PPP2R3A Inhibitors

PPP2R3A inhibitors primarily target the broader enzymatic complex of PP2A, affecting its activity and thereby influencing various cellular processes. Compounds like Cantharidin and Okadaic acid are classic inhibitors of PP2A, disrupting the dephosphorylation of serine/threonine residues in proteins. Tautomycin, much like Okadaic acid, obstructs PP2A activity, as do Rubratoxin A and LB-100. These chemicals, while varied in origin and structure, all contribute to a shift in the phosphorylation dynamics within cells, resulting in alterations in signal transduction, cell cycle regulation, and even apoptosis.

Moreover, Fostriecin, Calyculin A, and Endothall also serve as inhibitors, further expanding the array of compounds that modulate PP2A and, by extension, PPP2R3A's function. Interestingly, while CIP2A itself is a protein, chemical mimetics or compounds that act similarly can be impactful. Norcantharidin, found in Cantharidin, offers a slightly modified approach with similar inhibitory action. The inclusion of Enzyme System II and Perphenazine illustrates the diversity of molecules capable of PP2A inhibition.