Protein phosphatase 1 and protein phosphatase 2A (PP1 and PP2A)

Protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) are the most abundant and ubiquitous serine/threonine phosphatases in eukaryotic cells. Both enzymes are responsible for the majority of dephosphorylation of phosphoserine and phosphothreonine residues in a vast array of cellular proteins, making them crucial regulators of nearly all cellular processes, including signal transduction, the cell cycle, apoptosis, stress responses, transcription, glycogen metabolism, and more. Their enzymatic specificity and activity are achieved through assembly into multimeric holoenzymes that include various regulatory subunits, defining substrate preference and subcellular localization. Dysfunction or chemical inhibition of PP1 or PP2A has wide-ranging implications in human diseases, especially cancer, neurodegenerative and cardiovascular diseases, and is a significant therapeutic challenge due to their global regulatory roles.

Other names

PP1 (Protein phosphatase 1)PP2A (Protein phosphatase 2A)Serine/threonine protein phosphatase 1Serine/threonine protein phosphatase 2APPP1PPP2A

Direct inhibition of the phosphatase catalytic subunit Disruption/modulation of enzyme-substrate recognition and dephosphorylation activity Modulation via regulatory subunit binding