2021
The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2
Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. Communications Biology 2021, 4: 226. PMID: 33597714, PMCID: PMC7889885, DOI: 10.1038/s42003-021-01750-w.Peer-Reviewed Original ResearchConceptsCryo-electron microscopy structureHuman NKCC1Microscopy structureEssential residuesFunctional characterizationKCC transportersPlasma membraneStructural basisTransepithelial saltTransport activityMechanistic understandingTransportersStructural studiesCritical roleCotransporter NKCC1Computational analysisIon transportWater transportNeuronal excitabilityNKCC1PhosphorylationCell volumeNKCCKCC2Residues
2018
Polycystin-1, the product of the polycystic kidney disease gene PKD1, is post-translationally modified by palmitoylation
Roy K, Marin EP. Polycystin-1, the product of the polycystic kidney disease gene PKD1, is post-translationally modified by palmitoylation. Molecular Biology Reports 2018, 45: 1515-1521. PMID: 30073588, DOI: 10.1007/s11033-018-4224-6.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseaseProteins polycystin-1End-stage renal diseasePossible pharmacologic targetsStage renal diseasePossible modifiable factorsRate of progressionDominant polycystic kidney diseaseExpression levelsPolycystic kidney diseaseRenal diseaseKidney diseaseModifiable factorsCommon causePharmacologic targetPolycystin-1Carboxyl-terminal fragmentKidney cystsPC1 expressionPotential causesDiseaseDistinct mutationsPost-translational modificationsMultiple complementary approachesGenes PKD1
2017
Palmitoylation of the ciliary GTPase ARL13b is necessary for its stability and its role in cilia formation
Roy K, Jerman S, Jozsef L, McNamara T, Onyekaba G, Sun Z, Marin EP. Palmitoylation of the ciliary GTPase ARL13b is necessary for its stability and its role in cilia formation. Journal Of Biological Chemistry 2017, 292: 17703-17717. PMID: 28848045, PMCID: PMC5663873, DOI: 10.1074/jbc.m117.792937.Peer-Reviewed Original ResearchConceptsPost-translational attachmentMost mammalian cellsCiliary GTPase Arl13bCilia localizationProtein palmitoylationCiliary proteinsCilia proteinsProtein localizationCilia formationMammalian cellsCilia functionPalmitoylationPrimary ciliaPlasma membraneCilia resorptionArl13bFunctional importanceMyristoylationCiliaCritical roleProteinMouse kidneyLocalizationDepalmitoylationCellsCellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario
Majumder P, Roy K, Singh BK, Jana NR, Mukhopadhyay D. Cellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario. Disease Models & Mechanisms 2017, 10: 655-669. PMID: 28360125, PMCID: PMC5451165, DOI: 10.1242/dmm.027748.Peer-Reviewed Original ResearchConceptsAD-like conditionsDisease manifestCytoskeletal architecturePak1 proteinCytoskeleton stabilityAD mouse brainCytoskeletal proteinsGrb2 overexpressionGrb2Β-amyloid oligomersPotential new strategyCellular levelNeuronal lossAD patientsPreventive roleCytoskeletonProteinMouse brainBrain tissueExtracellular accumulationPotent inducerMolecular featuresUnique roleDomain levelCytoskeletal
2013
Differential Expression of Neuroblastoma Cellular Proteome due to AICD Overexpression
Chakrabarti A, Roy K, Mukhopadhyay D. Differential Expression of Neuroblastoma Cellular Proteome due to AICD Overexpression. Journal Of Alzheimer's Disease 2013, 38: 845-855. PMID: 24081375, DOI: 10.3233/jad-130695.Peer-Reviewed Original ResearchConceptsAmyloid-β protein precursor intracellular domainCell linesProteomic expression patternsDifferent functional classesCellular proteomeCytoskeletal dynamicsProtein foldingIntracellular domainExpression patternsBiological processesBiological pathwaysMALDI-MS identificationNormal proteomeDifferential expressionSHSY5Y cell lineNeuroblastoma cell linesKey playersProteomeAlzheimer's diseaseProtein overloadArtifactual consequenceProteinAD-like conditionsAD phenotypePathophysiological effectsGrowth Factor Receptor-Bound Protein 2 Promotes Autophagic Removal of Amyloid-β Protein Precursor Intracellular Domain Overload in Neuronal Cells
Roy K, Raychaudhuri M, Chakrabarti O, Mukhopadhyay D. Growth Factor Receptor-Bound Protein 2 Promotes Autophagic Removal of Amyloid-β Protein Precursor Intracellular Domain Overload in Neuronal Cells. Journal Of Alzheimer's Disease 2013, 38: 881-895. PMID: 24100123, DOI: 10.3233/jad-130929.Peer-Reviewed Original ResearchConceptsAmyloid-β protein precursor intracellular domainRole of Grb2Dynamin-independent mannerTypes of vesiclesAutophagic removalApoptosis pointsGrowth factor receptorIntracellular domainVesicle accumulationCaspase activityDisease brainNeuronal cellsAD cell modelGrb2Independent mannerFactor receptorVesiclesAutophagosomesExcess conditionsAlzheimer's disease brainProtein overloadStudy unravelsCell modelCytotoxic effectsCells