Abstract
Protein phosphatase 2A (PP2A) is a heterotrimeric serine/threonine phosphatase that has many inhibitory roles in cell proliferation and metastasis and promotes tumor suppressor activity. Protein methylesterase 1 (PME-1) inhibits PP2A through the removal of a methyl group from its catalytic subunit. Here, we discuss emerging reports that (1) PME-1 is over-expressed in cancer, (2) PME-1 inhibits PP2A activity and promotes cancer progression, and (3) can be chemically inhibited in vivo . We further show that PME-1 may have an important role in Wnt signaling in endometrial cancer that has yet to be fully explored and demonstrate that post-translational modifications of PP2A may play a role in PME-1 binding. Discussed within, the current literature supports continued evaluation of PME-1 as a potential therapeutic target and biomarker for cancer.
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