PP2A-B72/B130 Inhibitors

PP2A-B72/B130 inhibitors belong to a class of chemical compounds that target specific protein complexes within the cell, known as PP2A-B72 and PP2A-B130. These protein complexes play a crucial role in regulating various cellular processes, primarily through their involvement in the dephosphorylation of target proteins. Dephosphorylation is a reversible post-translational modification that controls the activity and function of proteins by removing phosphate groups from specific amino acid residues. PP2A-B72 and PP2A-B130 are regulatory subunits of protein phosphatase 2A (PP2A), which is a well-known serine/threonine phosphatase enzyme found in eukaryotic cells. The inhibition of PP2A-B72/B130 has garnered significant interest in the field of cell biology and molecular pharmacology due to its potential impact on various cellular pathways and functions.

PP2A-B72/B130 inhibitors are designed to specifically disrupt the function of these regulatory subunits, leading to the dysregulation of PP2A activity. By inhibiting the binding of PP2A-B72/B130 to the catalytic subunit of PP2A, these compounds can alter the substrate specificity and substrate dephosphorylation kinetics of the PP2A enzyme. This, in turn, can have wide-ranging effects on various signaling pathways, cell cycle progression, and cellular responses to external stimuli. The detailed mechanism of action and structural features of PP2A-B72/B130 inhibitors may vary among different compounds, but their common goal is to perturb the normal regulatory role of PP2A-B72 and PP2A-B130 within the PP2A holoenzyme, thereby providing valuable tools for researchers to investigate the physiological and pathological processes in which these regulatory subunits are involved. These inhibitors have the potential to uncover new insights into cell biology and may ultimately lead to the development of novel strategies for manipulating cellular functions.