Molecular Cancer Research Group, Department of Medical Biology, University of Tromsø - The Arctic University of Norway, Tromsø, Norway.
J Cell Biol. 2021 Jun 7;220(6). doi: 10.1083/jcb.202006128.
The Golgi complex is essential for the processing, sorting, and trafficking of newly synthesized proteins and lipids. Golgi turnover is regulated to meet different cellular physiological demands. The role of autophagy in the turnover of Golgi, however, has not been clarified. Here we show that CALCOCO1 binds the Golgi-resident palmitoyltransferase ZDHHC17 to facilitate Golgi degradation by autophagy during starvation. Depletion of CALCOCO1 in cells causes expansion of the Golgi and accumulation of its structural and membrane proteins. ZDHHC17 itself is degraded by autophagy together with other Golgi membrane proteins such as TMEM165. Taken together, our data suggest a model in which CALCOCO1 mediates selective Golgiphagy to control Golgi size and morphology in eukaryotic cells via its interaction with ZDHHC17.
高尔基复合体对于新合成的蛋白质和脂质的加工、分拣和运输至关重要。高尔基的周转率受到调控以满足不同的细胞生理需求。然而，自噬在高尔基周转率中的作用尚不清楚。在这里，我们发现 CALCOCO1 结合驻留在高尔基上的棕榈酰转移酶 ZDHHC17，以促进饥饿时高尔基通过自噬降解。细胞中 CALCOCO1 的耗竭会导致高尔基的扩张和其结构和膜蛋白的积累。ZDHHC17 本身会被自噬与其他高尔基体膜蛋白如 TMEM165 一起降解。总之，我们的数据表明，CALCOCO1 通过与 ZDHHC17 的相互作用，介导选择性的高尔基体自噬，以控制真核细胞中的高尔基大小和形态。
