Fyn Kinase Controls Tau Aggregation In Vivo
Adam Briner, Jürgen Götz, Juan Carlos Polanco
Abstract
brain lysates elicit less tau seeding in tau biosensor cells. Lastly, the fibrillization of tau is boosted by its pseudophosphorylation at the Fyn epitope Y18. Together, this identifies Fyn as a key regulator of tau pathology independently of Aβ-induced toxicity and thereby represents a potentially valuable therapeutic target for not only AD but also tauopathies more generally.
Topics & Concepts
FYNTau proteinCell biologyChemistryTauopathyHyperphosphorylationNeurodegenerationKinaseAlzheimer's diseaseBiologyNeurosciencePathologyMedicineDiseaseProto-oncogene tyrosine-protein kinase SrcAlzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsBioinformatics and Genomic Networks