Rossin Aurélie, Derouet Mathieu, Abdel-Sater Fadi, Hueber Anne-Odile
CNRS UMR 6543, Université de Nice Sophia-Antipolis, Institute of Developmental Biology and Cancer Research, Nice, France.
Biochem J. 2009 Apr 1;419(1):185-92, 2 p following 192. doi: 10.1042/BJ20081212.
S-palmitoylation is a lipid modification that 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 DD (death domain)-containing members of the TNFR [TNF (tumour necrosis factor) receptor] superfamily, 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 DR4 is palmitoylated, whereas DR5 and TNFR1 are not. Furthermore, DR4 palmitoylation is required for its raft localization and its ability to oligomerize, two essential features in TRAIL (TNF-related apoptosis-inducing ligand)-induced death signal transmission.
S-棕榈酰化是一种脂质修饰，它调节膜蛋白结合，并影响蛋白质运输、稳定性或聚集，因此在蛋白质信号传导中发挥重要作用。我们之前证明，Fas（TNFR [肿瘤坏死因子受体] 超家族中含死亡结构域的成员之一）的棕榈酰化对于该受体重新分布到脂筏中至关重要，而这是死亡信号传递的一个必要步骤。在此，我们研究了蛋白质棕榈酰化在其他含死亡结构域的死亡受体活性中的需求。我们发现DR4被棕榈酰化，而DR5和TNFR1未被棕榈酰化。此外，DR4的棕榈酰化是其定位于脂筏及其寡聚化能力所必需的，而这是TRAIL（肿瘤坏死因子相关凋亡诱导配体）诱导的死亡信号传导中的两个基本特征。
