棕榈酰化
蛋白质靶向
高尔基体
生物
ADP核糖基化因子
肉豆蔻酰化
内体
细胞生物学
转运蛋白
GTP酶
蛋白质分选信号
膜蛋白
生物化学
肽序列
膜
细胞内
基因
磷酸化
酶
信号肽
半胱氨酸
内质网
作者
Juan Wang,Lang-Fan Zheng,Su Ren,Donglin Li,Chen Chen,Huihui Sun,Liying Liu,Huiling Guo,Tong‐Jin Zhao
摘要
Protein palmitoylation is a post-translational lipid modification of proteins. Accumulating evidence reveals that palmitoylation functions as a sorting signal to direct proteins to destinations; however, the sorting mechanism remains largely unknown. Here, we show that ARF6 plays a general role in targeting palmitoylated proteins from the Golgi to the plasma membrane (PM). Through shRNA screening, we identified ARF6 as the key small GTPase in targeting CD36, a palmitoylated protein, from the Golgi to the PM. We found that the N-terminal myristoylation of ARF6 is required for its binding with palmitoylated CD36, and the GTP-bound form of ARF6 facilitates the delivery of CD36 to the PM. Analysis of stable isotope labeling by amino acids in cell culture revealed that ARF6 might facilitate the sorting of 359 of the 531 palmitoylated PM proteins, indicating a general role of ARF6. Our study has thus identified a sorting mechanism for targeting palmitoylated proteins from the Golgi to the PM.
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