: PMC13237827, DOI: 10.1158/0008-5472.can-25-3625.Peer-Reviewed Original ResearchThis study investigates how PI3K enables pancreatic cancer cells to resist KRAS inhibitors by activating wild-type RAS signaling, suggesting combined PI3K-KRAS targeting as a therapeutic strategy.From atomic to global connectivity in the structure of the SARS-CoV2-human ACE2 receptor complex
Subramanyan V, Anto A, Bhattacharyya M, Vishveshwara S, Vishveshwara S. From atomic to global connectivity in the structure of the SARS-CoV2-human ACE2 receptor complex. PLOS Complex Systems 2026, 3: e0000096. DOI: 10.1371/journal.pcsy.0000096.Peer-Reviewed Original Research
2024
A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs
Brown C, Ghosh S, McAllister R, Kumar M, Walker G, Sun E, Aman T, Panda A, Kumar S, Li W, Coleman J, Liu Y, Rothman J, Bhattacharyya M, Gupta K. A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs. Nature Methods 2024, 22: 412-421. PMID: 39609567, PMCID: PMC11810782, DOI: 10.1038/s41592-024-02517-x.Peer-Reviewed Original ResearchGene body DNA hydroxymethylation restricts the magnitude of transcriptional changes during aging
Occean J, Yang N, Sun Y, Dawkins M, Munk R, Belair C, Dar S, Anerillas C, Wang L, Shi C, Dunn C, Bernier M, Price N, Kim J, Cui C, Fan J, Bhattacharyya M, De S, Maragkakis M, de Cabo R, Sidoli S, Sen P. Gene body DNA hydroxymethylation restricts the magnitude of transcriptional changes during aging. Nature Communications 2024, 15: 6357. PMID: 39069555, PMCID: PMC11284234, DOI: 10.1038/s41467-024-50725-y.Peer-Reviewed Original Research
2023
Oligomeric organization of membrane proteins from native membranes at nanoscale spatial and single-molecule resolution
Walker G, Brown C, Ge X, Kumar S, Muzumdar M, Gupta K, Bhattacharyya M. Oligomeric organization of membrane proteins from native membranes at nanoscale spatial and single-molecule resolution. Nature Nanotechnology 2023, 19: 85-94. PMID: 38012273, PMCID: PMC10981947, DOI: 10.1038/s41565-023-01547-4.Peer-Reviewed Original Research
2020
Breakage of the Oligomeric CaMKII Hub by the Regulatory Segment of the Kinase
Karandur D, Bhattacharyya M, Xia Z, Lee YK, Muratcioglu S, McAffee D, McSpadden E, Qiu B, Groves JT, Williams ER, Kuriyan J. Breakage of the Oligomeric CaMKII Hub by the Regulatory Segment of the Kinase. ELife 2020, 9: e57784. PMID: 32902386, PMCID: PMC7538161, DOI: 10.7554/elife.57784.Peer-Reviewed Original ResearchFlexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation
Bhattacharyya M, Lee YK, Muratcioglu S, Qiu B, Nyayapati P, Schulman H, Groves JT, Kuriyan J. Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation. ELife 2020, 9: e53670. PMID: 32149607, PMCID: PMC7141811, DOI: 10.7554/elife.53670.Peer-Reviewed Original Research
2019
Structural Insights into the Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII).
Bhattacharyya M, Karandur D, Kuriyan J. Structural Insights into the Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII). Cold Spring Harbor Perspectives In Biology 2019, 12: a035147. PMID: 31653643, PMCID: PMC7263085, DOI: 10.1101/cshperspect.a035147.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
2017
Deconstruction of the Ras switching cycle through saturation mutagenesis
Bandaru P, Shah NH, Bhattacharyya M, Barton JP, Kondo Y, Cofsky JC, Gee CL, Chakraborty AK, Kortemme T, Ranganathan R, Kuriyan J. Deconstruction of the Ras switching cycle through saturation mutagenesis. ELife 2017, 6: e27810. PMID: 28686159, PMCID: PMC5538825, DOI: 10.7554/elife.27810.Peer-Reviewed Original Research
2016
Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II
Bhattacharyya M, Stratton MM, Going CC, McSpadden ED, Huang Y, Susa AC, Elleman A, Cao YM, Pappireddi N, Burkhardt P, Gee CL, Barros T, Schulman H, Williams ER, Kuriyan J. Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II. ELife 2016, 5: e13405. PMID: 26949248, PMCID: PMC4859805, DOI: 10.7554/elife.13405.Peer-Reviewed Original Research
Academic Achievements & Community Involvement
News & Links
Media
- SMALP-based purification of Trk receptor tyrosine kinase from cells with minimal perturbation to its endogenous lipid environment for spatial lipidomics analysis (to measure changes in the membrane lipid composition in the immediate vicinity of the kinase under different states of activation, ligand binding and disease-mutations), single-molecule studies and native-MS interrogation (to study the effect of the endogenous lipid environment on the organization and signaling of Trk receptor isoforms).
- A molecular mechanistic investigation of the signaling pathways impli- cated in learning and memory and the pathologies of Down Syndrome like cognitive impairments and accelerated aging
News
Get In Touch
Contacts
Pharmacology
Sterling Hall of Medicine, B-Wing - 333 Cedar Street, SHM B316B
New Haven, CT 06510
United States
Locations
SHM B316B
Academic Office
Sterling Hall of Medicine, B-Wing
333 Cedar Street
New Haven, CT 06510