PP2A-B56-α Inhibitors

PP2A-B56-α inhibitors constitute a diverse class of chemicals designed to modulate the activity of the PP2A-B56-α subunit, a crucial regulatory component of the PP2A phosphatase complex. Among the selected inhibitors, LB-100, Cantharidin, Okadaic Acid, OA-NO2, Perphenazine, LB-102, LB-301, Endosidin 2, SMAPs, C31, LC-2, and Etoposide demonstrate varying mechanisms of action, influencing the phosphatase activity of PP2A-B56-α. LB-100, a potent and selective PP2A inhibitor, directly binds to the PP2A-B56-α subunit, hindering its phosphatase activity. This direct inhibition disrupts dephosphorylation events mediated by PP2A-B56-α, leading to modulation of various cellular processes and signaling pathways. Cantharidin, a natural compound, acts as a direct inhibitor by specifically targeting the PP2A-B56-α subunit and impairing its phosphatase function. This direct inhibition alters the dephosphorylation landscape regulated by PP2A-B56-α, affecting downstream signaling pathways and cellular responses. Okadaic Acid and its derivative OA-NO2 serve as potent direct inhibitors by binding to the PP2A-B56-α subunit and disrupting its phosphatase activity. These compounds modulate PP2A-B56-α-mediated dephosphorylation events, influencing various cellular processes.

LB-102 and LB-301, derivatives of LB-100, act as direct inhibitors by specifically binding to the PP2A-B56-α subunit. Their direct inhibition modulates PP2A-B56-α-mediated dephosphorylation events, impacting downstream signaling pathways. Endosidin 2, a small molecule, interferes with PP2A-B56-α activity as a direct inhibitor, disrupting its phosphatase function and influencing cellular responses. SMAPs, while not direct inhibitors, enhance the phosphatase activity of PP2A-B56-α, representing an alternative strategy for impacting its activity. C31 and LC-2 are direct inhibitors that specifically target the PP2A-B56-α subunit, disrupting its phosphatase function. This direct inhibition modulates PP2A-B56-α-mediated dephosphorylation events, influencing various cellular processes and signaling pathways. Etoposide, a topoisomerase II inhibitor, exhibits secondary PP2A inhibitory effects by directly targeting the PP2A-B56-α subunit. This direct inhibition alters the dephosphorylation landscape regulated by PP2A-B56-α, affecting downstream signaling pathways and cellular responses.