4.6 Review

Tau, tau kinases, and tauopathies: An updated overview

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Summary: Tau protein can form hyperphosphorylated aggregates in neurodegenerative diseases like Alzheimer's, and phosphorylation of tau by cAMP-dependent protein kinase A (PKA) at Ser214 reduces its pathological assembly. The activation of adenylyl cyclase increases pTAU-S214 levels in N2a cells and rat hippocampal slices, and this effect is mimicked by GEBR-7b, a phosphodiesterase 4D inhibitor.

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Protein kinase G phosphorylates the Alzheimer's disease-associated tau protein at distinct Ser/Thr sites

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Summary: Phosphorylation is a key mechanism in regulating tau protein in neurodegenerative diseases, and the PKG protein kinase can phosphorylate tau at the Ser214 site, potentially reducing the pathological aggregation of tau protein, shifting it from a pro-aggregant to a neuroprotective conformation.

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The Microtubule-Associated Protein Tau is Also Phosphorylated on Tyrosine

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Phosphorylated Tau Interacts with c-Jun N-terminal Kinase-interacting Protein 1 (JIP1) in Alzheimer Disease

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Tau suppression in a neurodegenerative mouse model improves memory function

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Glycogen synthase kinase 3β induces caspase-cleaved tau aggregation in situ

JH Cho et al.

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Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK)

H Yoshida et al.

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Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

AD Alonso et al.

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XW Zhu et al.

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Tau protein isoforms, phosphorylation and role in neurodegenerative disorders

L Buée et al.

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Role of phosphorylation in the conformation of τ peptides implicated in Alzheimer's disease

NL Daly et al.

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