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Tau protein disrupts nucleocytoplasmic transport in Alzheimer's disease

Neuron. 2018; 
BaharehEftekharzadehJ. GavinDaigleLarisa E.KapinosAlyssaCoyneJuliaSchiantarelliYariCarlomagnoCaseyCookSean J.MillerSimonDujardinAna S.AmaralJonathan C.GrimaRachel E.BennettKatharinaTepperMichaelDeTureCharles R.VanderburgBianca T.CorjucSarah L.DeVosJose AntonioGonzalez…Bradley T.Hyman
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Mutant Libraries Nup98-S and Nup62-S are full F→S mutants of Nup98-FG and Nup62-FG. The plasmid constructs were bought from GenScript, expressed and purified as previously described (Wagner et al., 2015). Nup133 was immobilized to CM5 chip using an amine coupling procedure. All proteins were dialyzed into PBS pH 7.2 prior use. The Nup98 C-terminal half, Nup98-C, and Nup133 proteins were purchased from Mybiosource. Get A Quote

摘要

Tau is the major constituent of neurofibrillary tangles in Alzheimer’s disease (AD), but the mechanism underlying tau-associated neural damage remains unclear. Here, we show that tau can directly interact with nucleoporins of the nuclear pore complex (NPC) and affect their structural and functional integrity. Pathological tau impairs nuclear import and export in tau-overexpressing transgenic mice and in human AD brain tissue. Furthermore, the nucleoporin Nup98 accumulates in the cell bodies of some tangle-bearing neurons and can facilitate tau aggregation in vitro. These data support the hypothesis that tau can directly interact with NPC components, leading to their mislocalization and consequent disr... More

关键词

Alzheimer’s diseasetauopathiesnuclear pore complexNup98nucleocytoplasmic transport