Protein phosphatase 1 regulatory inhibitor subunit 14C (PPP1R14C)

Protein phosphatase 1 regulatory inhibitor subunit 14C (PPP1R14C) is a protein that acts as a high-affinity inhibitor of protein phosphatase 1 (PP1), especially the catalytic subunit PPP1CA, by binding in a phosphorylation-dependent manner. Upon phosphorylation, particularly at threonine 72, PPP1R14C becomes over 600-fold more potent as an inhibitor, functioning as a molecular switch to regulate phosphorylation states of target proteins in cellular signaling. Biological roles attributed to PPP1R14C include regulation of signaling cascades essential for neuronal activity, metabolism, contraction, cell division, and its potential involvement in cancer and thyroid disorders. The protein is related to other PP1 regulatory inhibitors (such as CPI17 and PPP1R14B) and may be detected serologically in certain breast cancers as antigen NY-BR-81, implicating a possible role as a tumor biomarker[1][2][3][4][5][6].

Other names

CPI17-likeKEPIkinase C-enhanced PP1 inhibitorPKC-potentiated PP1 inhibitory proteinserologically defined breast cancer antigen NY-BR-81protein phosphatase 1 regulatory inhibitor subunit 14Cprotein phosphatase 1, regulatory (inhibitor) subunit 14cNY-BR-816330514J04RikLOC100044150

Inhibition of protein phosphatase 1 (PP1) through phosphorylation-dependent binding to PP1 catalytic subunits, particularly PPP1CA