期刊
DEVELOPMENTAL CELL
卷 33, 期 5, 页码 603-610出版社
CELL PRESS
DOI: 10.1016/j.devcel.2015.04.015
关键词
-
资金
- ERC StG [260395]
- Kekst Family Institute for Medical Genetics
- Israel Science Foundation [ISF 843/11]
- German Israel Foundation [GIFI-1201-242.13/2012]
- Israel Ministry of Science
- [ERC-StG2013 337713]
- European Research Council (ERC) [260395] Funding Source: European Research Council (ERC)
Exposing cells to folding stress causes a subset of their proteins to misfold and accumulate in inclusion bodies (IBs). IB formation and clearance are both active processes, but little is known about their mechanism. To shed light on this issue, we performed a screen with over 4,000 fluorescently tagged yeast proteins for co-localization with a model mis-folded protein that marks IBs during folding stress. We identified 13 proteins that co-localize to IBs. Remarkably, one of these IB proteins, the uncharacterized and conserved protein Iml2, exhibited strong physical interactions with lipid droplet (LD) proteins. Indeed, we here show that IBs and LDs are spatially and functionally linked. We further demonstrate a mechanism for IB clearance via a sterol-based metabolite emanating from LDs. Our findings therefore uncover a function for Iml2 and LDs in regulating a critical stage of cellular proteostasis.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据