2008
Polycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling
Lal M, Song X, Pluznick JL, Di Giovanni V, Merrick DM, Rosenblum ND, Chauvet V, Gottardi CJ, Pei Y, Caplan MJ. Polycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling. Human Molecular Genetics 2008, 17: 3105-3117. PMID: 18632682, PMCID: PMC2722884, DOI: 10.1093/hmg/ddn208.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBinding SitesCell LineCell NucleusCHO CellsCricetinaeCricetulusGene Expression ProfilingGene Expression RegulationHumansLigandsOligonucleotide Array Sequence AnalysisPeptide FragmentsPolycystic Kidney, Autosomal DominantRecombinant ProteinsSignal TransductionSystems BiologyTCF Transcription FactorsTransfectionTRPP Cation ChannelsWnt ProteinsConceptsC-terminal tailCanonical WntPolycystin-1Wnt-dependent signalingDNA microarray analysisDependent gene transcriptionN-terminal portionInhibits canonical WntTCF proteinsT-cell factorAutosomal dominant polycystic kidney disease (ADPKD) casesMotif presentGene transcriptionDevelopmental processesMicroarray analysisWntPKD1 geneΒ-cateninNovel mechanism
2005
The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit
Zatti A, Chauvet V, Rajendran V, Kimura T, Pagel P, Caplan MJ. The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit. Molecular Biology Of The Cell 2005, 16: 5087-5093. PMID: 16107561, PMCID: PMC1266409, DOI: 10.1091/mbc.e05-03-0200.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Cytoplasmic C-terminal tailK-ATPase α-subunitPolycystin-1 proteinK-ATPase activityRegulation of NaChinese hamster ovary cellsProtein interactsHamster ovary cellsProtein exhibitΑ-subunitFunctional studiesAmino acidsPKD1 geneOvary cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseInteractsKinetic propertiesRegulationGenesTailProtein
2004
Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
Chauvet V, Tian X, Husson H, Grimm DH, Wang T, Hieseberger T, Igarashi P, Bennett AM, Ibraghimov-Beskrovnaya O, Somlo S, Caplan MJ. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. Journal Of Clinical Investigation 2004, 114: 1433-1443. PMID: 15545994, PMCID: PMC525739, DOI: 10.1172/jci21753.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell NucleusChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusDogsEmbryo, MammalianEpithelial CellsKidney TubulesMembrane ProteinsMiceMice, TransgenicPolycystic Kidney, Autosomal DominantProteinsSequence DeletionSignal TransductionStress, MechanicalTranscription Factor AP-1TRPP Cation ChannelsConceptsC-terminal tailAutosomal dominant polycystic kidney diseaseCell-matrix interactionsCiliary signalingSecond genePolycystin-2Polycystin-1C-terminusNovel pathwayProteolytic cleavageNuclear translocationMechanical stimuliGenesDominant polycystic kidney diseasePolycystic kidney diseasePrecise mechanismCleavageTerminusSignalingTranslocationNucleusPathway