a(CHEBI:"microcystin-LR")
These findings suggest a scenario in which MC-LR-mediated demethylation of PP2Ac is associated with GSK-3β phosphorylation at Ser9 and contributes to dissociation of Bα from PP2Ac, which would result in Bα degradation and disruption of PP2A/Bα-tau interactions, thus promoting tau hyperphosphorylation and paired helical filaments-tau accumulation and, consequently, axonal degeneration and cell death. PubMed:29228318
Two potent tumor-inducing toxins, okadaic acid (OA) and microcystin-LR (MCLR), specifically inhibit PP2A PubMed:19277525
The structural feature that PME-1 binds directly to the PP2A active site, overlapping the binding sites for OA and MCLR, also explains why these phosphatase inhibitors blocked the methylesterase activity of PME-1 PubMed:19277525
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