Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling

Description

S-palmitoylation is a lipid modification which regulates membrane-protein association and influences protein trafficking, stability or aggregation, thus playing an important role in protein signalling. We previously demonstrated that the palmitoylation of Fas, one of the death-domain (DD)-containing members of the tumor necrosis factor receptors (TNFR) super family, is essential for the redistribution of this receptor into lipid rafts, an obligatory step for the death signal transmission. Here we investigate the requirement of protein palmitoylation in the activities of other DD-containing death receptors. We show that whereas DR4 is palmitoylated, DR5 and TNFR1 are not. Furthermore, DR4 palmitoylation is required for its raft localization and its ability to oligomerize, two essential features in TRAIL induced-death signal transmission.

Abstract

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