The PP2A subunit PR130 is a key regulator of cell development and oncogenic transformation

Dzulko, M., Pons, M., Henke, A., Schneider, G., and Kramer, O. H. (2020). Biochim Biophys Acta Rev Cancer 1874, 188453


Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase. This enzyme is involved in a plethora of cellular processes, including apoptosis, autophagy, cell proliferation, and DNA repair. Remarkably, PP2A can act as a context-dependent tumor suppressor or promoter. Active PP2A complexes consist of structural (PP2A-A), regulatory (PP2A-B), and catalytic (PP2A-C) subunits. The regulatory subunits define the substrate specificity and the subcellular localization of the holoenzyme. Here we condense the increasing evidence that the PP2A B-type subunit PR130 is a critical regulator of cell identity and oncogenic transformation. We summarize knowledge on the biological functions of PR130 in normal and transformed cells, targets of the PP2A-PR130 complex, and how diverse extra- and intracellular stimuli control the expression and activity of PR130. We additionally review the impact of PP2A-PR130 on cardiac functions, neuronal processes, and anti-viral defense and how this might affect cancer development and therapy.