Protein phosphatase 1A (PPM1A)

Protein phosphatase 1A (PPM1A) is a metal ion (Mg2+/Mn2+)-dependent member of the PP2C family of serine/threonine phosphatases that catalyzes the removal of phosphate groups from a wide variety of protein substrates, acting as a negative regulator of key signaling pathways. PPM1A is involved in regulation of cell cycle progression (by dephosphorylating cyclin-dependent kinases), cellular stress responses (including p38 and JNK MAPK pathways), metabolic sensing via AMPK, and transcriptional regulation via dephosphorylation of Smad3 and YAP/TAZ, among others. It also modulates NF-κB activity and can interact with various other signaling nodes. PPM1A is essential for proper cellular proliferation, apoptosis, and metabolic homeostasis and is implicated in pathologies including cancer, autoimmunity, neurodegeneration, and inflammation. While representing an emerging therapeutic target, no specific small-molecule drugs are clinically approved against PPM1A, although its modulation continues to be a research focus in oncology and regenerative medicine[1][2][3][4][5].

Other names

Protein phosphatase Mg2+/Mn2+ dependent 1APP2C-alphaPP2CAProtein phosphatase 2C isoform alphaProtein phosphatase IAphosphatase 2C alphaprotein phosphatase 2C, alpha isoformPP2C-ALPHAPP2Calphaprotein phosphatase 1APPM1APPPM1AMGC9201

Enzyme inhibition (phosphatase inhibition); Potential restoration or blockade of signaling pathways (such as Hippo/YAP, AMPK, TGF-β/Smad)