Poul Henning Jensen, Denmark

Aarhus University DANDRITE, Biomedicine

Author Of 1 Presentation

PKR KINASE DIRECTLY REGULATES TAU EXPRESSION AND ALZHEIMER'S DISEASE-RELATED TAU PHOSPHORYLATION

Session Name
Session Type
SYMPOSIUM
Date
13.03.2021, Saturday
Session Time
10:00 - 11:45
Room
On Demand Symposia B
Lecture Time
10:45 - 11:00
Session Icon
On-Demand

Abstract

Aims

Deposition of extensively hyperphosphorylated tau in specific brain cells is a clear pathological hallmark in Alzheimer’s disease and other tauopathies. Furthermore, the well-established “tau hypothesis” postulate that hyperphosphorylation of tau abolishes its microtubule-stabilizing role, and leaves it vulnerable to self-assembly, thereby promoting neuronal dysfunction and death. This suggests a central role of hyperphosphorylation in tauopathies, but so far no disease-causing kinase has been identified. Here we investigate the relationship between acute encephalitis, activation of the inflammation/infection-activated kinase, PKR, and pathological tau phosphorylation.

Methods

PKRs role in tau phosphorylation was assessed via in vitro phosphorylation assays, cellular overexpression of constitutively active PKR, and PKR inhibition in rTg4510 mice brain slices, using specific phospho-tau antibodies. qPCR and microtubule-binding assays were also performed. Finally, to induce acute encephalopathy, robust inflammation, and PKR upregulation, Langat virus was intracranial injected in wild-type mice.

Results

We observe that PKR directly phosphorylates numerous abnormal and disease-modifying residues within tau including Thr181, Ser199/202, Thr231, Ser262, Ser396, Ser404 and Ser409. Similar, we find that these phosphorylations actively displace cellular tau from microtubules. In addition, PKR overexpression and knockdown, respectively, increase and decrease tau protein and mRNA levels in cells. Finally, acute encephalopathy induces robust inflammation and PKR upregulation, accompanied by abnormally phosphorylated full-length- and truncated tau.

Conclusions

These findings indicate that PKR, independent of other kinases, and upon acute brain inflammation, capably trigger pathological modulation of tau, which in turn, might form the initial pathologic seed in several tauopathies such as Alzheimer’s disease and Chronic traumatic encephalopathy where inflammation is severe.

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