Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae
Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae
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DOI：
10.1074/jbc.275.3.2057
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发表时间：
2000-01-21
影响因子：
4.8
通讯作者：
Robson, SC
中科院分区：
文献类型：
--
作者：
Koziak, K;Kaczmarek, E;Robson, SC
外核苷酸酶通过水解细胞外核苷酸影响嘌呤能受体功能，CD 39是一种整合的膜蛋白，是核苷5 '-三磷酸二磷酸水解酶家族的原型成员。天然CD 39蛋白具有两个胞质内结构域和两个跨膜结构域。有一个大的细胞外结构域，经历广泛的糖基化，可以通过有限的蛋白水解后修饰，我们已经确定了一个潜在的硫酯连接位点的N-末端区域内的CD 39的S-酰化，并证明该区域经历棕榈酰化的组成方式。蛋白质的该区域的共价脂质修饰似乎在质膜缔合和靶向CD 39至小窝中都是重要的。这些专门的质膜结构域富含G蛋白偶联受体，似乎整合细胞活化事件。我们认为棕榈酰化可以调节CD 39在调节细胞信号转导通路中的功能。
Ectonucleotidases influence purinergic receptor function by the hydrolysis of extracellular nucleotides, CD39 is an integral membrane protein that is a prototype member of the nucleoside 5'-triphosphate diphosphohydrolase family. The native CD39 protein has two intracytoplasmic and two transmembrane domains. There is a large extracellular domain that undergoes extensive glycosylation and can be post-translationally modified by limited proteolysis, We have identified a potential thioester linkage site for S-acylation within the N-terminal region of CD39 and demonstrate that this region undergoes palmitoylation in a constitutive manner. The covalent lipid modification of this region of the protein appears to be important both in plasma membrane association and in targeting CD39 to caveolae. These specialized plasmalemmal domains are enriched in G protein-coupled receptors and appear to integrate cellular activation events. We suggest that palmitoylation could modulate the function of CD39 in regulating cellular signal transduction pathways.