Palmitoylation of LAT contributes to its subcellular localization and stability.
Palmitoylation of LAT contributes to its subcellular localization and stability.
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DOI：
10.1016/j.bbrc.2006.01.076
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发表时间：
2006-03
影响因子：
3.1
通讯作者：
N. Tanimura;S. Saitoh;S. Kawano;A. Kosugi;K. Miyake
中科院分区：
文献类型：
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作者：
N. Tanimura;S. Saitoh;S. Kawano;A. Kosugi;K. Miyake
棕榈酰化是蛋白质转运到脂筏的修饰。在没有棕榈酰化的情况下，介导T细胞受体信号传导的接头分子T细胞活化连接子（LAT）不能定位于脂筏中并介导T细胞活化。我们在这里显示了一个新的作用棕榈酰化的LAT运输到质膜和LAT蛋白的稳定性。缺乏棕榈酰化的人LAT突变体不能运输到质膜，尽管存在跨膜部分。缺乏棕榈酰化的小鼠LAT突变体是不稳定的，容易通过蛋白酶体途径降解。当细胞外部分与小鼠的细胞外部分交换时，人LAT突变体变得不稳定，表明棕榈酰化和细胞外部分调节LAT的稳定性。这些结果表明，棕榈酰化在运输到质膜和LAT的稳定性中具有重要作用。
Palmitoylation is a protein modification for trafficking to lipid raft. Without palmitoylation, linker for activation of T cells (LAT), an adaptor molecule mediating T cell receptor signaling, is unable to localize in lipid rafts and to mediate T cell activation. We here show a novel role for palmitoylation in LAT trafficking to the plasma membrane and in the stability of the LAT protein. The human LAT mutant lacking palmitoylation was unable to traffic to the plasma membrane despite the presence of transmembrane portion. The mouse LAT mutant lacking palmitoylation was unstable and susceptible to degradation via the proteasome pathway. The human LAT mutant became unstable when the extracellular portion was swapped for that from mouse, indicating that both palmitoylation and the extracellular portion regulate the stability of LAT. These results suggest that palmitoylation has an important role in trafficking to the plasma membrane and the stability of LAT.