2021
Interdependent Regulation of Polycystin Expression Influences Starvation-Induced Autophagy and Cell Death
Decuypere JP, Van Giel D, Janssens P, Dong K, Somlo S, Cai Y, Mekahli D, Vennekens R. Interdependent Regulation of Polycystin Expression Influences Starvation-Induced Autophagy and Cell Death. International Journal Of Molecular Sciences 2021, 22: 13511. PMID: 34948309, PMCID: PMC8706473, DOI: 10.3390/ijms222413511.Peer-Reviewed Original ResearchConceptsProximal tubular epithelial cellsAutosomal dominant polycystic kidney diseaseEarly-stage ADPKD patientsCell deathPC2 expressionDominant polycystic kidney diseaseTubular epithelial cellsRenal cell survivalPolycystin-1Polycystic kidney diseaseCell survivalPolycystin-2Basal autophagyAutophagic cell survivalCell death resistanceADPKD progressionKidney diseaseADPKD patientsLess cell deathPC1 levelsChronic starvationHealthy individualsDuct cellsEpithelial cellsDeath
2010
Polycystin-2 Activation by Inositol 1,4,5-Trisphosphate-induced Ca2+ Release Requires Its Direct Association with the Inositol 1,4,5-Trisphosphate Receptor in a Signaling Microdomain*
Sammels E, Devogelaere B, Mekahli D, Bultynck G, Missiaen L, Parys JB, Cai Y, Somlo S, De Smedt H. Polycystin-2 Activation by Inositol 1,4,5-Trisphosphate-induced Ca2+ Release Requires Its Direct Association with the Inositol 1,4,5-Trisphosphate Receptor in a Signaling Microdomain*. Journal Of Biological Chemistry 2010, 285: 18794-18805. PMID: 20375013, PMCID: PMC2881802, DOI: 10.1074/jbc.m109.090662.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseKidney diseaseGlutathione S-transferase pulldown experimentsEndoplasmic reticulumTrisphosphate receptorAgonist-induced intracellularTerminal ligand-binding domainMouse renal epithelial cellsTerminal cytoplasmic tailLigand-binding domainAdenoviral expression systemRenal epithelial cellsSignaling microdomainPathological mutantsPulldown experimentsTrisphosphate-induced Ca2Cytoplasmic tailAcidic clusterPolycystin-1Polycystin-2TRPP2Epithelial cellsExpression systemRegulation of ciliary trafficking of polycystin-2 and the pathogenesis of autosomal dominant polycystic kidney disease.
Cai Y, Tang Z. Regulation of ciliary trafficking of polycystin-2 and the pathogenesis of autosomal dominant polycystic kidney disease. Journal Of Central South University Medical Sciences 2010, 35: 93-9. PMID: 20197605, DOI: 10.3969/j.issn.1672-7347.2010.02.001.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseasePolycystic kidney diseaseDominant polycystic kidney diseaseKidney diseasePathogenesis of ADPKDRenal epithelial cellsAccumulated evidenceEpithelial cellsKidney cystsDiseasePathogenesisPossible roleDisorder characteristicsPolycystin-1Polycystin-2Primary cilia
2005
Polycystin-2 Regulates Proliferation and Branching Morphogenesis in Kidney Epithelial Cells*
Grimm DH, Karihaloo A, Cai Y, Somlo S, Cantley LG, Caplan MJ. Polycystin-2 Regulates Proliferation and Branching Morphogenesis in Kidney Epithelial Cells*. Journal Of Biological Chemistry 2005, 281: 137-144. PMID: 16278216, DOI: 10.1074/jbc.m507845200.Peer-Reviewed Original ResearchConceptsPolycystin-2Kidney epithelial cellsPolycystin-1Cell proliferationRegulation of tubulogenesisWild-type proteinMultiple fluid-filled cystsAutosomal dominant polycystic kidney diseaseTubule formationEpithelial cellsExtracellular-related kinaseRegulatory machineryPolycystin proteinsBranching morphogenesisNegative regulatorRespective proteinsGenes PKD1Regulates ProliferationChannel mutantsMorphogenesisFluid-filled cystsCell growthProper growthChannel activityProtein
2004
Calcium Dependence of Polycystin-2 Channel Activity Is Modulated by Phosphorylation at Ser812 *
Cai Y, Anyatonwu G, Okuhara D, Lee KB, Yu Z, Onoe T, Mei CL, Qian Q, Geng L, Wiztgall R, Ehrlich BE, Somlo S. Calcium Dependence of Polycystin-2 Channel Activity Is Modulated by Phosphorylation at Ser812 *. Journal Of Biological Chemistry 2004, 279: 19987-19995. PMID: 14742446, DOI: 10.1074/jbc.m312031200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBiotinylationCalciumCasein Kinase IICell MembraneDNA, ComplementaryEndoplasmic ReticulumGenes, DominantGlutathione TransferaseGlycosylationMembrane ProteinsMiceMice, Inbred BALB CMicroscopy, FluorescenceMutationPhosphatesPhosphorylationPrecipitin TestsProtein Serine-Threonine KinasesProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionSerineTime FactorsTRPP Cation ChannelsConceptsPolycystin-2Non-phosphorylated formChannel activityCation channelsCultured epithelial cellsActivation/inactivationPolycystic kidney diseaseProtein phosphorylationSubstitution mutantsNon-selective cation channelsConstitutive phosphorylationDivalent cation channelsPolycystin-1Substrate domainEndoplasmic reticulumPhosphorylationSingle-channel studiesVivo analysisControl cellsEpithelial cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseaseOpen probabilityCellsCK2
2002
Polycystin-2 is an intracellular calcium release channel
Koulen P, Cai Y, Geng L, Maeda Y, Nishimura S, Witzgall R, Ehrlich BE, Somlo S. Polycystin-2 is an intracellular calcium release channel. Nature Cell Biology 2002, 4: 191-197. PMID: 11854751, DOI: 10.1038/ncb754.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium ChannelsCalcium SignalingEndoplasmic ReticulumHumansIn Vitro TechniquesKidneyLLC-PK1 CellsMembrane PotentialsMembrane ProteinsMiceMice, Inbred C57BLMutationMutation, MissensePolycystic Kidney, Autosomal DominantRecombinant ProteinsSequence DeletionSignal TransductionSwineTRPP Cation ChannelsConceptsAutosomal dominant polycystic kidney diseaseIntracellular calcium release channelsPolycystic kidney diseaseCalcium release channelKidney diseaseTransient receptor potential channelsIntracellular calcium releaseDominant polycystic kidney diseaseRelease channelCalcium release signalsPolycystin-2 functionsType 2 autosomal dominant polycystic kidney diseaseCalcium releasePolycystin-2Single-channel studiesEpithelial cellsPotential channelsDiseaseMissense mutationsRelease signalsCarboxy-terminal truncationDisease-causing missense mutations