The direct and indirect effects of α-synuclein on microtubule stability in the pathogenesis of Parkinson’s disease

References

• CartelliDCappellettiGMicrotubule destabilization paves the way to Parkinson’s diseaseMol Neurobiol20165496762677427757833
   PubMed Web of Science ®Google Scholar
• SingletonABFarrerMJohnsonJalpha-Synuclein locus triplication causes Parkinson’s diseaseScience2003302564684114593171
   PubMed Web of Science ®Google Scholar
• ZhouRHuangYLiXMolecular interaction of α-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cellsMol Biol Rep20093773183319219826908
   PubMed Web of Science ®Google Scholar
• ProtsIVeberVBreySα-Synuclein oligomers impair neuronal microtubule-kinesin interplayJ Biol Chem201328830217422175423744071
   PubMed Web of Science ®Google Scholar
• LeeHKhoshaghidehFLeeSLeeSImpairment of microtubule-dependent trafficking by overexpression of α-synucleinEur J Neurosci200624113153316217156376
   PubMed Web of Science ®Google Scholar
• Volpicelli-DaleyLGambleKSchultheissCRiddleDWestALeeVFormation of -synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomesMol Biol Cell201425254010402325298402
   PubMed Web of Science ®Google Scholar
• AlimMHossainMArimaKTubulin seeds α-synuclein fibril formationJ Biol Chem200127732112211711698390
   PubMed Web of Science ®Google Scholar
• ChenLJinJDavisJOligomeric α-synuclein inhibits tubulin polymerizationBiochem Biophys Res Commun2007356354855317374364
   PubMed Web of Science ®Google Scholar
• CartelliDAlivertiABarbiroliAα-Synuclein is a Novel Micro-tubule DynamaseSci Rep201663328927628239
   PubMed Web of Science ®Google Scholar
• VosselKAXuJCFomenkoVTau reduction prevents Aß-induced axonal transport deficits by blocking activation of GSK3ßJ Cell Biol201511209 (3):419–433.
   Google Scholar
• GeddesJα-Synuclein: a potent inducer of tau pathologyExp Neurol2005192224425015755542
   PubMed Web of Science ®Google Scholar
• Volpicelli-DaleyLEffects of α-synuclein on axonal transportNeurobiol Dis201710532132727956085
   PubMed Web of Science ®Google Scholar
• IshizawaTMattilaPDaviesPWangDDicksonDColocalization of tau and alpha-synuclein epitopes in Lewy bodiesJ Neuropathol Exp Neurol200362438939712722831
   PubMed Web of Science ®Google Scholar
• JensenPHagerHNielsenMHøjrupPGliemannJJakesRα-Synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356J Biol Chem199927436254812548910464279
   PubMed Web of Science ®Google Scholar
• WischikCNovakMEdwardsPKlugATichelaarWCrowtherRStructural characterization of the core of the paired helical filament of Alzheimer diseaseProc Natl Acad Sci U S A19888513488448882455299
   PubMed Web of Science ®Google Scholar
• KadavathHHofeleRBiernatJTau stabilizes microtubules by binding at the interface between tubulin heterodimersProc Natl Acad Sci U S A2015112247501750626034266
   PubMed Web of Science ®Google Scholar
• MukraschMBiernatJvon BergenMGriesingerCMandelkowEZweckstetterMSites of tau important for aggregation populate β-structure and bind to microtubules and polyanionsJ Biol Chem200528026249782498615855160
   PubMed Web of Science ®Google Scholar
• Morishima-KawashimaMHasegawaMTakioKProline-directed and non-proline-directed phosphorylation of PHF-tauJ Biol Chem199527028238297822317
   PubMed Web of Science ®Google Scholar
• HaggertyTCredleJRodriguezOHyperphosphorylated Tau in an α-synuclein-overexpressing transgenic model of Parkinson’s diseaseEur J Neurosci20113391598161021453448
   PubMed Web of Science ®Google Scholar
• BiernatJGustkeNDrewesGMandelkowEMandelkowEPhosphorylation of Ser262 strongly reduces binding of tau to microtu-bules: distinction between PHF-like immunoreactivity and microtubule bindingNeuron19931111531638393323
