Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function
Ko HS, Lee Y, Shin JH, Karuppagounder SS, Gadad BS, Koleske AJ, Pletnikova O, Troncoso JC, Dawson VL, Dawson TM. Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 16691-16696. PMID: 20823226, PMCID: PMC2944759, DOI: 10.1073/pnas.1006083107.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCell DeathCell LineDopamineGene Knockout TechniquesHumansIn Vitro TechniquesMiceMice, KnockoutMolecular Sequence DataMutationNeuronsParkinson DiseasePC12 CellsPhosphorylationProto-Oncogene Proteins c-ablRatsRecombinant Fusion ProteinsStress, PhysiologicalUbiquitinationUbiquitin-Protein LigasesConceptsParkinson's diseaseTreatment of PDSTI-571Postmortem PD brainsSporadic Parkinson's diseaseC-AblProtective functionNonreceptor tyrosine kinase c-AblMPTP intoxicationUbiquitin E3 ligase activityNeuroprotective approachesPD brainsSubstantia nigraDopaminergic neurotoxinProtective effectProtein type 2Subsequent neurotoxicityNervous systemType 2Parkin inactivationAutosomal recessive Parkinson's diseaseConditional knockoutKinase inhibitorsRecessive Parkinson's diseaseTyrosine kinase c-Abl