Posttranslational cleavage of cell‐surface receptors

Abstract Nascent polypeptides generated by eukaryotes rarely represent the true form of mature proteins. Instead, many newly synthesized proteins undergo posttranslational modifications that may mediate either subtle or profound effects on the function of the protein. In this review, we focus on proteolytic cleavage as a type of irreversible posttranslational modification. We describe the different proteolytic mechanisms of three disparate families of cell‐surface receptors; Notch receptors, protease‐activated receptors (PARs) and G‐protein receptor proteolytic site (GPS) containing receptors. All of these exemplify how posttranslational modification by proteolysis can greatly affect receptor function through a variety of intriguing mechanisms.