2015
Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase
Hudson AM, Mannix KM, Cooley L. Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase. Genetics 2015, 201: 1117-1131. PMID: 26384358, PMCID: PMC4649639, DOI: 10.1534/genetics.115.181289.Peer-Reviewed Original ResearchConceptsKelch functionE3 ligaseCullin-RING E3 ligaseGermline ring canalsActin cytoskeletal organizationDrosophila kelch proteinUbiquitin ligase activityCross-link F-actinUbiquitin E3 ligaseRing canalsKelch proteinProtein substratesCytoskeletal defectsCytoskeletal organizationCytoskeletal remodelingLigase activityCullin 3KelchF-actinCytoskeletonLigaseProteasomeVivoCul3Mutagenesis
2014
Angiotensin II signaling via protein kinase C phosphorylates Kelch-like 3, preventing WNK4 degradation
Shibata S, Arroyo JP, Castañeda-Bueno M, Puthumana J, Zhang J, Uchida S, Stone KL, Lam TT, Lifton RP. Angiotensin II signaling via protein kinase C phosphorylates Kelch-like 3, preventing WNK4 degradation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 15556-15561. PMID: 25313067, PMCID: PMC4217463, DOI: 10.1073/pnas.1418342111.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAngiotensin IIAnimalsCarrier ProteinsCell LineHumansKidneyMice, Inbred C57BLMicrofilament ProteinsMolecular Sequence DataPhosphorylationPhosphoserineProtein BindingProtein Kinase CProtein Serine-Threonine KinasesProteolysisSignal TransductionConceptsRenal salt reabsorptionAngiotensin IIVolume depletionSalt reabsorptionNormal physiologic responseProtein kinase CAII administrationBlood pressureCardiovascular diseaseGlobal burdenPhysiologic responsesCullin 3Kinase CNaCl cotransporterReabsorptionHuman genetic studiesSecretionHypertensionNormal mechanismsWNK4 degradationMissense mutationsSerine 433WNK4Inverse relationshipCultured cells
2013
Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4
Shibata S, Zhang J, Puthumana J, Stone KL, Lifton RP. Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 7838-7843. PMID: 23576762, PMCID: PMC3651502, DOI: 10.1073/pnas.1304592110.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsChlorocebus aethiopsCOS CellsCullin ProteinsElectrolytesGene Expression RegulationHomeostasisHumansIntracellular Signaling Peptides and ProteinsMicrofilament ProteinsMinor Histocompatibility AntigensMutationPotassium Channels, Inwardly RectifyingProtein BindingProtein Serine-Threonine KinasesProteomicsPseudohypoaldosteronismUbiquitinUbiquitinationWNK Lysine-Deficient Protein Kinase 1ConceptsPseudohypoaldosteronism type IICullin 3Disease-causing mutationsWNK4 levelsE3 ubiquitin ligase complexUbiquitin ligase complexDominant disease-causing mutationsRare Mendelian syndromePHAII-causing mutationsLigase complexTarget ubiquitinationUbiquitinationRenal salt reabsorptionMolecular explanationMendelian syndromesSpecific substratesCell surfaceWNK4Renal outer medullaryMutationsProtein levelsKelchKLHL3Specific roleElectrolyte homeostasis
2012
Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities
Boyden LM, Choi M, Choate KA, Nelson-Williams CJ, Farhi A, Toka HR, Tikhonova IR, Bjornson R, Mane SM, Colussi G, Lebel M, Gordon RD, Semmekrot BA, Poujol A, Välimäki MJ, De Ferrari ME, Sanjad SA, Gutkin M, Karet FE, Tucci JR, Stockigt JR, Keppler-Noreuil KM, Porter CC, Anand SK, Whiteford ML, Davis ID, Dewar SB, Bettinelli A, Fadrowski JJ, Belsha CW, Hunley TE, Nelson RD, Trachtman H, Cole TR, Pinsk M, Bockenhauer D, Shenoy M, Vaidyanathan P, Foreman JW, Rasoulpour M, Thameem F, Al-Shahrouri HZ, Radhakrishnan J, Gharavi AG, Goilav B, Lifton RP. Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities. Nature 2012, 482: 98-102. PMID: 22266938, PMCID: PMC3278668, DOI: 10.1038/nature10814.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceBlood PressureCarrier ProteinsCohort StudiesCullin ProteinsElectrolytesExonsFemaleGene Expression ProfilingGenes, DominantGenes, RecessiveGenotypeHomeostasisHumansHydrogen-Ion ConcentrationHypertensionMaleMiceMicrofilament ProteinsModels, MolecularMolecular Sequence DataMutationPhenotypePotassiumPseudohypoaldosteronismSodium ChlorideWater-Electrolyte Imbalance
2010
Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton
Hudson AM, Cooley L. Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton. Journal Of Cell Biology 2010, 188: 29-37. PMID: 20065088, PMCID: PMC2812842, DOI: 10.1083/jcb.200909017.Peer-Reviewed Original ResearchConceptsDrosophila KelchCullin 3Cullin-RING ubiquitin E3 ligasesGermline ring canalsSubstrate adaptor proteinCullin-RING ligaseDiverse protein familiesF-actin cytoskeletal structureUbiquitin E3 ligasesProtein ubiquitylationActin cytoskeletonE3 ligasesRing canalsAdaptor proteinProtein familySequence motifsCytoskeletal structuresFilamentous actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeats
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