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The endosomal sorting complex required for transport complex negatively regulates Erg6 degradation under specific glucose restriction conditions.
Traffic ( IF 3.6 ) Pub Date : 2020-05-06 , DOI: 10.1111/tra.12732
Ao Zhang 1 , Ying Meng 1 , Qunli Li 1 , Yongheng Liang 1
Affiliation  

Lipid droplets (LDs) are cytosolic fat storage organelles that play roles in lipid metabolism, trafficking and signaling. Breakdown of LDs in Saccharomyces cerevisiae is mainly achieved by lipolysis and lipophagy. In this study, we found that the endosomal sorting complex required for transport (ESCRT) in S. cerevisiae negatively regulated the turnover of a LD marker, Erg6, under both simplified glucose restriction (GR) and acute glucose restriction (AGR) conditions by monitoring the localization and degradation of Erg6. Loss of Vps27, Snf7 or Vps4, representative subunits of the ESCRT machinery, facilitated the delivery of Erg6‐GFP to vacuoles and its degradation depending on the lipophagy protein Atg15 under simplified GR. Additionally, the lipolysis proteins Tgl3 and Tgl4 were also involved in the enhanced vacuolar localization and degradation of Erg6‐GFP in vps4 Δ cells. Furthermore, we found that Atg14, which is required for the formation of putatively liquid‐ordered (Lo) membrane domains on the vacuole that act as preferential internalization sites for LDs, abundantly localized to vacuolar membranes in ESCRT mutants. Most importantly, the depletion or overexpression of Atg14 correspondingly abolished or promoted the observed Erg6 degradation in ESCRT mutant cells. We propose that Atg14 together with other proteins promotes Erg6 degradation in ESCRT mutant cells under specific glucose restriction conditions. These results shed new light on the regulation of ESCRT on LD turnover.

中文翻译:

运输复合物所需的内体分选复合物在特定的葡萄糖限制条件下负调节Erg6降解。

脂质小滴(LDs)是胞质脂肪存储细胞器,在脂质代谢,运输和信号传导中发挥作用。酿酒酵母中LDs的分解主要通过脂解和脂吞噬来实现。在这项研究中,我们发现酿酒酵母中需要运输的内体分选复合物(ESCRT)通过监测Erg6的定位和降解,在简化的葡萄糖限制(GR)和急性葡萄糖限制(AGR)条件下对LD标记物Erg6的转化产生负调控。ESCRT机制的代表性亚基Vps27,Snf7或Vps4的丢失促进了Erg6-GFP的空泡传递和其降解,这取决于在简化GR下的脂噬蛋白Atg15。此外,脂解蛋白Tgl3和Tgl4也参与了vps4中增强的液泡定位和Erg6-GFP的降解Δ细胞。此外,我们发现Atg14是在液泡上形成假定为液态的(Lo)膜结构域所必需的,该膜结构域充当LD的优先内部化位点,在ESCRT突变体中大量定位于液泡膜。最重要的是,Atg14的耗竭或过表达相应地消除或促进了ESCRT突变细胞中观察到的Erg6降解。我们建议Atg14与其他蛋白质一起在特定的葡萄糖限制条件下促进ESCRT突变细胞中的Erg6降解。这些结果为ESCRT对LD营业额的调控提供了新的思路。
更新日期:2020-06-29
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