PEBP1 binds to phosphatidylethanolamine, a type of phospholipid found in biological membranes. It also has the ability to bind ATP and opioids, although with lower affinity for phosphatidylinositol and phosphatidylcholine . PEBP1 acts as a serine protease inhibitor, inhibiting enzymes such as thrombin, neuropsin, and chymotrypsin, but not trypsin, tissue-type plasminogen activator, and elastase .
One of the key functions of PEBP1 is its role as an inhibitor of the kinase activity of RAF1. It achieves this by inhibiting RAF1’s activation and dissociating the RAF1/MEK complex, acting as a competitive inhibitor of MEK phosphorylation . This inhibition is crucial in regulating the MAPK signaling pathway, which is involved in cell growth, differentiation, and apoptosis.
PEBP1 has been implicated in numerous human cancers and may act as a metastasis suppressor gene . Its ability to modulate key signaling pathways makes it a potential target for cancer therapy. Additionally, PEBP1 has been proposed as a biomarker for Alzheimer’s disease due to its involvement in neural development and its specific binding to phosphatidylethanolamine .
Recombinant PEBP1 is produced using recombinant DNA technology, which involves inserting the gene encoding PEBP1 into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications, including studying its structure and function, as well as its role in disease processes.