p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205))
However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945
However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945
Trans- genic mice with reduced PP2A activity show increased tau phosphorylation at Ser202/Thr205 and Ser42 [46]. PubMed:22299660
Immunocytological analysis with AT8 antibody against phosphorylated Tau (Ser202/Thr205) demonstrated that Otub1 expression drastically increased phospho-Tau (p-Tau Ser202/Thr205) in primary neurons compared with GFP expression (Fig. 3a). PubMed:28083634
Biochemical analysis confirmed a sharp increase of phosphorylated Tau at Ser202/Thr205 in Otub1-infected primary neurons (Fig. 3b). PubMed:28083634
AAV-driven expression of Otub1-C91A did not increase AT8-positive Tau, in contrast to expression of wild-type Otub1 and the N-terminally truncated form of Otub1. This was demonstrated by immunofluorescence staining (Fig. 6a) and confirmed by biochemical analysis (Fig. 6b). PubMed:28083634
AAV-driven expression of Otub1-C91A did not increase AT8-positive Tau, in contrast to expression of wild-type Otub1 and the N-terminally truncated form of Otub1. This was demonstrated by immunofluorescence staining (Fig. 6a) and confirmed by biochemical analysis (Fig. 6b). PubMed:28083634
AAV-driven expression of Otub1-C91A did not increase AT8-positive Tau, in contrast to expression of wild-type Otub1 and the N-terminally truncated form of Otub1. This was demonstrated by immunofluorescence staining (Fig. 6a) and confirmed by biochemical analysis (Fig. 6b). PubMed:28083634
Moreover, NF-κB – induced IL1 genesis has been shown to precipitate tau phosphorylation at Ser202 and Thr205 (AT8 epitopes) via the activation of the p38- MAPK pathway PubMed:28745240
Moreover, NF-κB – induced IL1 genesis has been shown to precipitate tau phosphorylation at Ser202 and Thr205 (AT8 epitopes) via the activation of the p38- MAPK pathway PubMed:28745240
Furthermore, NF-κB - induced IL6 has been demonstrated to evoke hyperphosphorylation of tau at Ser202 and Thr205 via the activation of the cdk5/p35 complex PubMed:28745240
Furthermore, NF-κB - induced IL6 has been demonstrated to evoke hyperphosphorylation of tau at Ser202 and Thr205 via the activation of the cdk5/p35 complex PubMed:28745240
Furthermore, NF-κB - induced IL6 has been demonstrated to evoke hyperphosphorylation of tau at Ser202 and Thr205 via the activation of the cdk5/p35 complex PubMed:28745240
Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931
Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931
In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931
When combined with ERK2 catalyzed phosphorylation, the turn-like disrupting G207V mutation in TauF8 hence leads to fast aggregation that already occurs during the phosphorylation reaction. PubMed:28784767
However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945
In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.