ArticleFrontiers in drug discovery2024
A Small Molecule Inhibitor of Leucine Carboxyl Methyltransferase-1 Inhibits Cancer Cell Survival.
Article in Frontiers in drug discovery, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Reversible phosphorylation is the basis for signal transduction in eukaryotic cells, and this is tightly controlled by the complex interplay of kinases and phosphatases. Many malignancies are characterized by dysregulation of the delicate protein phosphorylation balance. The targeting of protein phosphatases has been gaining attention as their role in cancer development and progression has been elucidated. The protein phosphatase-2A (PP2A) family of phosphatases are the primary cellular serine/threonine phosphatases. PP2A heterotrimers containing the B55α (PR55α) regulatory subunit have been associated with oncogenic signaling, and B55 subunits are found exclusively in forms of PP2A in which the carboxyl terminus of the catalytic subunit (PP2Ac) is methylated. Methylation of PP2Ac is primarily mediated by leucine carboxyl methyltransferase-1 (LCMT-1). Demethylation is controlled by an esterase, PP2A methylesterase (PME-1). We tested two potential LCMT-1 small molecule inhibitors and found that methyl 4-methyl-2-[(2-methylbenzoyl)amino]-5-[[(3-methylphenyl)amino]carbonyl]-3-thiophenecarboxylate (henceforth referred to as Compound 2) significantly inhibited PP2Ac methylation
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