EC Number   |
General Information |
Reference |
|---|
   2.7.11.26 | evolution |
sequence comparisons of diverse protein kinases, phylogenetic tree of tau protein kinases and analysis |
740531 |
| 2.7.11.26 | evolution |
TTBK2 is a serine/threonine protein kinase of the CK1 superfamily |
740135 |
| 2.7.11.26 | malfunction |
abnormal tau phosphorylation (p-tau) occurs after hypoxic damage to the brain associated with traumatic brain injury and stroke |
-, 740410 |
| 2.7.11.26 | malfunction |
AMPK inhibition leads to a rapid decrease of tau phosphorylation. AMP-activated protein kinase (AMPK) is deregulated in the Alzheimer's disease brain where it co-localized with phosphorylated tau in pre-tangle and tangle bearing neurons. AMPK mice deficient for one of the catalytic alpha subunits display reduced endogenous tau phosphorylation. AMPK deficiency reduces tau pathology in the PS19 mouse model of tauopathy |
-, 741419 |
| 2.7.11.26 | malfunction |
chronic inhibition of GSK-3 enhances glycolysis |
704555 |
| 2.7.11.26 | malfunction |
comparison of phosphorylation sites in human Alzheimer and control brain with recombinant tau phosphorylated by GSK-3 in vitro, several sites are not phosphrylated in Alzheimer's disease samples, overview. Inhibiting GSK-3 with SB-415286 also protects cultured neurons from cell death induced by reduced phosphatidylinositol 3-kinase activity, and this protection is paralleled by decreased tau phosphorylation |
740530 |
| 2.7.11.26 | malfunction |
deletion of the C-terminus alphaDELTACT-4 leads to loss of nearly all activity of the GSK-3 isoform and abolishes suppression of Wnt signaling, GSK-3 C-terminal deletions mutants fail to interact with axin GID |
740691 |
| 2.7.11.26 | malfunction |
deletion of the C-terminus betaDELTACT-4 leads to loss of nearly all activity of the GSK-3 isoform and abolishes suppression of Wnt signaling, GSK-3 C-terminal deletions mutants fail to interact with axin GID |
740691 |
| 2.7.11.26 | malfunction |
disrupting expression of isoform TTBK-d results in loss of spermatozoa, but not spermatids. In the soma, isoform TTBK-d RNAi impairs the function of multiciliated epidermal cells in propelling planarian movement, as well as the osmoregulatory function of protonephridia. Decreased density and structural defects of motile cilia are observed in the epidermis |
761870 |
| 2.7.11.26 | malfunction |
functional status of glycogen synthase kinase-3 and correlated appearance of distinct tau phospho-epitopes: neurons displaying increases in activation of phosphorylation of glycogen synthase kinase-3alpha/beta at tyrosine 279/216 also show an intense rather than moderate AT8 (phospho-Ser202/Thr205 tau) immunoreactivity, and immunoreactivity for AT100 (phospho-Ser212/Thr214 tau) and phosphorylated Ser422, phospho-epitopes associated with fibrillar tau pathology. These neurons are rare in 8.5-month-old, but numerous in 18.5- and 28-month-old pR5 mice. Tau- rather than an amyloid-beta peptide-induced pathology is associated with increased neuronal tyrosine phosphorylation. Tyrosine phosphorylation only increases in neurons with fibrillar tau pathology |
-, 741065 |
