Evidences complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) to p(HGNC:PPME1)

Thus, PME-1 appears to exist in an inactive conformation in the absence of PP2A binding.

Structural analysis of the heterotrimeric PME-1-PP2A complex showed that PME-1 is only activated upon binding to PP2A (Figure 4, left panel).

Interestingly, although PME-1 is activated by PP2A binding, the catalytic subunit of PP2A is inactivated in this process, not just through demethylation but also by loss of the catalytic metal ions

A portion of cellular PP2A stably associated with PME-1 and was catalytically inactive [80]; intriguingly, this inactive portion of PP2A could be re-activated by PP2A phosphatase activator (PTPA), but not by LCMT1, ruling out the possibility that inactivation was solely caused by demethylation

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

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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.