Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy.

Regulation of Golgi turnover by CALCOCO1-mediated selective autophagy.
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DOI:
10.1083/jcb.202006128
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发表时间:
2021-06-07
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Johansen T
Johansen T
中科院分区:
其他
文献类型:
--
作者:
Nthiga TM;Shrestha BK;Bruun JA;Larsen KB;Lamark T;Johansen T

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Nthiga et al. identify CALCOCO1 as a receptor for autophagic degradation of Golgi during nutrient starvation. CALCOCO1 binds the Golgi-resident palmitoyltransferase ZDHHC17 and ATG8 family proteins to facilitate Golgiphagy to control Golgi size. Depletion of CALCOCO1 causes expansion of the Golgi and accumulation of its structural and membrane proteins. 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.
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