Hyperphosphorylation of Tau in PHF

@article{Morishimakawashima1995HyperphosphorylationOT,
  title={Hyperphosphorylation of Tau in PHF},
  author={Maho Morishima-kawashima and Masato Hasegawa and Koji Takio and Masami Suzuki and Hirotaka Yoshida and Atsushi Watanabe and Koiti Titani and Yasuo Ihara},
  journal={Neurobiology of Aging},
  year={1995},
  volume={16},
  pages={365-371}
}
Tau Becomes a More Favorable Substrate for GSK-3 When It Is Prephosphorylated by PKA in Rat Brain*
TLDR
It is demonstrated for the first time that phosphorylation of tau by PKA primes it for phosphorylated by GSK-3 at the Tau-1 and the PHF-1 sites and that an associated loss in spatial memory is inhibited by inhibition of the hyperphosphorylated tau.
Dephosphorylation of Tau Protein by Calcineurin Triturated into Neural Living Cells
TLDR
Recombinant calcineurin introduced into cells that have been treated with okadaic acid and cyclosporin A, which are inhibitors of phosphatases (PP1/PP2A and PP2B), has a direct effect on the phosphorylation status on allosphorylation sites studied.
Positional effects of phosphorylation on the stability and morphology of tau-related amyloid fibrils.
TLDR
To understand the effect of phosphorylation on the fibrillation of tau, tau-derived phosphorylated peptides were utilized and possible protofilament models with four β-sheets were constructed to consider the positional effects of the serine and/or tyrosine phosphorylations.
Microtubule‐Affinity Regulating Kinase (MARK) Is Tightly Associated with Neurofibrillary Tangles in Alzheimer Brain: A Fluorescence Resonance Energy Transfer Study
TLDR
This study implicates the non-proline directed kinase MARK in PHF-tau phosphorylation, by virtue of its close intermolecular association with the phosphorylated Ser262 epitope on PHF -tau as assessed by fluorescence resonance energy transfer.
Dephosphorylation of microtubule‐associated protein tau by protein phosphatase 5
TLDR
The results suggest that PP5 plays a role in the dephosphorylation of tau and might be involved in the molecular pathogenesis of Alzheimer's disease.
Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau
TLDR
Tyr-310 phosphorylation has a unique role in the regulation of Tau aggregation, microtubule, and lipid interactions and is highlighted by NMR experiments indicated that these effects are mediated by a local decrease in β-sheet propensity of Tau's PHF6 domain.
Isomerase Pin1 Stimulates Dephosphorylation of Tau Protein at Cyclin-dependent Kinase (Cdk5)-dependent Alzheimer Phosphorylation Sites*
TLDR
Pin1 binds phospho-Tau and stimulates its dephosphorylation at Cdk5-mediated phosphorylation sites, indicating that Pin1 is generally involved in the regulation of Tau hyperphosphorlation and hence the etiology of tauopathies.
Combinatorial Tau Pseudophosphorylation
TLDR
The conventional view of combinatorial phosphorylation in normal and pathological Tau action is reassessed, with marked contrast to the expectation that doubly pseudophosphorylated Tau would be less functional than either of its corresponding singly pseudophilelated forms.
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References

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Proline-directed and Non-proline-directed Phosphorylation of PHF-tau (*)
TLDR
The abnormal phosphorylation of PHF-tau can be considered to consist of fetal typeosphorylation and additional proline-directed and non-proline- directed phosphorylated peptides.
In vivo phosphorylation sites in fetal and adult rat tau.
A68: a major subunit of paired helical filaments and derivatized forms of normal Tau.
TLDR
The major subunits of a class of PHFs are A68 proteins and the excessive or inappropriate phosphorylation of normal tau may change its apparent Mr, thus transforming tau into A68.
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