Moitrayee Bhattacharyya, PhD
Assistant Professor of PharmacologyCards
About
Titles
Assistant 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.
Last Updated on April 07, 2025.
Appointments
Pharmacology
Assistant ProfessorPrimary
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 PMID: 42095550, 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.
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 ResearchTarget membrane proteinsMembrane proteinsMembrane contextSynaptic vesicle membrane proteinVesicle membrane proteinsMammalian membrane proteinsMembrane-active polymersExtraction of membrane proteinsNative nanodiscsOrganellar membranesNative membrane environmentMultiprotein complexesMolecular contextCellular membranesMembrane environmentQuantitative platformBioanalytical approachesExtraction efficiencyOpen-access databasesProteinMembraneExtraction conditionsNanodiscsTarget MPGene 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 ResearchConceptsTissue-specific functionsDNA hydroxymethylationMagnitude of transcriptional changesAlternative splicing eventsMagnitude of gene expression changesTissue-specific genesGene expression changesGene bodiesSplicing eventsDNA methylationModel organismsTranscriptional changesExpression changesGenesAge-related diseasesFunctional roleMouse liverHuman tissuesProlonged quiescenceRestriction functionSplicingDNAMiceAge-related contextSenescence
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 ResearchMembrane proteinsNative membranesOligomeric organizationDiverse membrane proteinsMembrane protein biologyNative cell membranesTarget membrane proteinsNative membrane environmentSingle-molecule resolutionSingle-molecule platformReceptor tyrosine kinasesOligomeric distributionNative nanodiscsOligomerization statusProtein biologySmall GTPaseGrowth factor bindingMembrane environmentOligomeric assembliesTyrosine kinaseCritical regulatorOncogenic mutationsCell membraneProteinMembrane
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 ResearchConceptsRegulatory segmentDependent protein kinase IIExchange of subunitsProtein kinase IIMammalian cellsFluorescence intensity analysisKinase IIOligomeric enzymesHoloenzymePhosphorylated peptidesNeuronal signalingSmall oligomersActive stateSubunitsCaMKIIActivationCrucial roleMolecular dynamics simulationsMass spectrometryKinasePhosphorylationSignalingHub structureBindsEnzymeFlexible 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 ResearchConceptsInhibitory autophosphorylationResidue linkerDependent protein kinase IISingle-molecule assaysMammalian cell expressionProtein kinase IICaMKII variantsShort linkerTransphosphorylation ratesKinase domainCaMKII holoenzymeKinase IIAutophosphorylationHoloenzymeFlexible linkerPrincipal isoformCalcium signalsRelative levelsIsoformsCaMKIIHuman CaCell expressionLinkerVariantsSequence
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 StatementsConceptsDependent protein kinase IIProtein kinase IIKinase domainKinase IISerine/threonine kinaseSpecialized isoformIntact holoenzymeThreonine kinaseCaMKII functionCaMKII holoenzymeSubunit exchangeStructural insightsRecent electron microscopic investigationsCaMKII activityStructural mechanismsFlexible linkerCardiac signalingCentral hubHoloenzymeCaMKIICurrent understandingKey roleKinaseSignalingElectron microscopic investigations
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 ResearchConceptsInactive stateNucleotide exchange factorsDeep mutational scanningVertebrate lineageSequence conservationRas proteinsEvolutionary analysisHigh conservationExchange factorMutational toleranceRas dynamicsMutational effectsSelection pressureMutational scanningGlobal selection pressureSaturation mutagenesisMutational dataRas sequencesProteinBiochemical analysisBiochemical networksMechanistic explanationRegulatorMutationsConservation
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 ResearchConceptsDependent protein kinase IIProtein kinase IICaMKII holoenzymeKinase IIExchange of subunitsKinase domainSubunit exchangeIntersubunit interfaceMolecular mechanismsOligomeric enzymesHoloenzymeHub interfaceCalmodulinCaMKIIThree-way competitionUnactivated onesDimersDodecamericSubunitsOrganismsEnzymeHubMechanismSpiral formActivationProtein Structure and Function: Looking through the Network of Side-Chain Interactions.
Bhattacharyya M, Ghosh S, Vishveshwara S. Protein Structure and Function: Looking through the Network of Side-Chain Interactions. Current Protein And Peptide Science 2016, 17: 4-25. PMID: 26412788, DOI: 10.2174/1389203716666150923105727.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsNetwork theoryImportant problemComplex biological problemsProtein structure networksBipartite networksStructure networkEquilibrium structureModel validationDifferent schemesBiological problemsProblemNetwork approachTheoryNetwork metricsGeneral applicationComplex phenomenonGeneral featuresFormalismNetworkLarge numberProtein structureGeometrySpecific featuresBiological dataEnsemble
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
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Academic Office Number
Mailing Address
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