2019
Apical-Basal Polarity Signaling Components, Lgl1 and aPKCs, Control Glutamatergic Synapse Number and Function
Scott J, Thakar S, Mao Y, Qin H, Hejran H, Lee SY, Yu T, Klezovitch O, Cheng H, Mu Y, Ghosh S, Vasioukhin V, Zou Y. Apical-Basal Polarity Signaling Components, Lgl1 and aPKCs, Control Glutamatergic Synapse Number and Function. IScience 2019, 20: 25-41. PMID: 31546104, PMCID: PMC6817635, DOI: 10.1016/j.isci.2019.09.005.Peer-Reviewed Original ResearchAtypical protein kinase CsApical-basal polarity proteinsPolarity proteinsPlanar cell polarity proteinsCell polarity proteinsConditional knockoutSynapse formationProtein kinase CsSmith-Magenis syndromeGlutamatergic synapse developmentSynapse numberKnockout embryosSignaling ComponentsSynapse developmentNormal synapse formationLgl1ProteinPostsynaptic densityCultured cortical neuronsKnockoutSynaptosome fractionVangl2EmbryosImpaired plasticityCortical neurons
2018
PAR3–PAR6–atypical PKC polarity complex proteins in neuronal polarization
Hapak SM, Rothlin CV, Ghosh S. PAR3–PAR6–atypical PKC polarity complex proteins in neuronal polarization. Cellular And Molecular Life Sciences 2018, 75: 2735-2761. PMID: 29696344, PMCID: PMC11105418, DOI: 10.1007/s00018-018-2828-6.BooksConceptsPar3-Par6Neuronal polarityNeuronal polarizationPolarity complex proteinsAPKC kinase activityEukaryotic cell typesProtein complexesComplex proteinsKinase activityPar6APKCSignaling mechanismCell typesPar3Effector moleculesProteinImportant roleEffector functionsPolarityComplexesFundamental featuresPathwayRoleAssemblyCells
2015
PKCι interacts with Rab14 and modulates epithelial barrier function through regulation of claudin-2 levels
Lu R, Dalgalan D, Mandell EK, Parker SS, Ghosh S, Wilson JM. PKCι interacts with Rab14 and modulates epithelial barrier function through regulation of claudin-2 levels. Molecular Biology Of The Cell 2015, 26: 1523-1531. PMID: 25694446, PMCID: PMC4395131, DOI: 10.1091/mbc.e14-12-1613.Peer-Reviewed Original ResearchConceptsClaudin-2 levelsSmall GTPase Rab14Claudin-2 protein levelsClaudin-2Junction proteinsTransepithelial resistanceEpithelial polarityIntracellular punctaTight junction componentsTight junction proteinsPlasma membraneNormal assemblyRab14 expressionRab14Junction componentsPKCιKnockdownEpithelial barrier functionProtein levelsTight junctionsZO-1ProteinParacellular permeabilityClaudin-1APKC
2010
Telomere-independent Rap1 is an IKK adaptor and regulates NF-κB-dependent gene expression
Teo H, Ghosh S, Luesch H, Ghosh A, Wong ET, Malik N, Orth A, de Jesus P, Perry AS, Oliver JD, Tran NL, Speiser LJ, Wong M, Saez E, Schultz P, Chanda SK, Verma IM, Tergaonkar V. Telomere-independent Rap1 is an IKK adaptor and regulates NF-κB-dependent gene expression. Nature Cell Biology 2010, 12: 758-767. PMID: 20622870, DOI: 10.1038/ncb2080.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBlotting, WesternCell LineCell Line, TumorChromatin ImmunoprecipitationChromatography, GelHeLa CellsHumansI-kappa B KinaseImmunohistochemistryImmunoprecipitationKaplan-Meier EstimateMiceNF-kappa BPhosphorylationPolymerase Chain ReactionProtein BindingRNA, Small InterferingShelterin ComplexTelomere-Binding ProteinsTissue Array Analysis
2005
Coexpressed EphA Receptors and Ephrin-A Ligands Mediate Opposing Actions on Growth Cone Navigation from Distinct Membrane Domains
Marquardt T, Shirasaki R, Ghosh S, Andrews SE, Carter N, Hunter T, Pfaff SL. Coexpressed EphA Receptors and Ephrin-A Ligands Mediate Opposing Actions on Growth Cone Navigation from Distinct Membrane Domains. Cell 2005, 121: 127-139. PMID: 15820684, DOI: 10.1016/j.cell.2005.01.020.Peer-Reviewed Original ResearchConceptsDistinct membrane domainsMembrane domainsGrowth conesContact-dependent signalingEph receptor tyrosine kinasesReceptor tyrosine kinasesNeuronal growth conesGrowth cone navigationEphA receptorsMotor neuron growth conesSubcellular arrangementGuidance receptorsNeuron growth conesTyrosine kinaseEphrin proteinsReceptor proteinCell typesEphrinProteinPathological processes