2017
SHARPIN-mediated regulation of protein arginine methyltransferase 5 controls melanoma growth
Tamiya H, Kim H, Klymenko O, Kim H, Feng Y, Zhang T, Han JY, Murao A, Snipas SJ, Jilaveanu L, Brown K, Kluger H, Zhang H, Iwai K, Ronai Z. SHARPIN-mediated regulation of protein arginine methyltransferase 5 controls melanoma growth. Journal Of Clinical Investigation 2017, 128: 517-530. PMID: 29227283, PMCID: PMC5749505, DOI: 10.1172/jci95410.Peer-Reviewed Original ResearchConceptsLinear ubiquitin chain assembly complexType II protein arginine methyltransferaseProtein arginine methyltransferase 5Protein arginine methyltransferaseTranscription factor Sox10Cyclin-dependent kinase inhibitor 2ATranscriptional corepressor SKIArginine dimethylationArginine methyltransferasePRMT5 activityAssembly complexMelanoma growthMethyltransferase activityPRMT5PRMT5 inhibitionRegulatory axisInhibitor 2ASHARPINNF-κB signalingHuman cancersMethylthioadenosine phosphorylaseMultiproteinImportant roleDimethylationMethyltransferase
2016
MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells
Kryukov GV, Wilson FH, Ruth JR, Paulk J, Tsherniak A, Marlow SE, Vazquez F, Weir BA, Fitzgerald ME, Tanaka M, Bielski CM, Scott JM, Dennis C, Cowley GS, Boehm JS, Root DE, Golub TR, Clish CB, Bradner JE, Hahn WC, Garraway LA. MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells. Science 2016, 351: 1214-1218. PMID: 26912360, PMCID: PMC4997612, DOI: 10.1126/science.aad5214.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferase 5Methylthioadenosine phosphorylaseCancer cell linesMultiple cancer lineagesPutative drug targetsCell linesTumor suppressor geneComprehensive genomic profilingCancer cell dependenciesEnzyme methylthioadenosine phosphorylaseArginine methyltransferaseCancer lineagesFunctional characterizationCancer dependenciesPRMT5 inhibitorsSuppressor geneDrug targetsTherapeutic strategiesPreferential impairmentMTAP deletionEnzymatic activityGenomic alterationsGenomic profilingCell dependencyCancer cells
2011
PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition
Liu L, Qi H, Wang J, Lin H. PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. Development 2011, 138: 1863-1873. PMID: 21447556, PMCID: PMC3074456, DOI: 10.1242/dev.059287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedArgonaute ProteinsCarrier ProteinsDEAD-box RNA HelicasesDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFemaleGene Expression Regulation, DevelopmentalGene SilencingGerm CellsMaleModels, BiologicalMutagenesis, InsertionalPeptide Initiation FactorsProtein BindingRibonucleoproteinsRNA-Binding ProteinsRNA-Induced Silencing ComplexConceptsPiRNA pathway componentsPIWI-interacting RNAsArgonaute 3PiRNA pathwayPIWI proteinsTransposon activationPathway componentsPIWI protein AubergineTudor domain proteinsP-body componentsN-terminal domainNuage componentsPiRNA mutantsTransposon controlGermline developmentTudor domainMutant ovariesArginine methyltransferaseGermline genomeEpigenetic regulationPerinuclear structuresNuageAdult ovariesArginine residuesFunctional interaction
2000
PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*
Tang J, Frankel A, Cook R, Kim S, Paik W, Williams K, Clarke S, Herschman H. PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*. Journal Of Biological Chemistry 2000, 275: 7723-7730. PMID: 10713084, DOI: 10.1074/jbc.275.11.7723.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferase activityArginine methyltransferase activityMurine tissue extractsMammalian cellsRat1 cellsMethyltransferase activityType I protein arginine methyltransferasesType I protein arginine methyltransferaseHeterogeneous nuclear ribonucleoprotein A1Protein arginine methyltransferasesProtein arginine methyltransferaseFDH activityHigh molecular weight complexesDomain fusion proteinMolecular weight complexesMethyl donor substrateDimethylarginine residuesArginine methyltransferasesArginine methyltransferaseEucaryotic proteinsPRMT1 activityDehydrogenase proteinFusion proteinEnzyme activity presentWeight complexes
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