2016
Kidney Tubular Ablation of Ocrl/Inpp5b Phenocopies Lowe Syndrome Tubulopathy
Inoue K, Balkin DM, Liu L, Nandez R, Wu Y, Tian X, Wang T, Nussbaum R, De Camilli P, Ishibe S. Kidney Tubular Ablation of Ocrl/Inpp5b Phenocopies Lowe Syndrome Tubulopathy. Journal Of The American Society Of Nephrology 2016, 28: 1399-1407. PMID: 27895154, PMCID: PMC5407733, DOI: 10.1681/asn.2016080913.Peer-Reviewed Original ResearchConceptsEarly embryonic lethalityTransporter 5Dent's diseaseIndependent endocytosisEmbryonic lethalityRedundant functionsType 2 inositolHuman phenotypesProximal tubule endocytosisOculocerebrorenal syndromeGenetic ablationCellular levelGermline knockoutLowe syndromeEndocytosisMouse backgroundMice resultsMutationsInositolLow molecular weight proteinuriaINPP5BParalogsProximal tubule functionDramatic effectOCRL
2014
A role of OCRL in clathrin-coated pit dynamics and uncoating revealed by studies of Lowe syndrome cells
Nández R, Balkin DM, Messa M, Liang L, Paradise S, Czapla H, Hein MY, Duncan JS, Mann M, De Camilli P. A role of OCRL in clathrin-coated pit dynamics and uncoating revealed by studies of Lowe syndrome cells. ELife 2014, 3: e02975. PMID: 25107275, PMCID: PMC4358339, DOI: 10.7554/elife.02975.Peer-Reviewed Original ResearchMeSH KeywordsCells, CulturedClathrinClathrin-Coated VesiclesCoated Pits, Cell-MembraneEndocytosisFibroblastsHEK293 CellsHeLa CellsHumansLuminescent ProteinsMicroscopy, ConfocalMicroscopy, ElectronMicroscopy, FluorescenceMutationOculocerebrorenal SyndromePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein BindingProteomeProteomicsRNA InterferenceSorting Nexins
2011
Chloride Channel (Clc)-5 Is Necessary for Exocytic Trafficking of Na+/H+ Exchanger 3 (NHE3)*
Lin Z, Jin S, Duan X, Wang T, Martini S, Hulamm P, Cha B, Hubbard A, Donowitz M, Guggino SE. Chloride Channel (Clc)-5 Is Necessary for Exocytic Trafficking of Na+/H+ Exchanger 3 (NHE3)*. Journal Of Biological Chemistry 2011, 286: 22833-22845. PMID: 21561868, PMCID: PMC3123051, DOI: 10.1074/jbc.m111.224998.Peer-Reviewed Original ResearchConceptsKO miceTrafficking of NHE3Proximal tubulesOpossum kidney cellsNHE3 activityDent's diseaseClC-5Surface expressionNHE3 surface expressionKidney cellsRenal proximal tubulesTotal protein levelsChloride/proton exchangerRates of basalReduced surface expressionKnockdown cellsParathyroid hormoneWT miceDegree of inhibitionCLCN5 geneSurface NHE3MiceTubule perfusionReduced expressionTwo-photon microscopy
2010
Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1
Swan LE, Tomasini L, Pirruccello M, Lunardi J, De Camilli P. Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 3511-3516. PMID: 20133602, PMCID: PMC2840420, DOI: 10.1073/pnas.0914658107.Peer-Reviewed Original Research
2009
A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism
Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism. The EMBO Journal 2009, 28: 1831-1842. PMID: 19536138, PMCID: PMC2711190, DOI: 10.1038/emboj.2009.155.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesClathrinCoated VesiclesEndocytosisHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositolsPhospholipidsPhosphoric Monoester HydrolasesProtein ConformationProtein Structure, TertiaryRatsSequence AlignmentConceptsPH domainNH2-terminal portionEndocytic clathrin-coated pitsClathrin-binding siteClathrin-coated pitsNMR structure determinationNH2-terminal regionCOOH-terminal regionClathrin-box motifsMembrane traffickingEvolutionary pressureSimilar proteinsINPP5BOCRLSpecialized functionsSequence dissimilarityLowe syndromePhosphoinositide metabolismDent's diseaseHeavy chainMutationsRecruitment efficiencyStructure determinationMetabolismDomain
2008
All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding
McCrea HJ, Paradise S, Tomasini L, Addis M, Melis MA, De Matteis MA, De Camilli P. All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding. Biochemical And Biophysical Research Communications 2008, 369: 493-499. PMID: 18307981, PMCID: PMC2442618, DOI: 10.1016/j.bbrc.2008.02.067.Peer-Reviewed Original ResearchConceptsDisease-causing missense mutationsSpecific cellular sitesActive Rab5Endocytic pathwayProtein networkOCRLPatient mutationsAPPL1Missense mutationsLowe syndromeCellular sitesDisease phenotypeRab5Renal Fanconi syndromeMutationsDent's diseaseEndosomesDomainProteinBilateral cataractsNeonatal hypotoniaReabsorption defectFanconi syndromePhenotypeInositol
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply