<i>In vitro</i> reconstitution of Wnt acylation reveals structural determinants of substrate recognition by the acyltransferase human Porcupine.

ABSTRACT: Wnt proteins regulate a large number of processes, including cellular growth, differentiation, and tissue homeostasis, through the highly conserved Wnt signaling pathway in metazoans. Porcupine (PORCN) is an endoplasmic reticulum (ER)-resident integral membrane enzyme that catalyzes posttranslational modification of Wnts with palmitoleic acid, an unsaturated lipid. This unique form of lipidation with palmitoleic acid is a vital step in the biogenesis and secretion of Wnt, and PORCN inhibitors are currently in clinical trials for cancer treatment. However, PORCN-mediated Wnt lipidation has not been reconstituted in vitro with purified enzyme. Here, we report the first successful purification of human PORCN and confirm, through in vitro reconstitution with the purified enzyme,

SUBMITTER: Lee CJ 

PROVIDER: S-EPMC6322882 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature