Asparagine residue 368 is involved in Alzheimer's disease tau strain–specific aggregation
Shotaro Shimonaka, Shin‐ei Matsumoto, Montasir Elahi, Koichi Ishiguro, Masato Hasegawa, Nobutaka Hattori, Yumiko Motoi
Abstract
models. Furthermore, to identify the minimum sequence responsible for tau aggregation, we systematically repeated cellular tau aggregation assays for the delineation of shorter deletion sites and revealed that Asn-368 mutation suppressed tau aggregation triggered by an AD tau seed, but not using other tauopathy seeds. Our study suggested that 353-368 aa is a novel aggregation-responsible sequence other than PHF6 and PHF6*, and within this sequence, the Asn-368 residue plays a role in strain-specific tau aggregation in different tauopathies.
Topics & Concepts
TauopathyProgressive supranuclear palsyCorticobasal degenerationFibrilTau proteinMutantChemistryProtein aggregationBiochemistryNeurodegenerationBiologyBiophysicsAlzheimer's diseaseGeneticsMedicineDiseasePathologyGeneAtrophyAlzheimer's disease research and treatmentsCholinesterase and Neurodegenerative DiseasesDementia and Cognitive Impairment Research