Protein phosphatase 2A catalytic subunit (PP2A-C)

Protein phosphatase 2A catalytic subunit (PP2A-C) is the core enzymatic subunit of protein phosphatase 2A, a major serine/threonine phosphatase in eukaryotic cells responsible for the dephosphorylation of a wide spectrum of signaling proteins, including key regulators such as Akt, p53, c-Myc, β-catenin, Raf, MEK, and AKT[1][3]. PP2A typically functions as a heterotrimeric complex consisting of a catalytic subunit (C, encoded by the PPP2CA and PPP2CB genes), a scaffold subunit (A), and a variable regulatory subunit (B) which determines substrate specificity[1][3]. PP2A is considered a tumor suppressor due to its role in constraining many oncogenic pathways; its inactivation—commonly observed in diverse cancers and some neurodegenerative disorders—contributes to unregulated cell growth and survival[2][4][6][7]. Restoration or activation of PP2A activity is an emerging therapeutic strategy in oncology and inflammatory disease, but the enzyme’s complex regulation and tissue ubiquity present major therapeutic challenges[1][4][6]. PP2A is also implicated in cell cycle control, apoptosis, signal transduction, and maintenance of genomic stability[3][6][7]. Drugs targeting PP2A include activators (PP2A-activating drugs, such as FTY720 and rubratoxin) and inhibitors (such as fostriecin and cantharidin, mainly as research tools)[1][4][6]. Safety concerns include the risk of broad disruption to essential signaling in normal cells due to the widespread and critical functions of this enzyme[1][6].

Other names

PP2A catalytic subunitPP2ACPPP2CA (gene)PPP2CB (gene)Protein phosphatase 2A C subunit

Activation (reactivation) of tumor suppressor function, Inhibition of oncogenic phosphatase inhibition, Selective PP2A subunit targeting, Dephosphorylation of oncogenic kinases and regulators