Tau binding protein CAPON induces tau aggregation and neurodegeneration
نویسندگان
چکیده
منابع مشابه
P 97: Neurodegeneration Induced by Tau protein
Tau is one of several types of microtubule-associated proteins (MAPs), responsible for the assembly and stability of microtubule networks that is present only in neurons and predominantly localized in axons which its functions are tightly regulated by phosphorylation. Via as yet unknown mechanisms, tau becomes hyperphosphorylated and accompanies with neuronal degeneration, loss of synapses...
متن کاملTau protein and tau aggregation inhibitors.
Alzheimer disease is characterized by pathological aggregation of two proteins, tau and Abeta-amyloid, both of which are considered to be toxic to neurons. In this review we summarize recent advances on small molecule inhibitors of protein aggregation with emphasis on tau, with activities mediated by the direct interference of self-assembly. The inhibitors can be clustered in several compound c...
متن کاملp 97: neurodegeneration induced by tau protein
tau is one of several types of microtubule-associated proteins (maps), responsible for the assembly and stability of microtubule networks that is present only in neurons and predominantly localized in axons which its functions are tightly regulated by phosphorylation. via as yet unknown mechanisms, tau becomes hyperphosphorylated and accompanies with neuronal degeneration, loss of synapses, abe...
متن کاملCoenzyme q induces tau aggregation, tau filaments, and Hirano bodies.
Tau aggregation is a common feature of tauopathies such as Alzheimer disease (AD). In AD, tau assembles into fibrillar polymers; it may also be present in other aberrant aggregates, including Hirano bodies. The mechanisms leading to tau polymerization in vivo are not understood. In this study, we found that coenzyme Q (ubiquinone) facilitates tau aggregation after binding to tau molecules at th...
متن کاملTau protein liquid–liquid phase separation can initiate tau aggregation
The transition between soluble intrinsically disordered tau protein and aggregated tau in neurofibrillary tangles in Alzheimer's disease is unknown. Here, we propose that soluble tau species can undergo liquid-liquid phase separation (LLPS) under cellular conditions and that phase-separated tau droplets can serve as an intermediate toward tau aggregate formation. We demonstrate that phosphoryla...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature Communications
سال: 2019
ISSN: 2041-1723
DOI: 10.1038/s41467-019-10278-x