   PubMed Web of Science ®Google Scholar
• DukaTDukaVJoyceJSidhuAα-Synuclein contributes to GSK-3β-catalyzed Tau phosphorylation in Parkinson’s disease modelsFASEB J20092392820283019369384
   PubMed Web of Science ®Google Scholar
• GąssowskaMCzapskiGPająkBCieślikMLenkiewiczAAdamczykAExtracellular α-synuclein leads to microtubule destabilization via GSK-3β-dependent tau phosphorylation in PC12 cellsPLoS One201494e9425924722055
   PubMed Web of Science ®Google Scholar
• HongoHKiharaTKumeTGlycogen synthase kinase-3β activation mediates rotenone-induced cytotoxicity with the involvement of microtubule destabilizationBiochem Biophys Res Commun20124261949922922102
   PubMed Web of Science ®Google Scholar
• QureshiHPaudelHParkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-synuclein mutations promote tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitroJ Biol Chem201028675055506821127069
   PubMed Web of Science ®Google Scholar
• GiassonBInitiation and synergistic fibrillization of tau and alpha-synucleinScience2003300561963664012714745
   PubMed Web of Science ®Google Scholar
• MorrisMMaedaSVosselKMuckeLThe many faces of tauNeuron201170341042621555069
   PubMed Web of Science ®Google Scholar
• CashAAlievGSiedlakSMicrotubule reduction in Alzheimer’s disease and aging is independent of τ filament formationAm J Pathol200316251623162712707046
   PubMed Web of Science ®Google Scholar
• LiBChohanMGrundke-IqbalIIqbalKDisruption of microtubule network by Alzheimer abnormally hyperphosphorylated tauActa Neuropathol2007113550151117372746
   PubMed Web of Science ®Google Scholar
• LiuFLiBTungEGrundke-IqbalIIqbalKGongCSite-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregationEur J Neurosci200726123429343618052981
   PubMed Web of Science ®Google Scholar
• RoyBJacksonGInteractions between Tau and α-synuclein augment neurotoxicity in a Drosophila model of Parkinson’s diseaseHum Mol Genet201423113008302324430504
   PubMed Web of Science ®Google Scholar
• StokinGGoldsteinLAxonal transport and Alzheimer’s diseaseAnnu Rev Biochemistry2006751607627
   Web of Science ®Google Scholar
• del SerTLovestoneSBoada-RoviraMA phase II randomized, double-blind, parallel group, 26-week study of GSK-3 inhibitor tideglusib in Alzheimer’s disease (ARGO trial)Alzheimer’s & Dementia201394P689P690
   Google Scholar
• Morales-GarciaJPalomoVRedondoMCrosstalk between phosphodiesterase 7 and glycogen synthase kinase-3: two relevant therapeutic targets for neurological disordersACS Chem Neurosci20145319420424437940
   PubMed Web of Science ®Google Scholar
• Villar-PiquéALopes da FonsecaTOuteiroTStructure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathiesJ Neurochem201513924025526190401
   PubMed Web of Science ®Google Scholar
• CartelliDCasagrandeFBuscetiCMicrotubule alterations occur early in experimental parkinsonism and the microtubule stabilizer epothilone D is neuroprotectiveSci Rep20133183723670541
   PubMed Web of Science ®Google Scholar
• GuoJCovellDDanielsJDistinct α-Synuclein Strains Differentially Promote Tau Inclusions in NeuronsCell2013154110311723827677
   PubMed Web of Science ®Google Scholar
• LashuelHOverkCOueslatiAMasliahEThe many faces of α-synuclein: from structure and toxicity to therapeutic targetNat Rev Neurosci2013141384823254192
   PubMed Web of Science ®Google Scholar
• DopplerKEbertSÜçeylerNCutaneous neuropathy in Parkinson’s disease: a window into brain pathologyActa Neuropathol201412819910924788821
   PubMed Web of Science ®Google Scholar
• DonadioVIncensiAPiccininiCSkin nerve misfolded α-synuclein in pure autonomic failure and Parkinson diseaseAnn Neurol201679230631626606657
   PubMed Web of Science ®Google Scholar