The endosomal sorting complex required for transport complex negatively regulates Erg6 degradation under specific glucose restriction conditions

The endosomal sorting complex required for transport complex negatively regulates Erg6 degradation under specific glucose restriction conditions
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转运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向调节 Erg6 降解

DOI:
10.1111/tra.12732
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发表时间:
2020-05
期刊:
影响因子:
4.5
通讯作者:
Yongheng Liang
Yongheng Liang
中科院分区:
生物学2区
文献类型:
--
作者:
Ao Zhang;Ying Meng;Qunli Li;Yongheng Liang

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脂滴(Lipid drops,LD)是细胞内储存脂肪的细胞器,在脂质代谢、运输和信号转导中发挥重要作用。LD在酿酒酵母中的分解主要通过脂解和噬脂作用实现。在这项研究中,我们发现,内体分选复合物所需的运输(ESCRT)在S。在简化葡萄糖限制(GR)和急性葡萄糖限制(AGR)条件下,酿酒酵母通过监测Erg 6的定位和降解来负调节LD标记Erg 6的周转。ESCRT机制的代表性亚基Vps 27、Snf 7或Vps 4的缺失促进了Erg 6-GFP向空泡的递送及其在简化GR下依赖于噬脂蛋白Atg 15的降解。此外,脂解蛋白Tgl 3和Tgl 4也参与了增强的vps 4 Δ细胞中Erg 6-GFP的空泡定位和降解。此外,我们发现,Atg 14,这是必要的形成pupillary liquid-ordered(Lo)膜结构域的液泡,作为优先内化网站的LD,大量定位于液泡膜ESCRT突变体。最重要的是,Atg 14的耗竭或过表达相应地消除或促进ESCRT突变细胞中观察到的Erg 6降解。我们建议,Atg 14与其他蛋白质一起促进Erg 6降解ESCRT突变细胞在特定的葡萄糖限制条件下。这些结果为ESCRT对LD周转的调控提供了新的思路。
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 vps4Δ 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.
DOI: 10.1016/j.bbalip.2017.06.008
发表时间: 2017-10
期刊: Biochimica et biophysica acta. Molecular and cell biology of lipids
影响因子: --
作者:
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发表时间: 2018-08-03
期刊: Molecules (Basel, Switzerland)
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发表时间: 1983-10
影响因子: 3.2
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DOI: 10.1016/j.celrep.2017.03.026
发表时间: 2017-04-04
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影响因子: 8.8
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