COPII 亚基与自噬受体协同作用，将内质网靶向降解。
A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation.
机构信息
Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA 92093, USA.
Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.
出版信息
Science. 2019 Jul 5;365(6448):53-60. doi: 10.1126/science.aau9263.
The COPII-cargo adaptor complex Lst1-Sec23 selectively sorts proteins into vesicles that bud from the endoplasmic reticulum (ER) and traffic to the Golgi. Improperly folded proteins are prevented from exiting the ER and are degraded. ER-phagy is an autophagic degradation pathway that uses ER-resident receptors. Working in yeast, we found an unexpected role for Lst1-Sec23 in ER-phagy that was independent from its function in secretion. Up-regulation of the stress-inducible ER-phagy receptor Atg40 induced the association of Lst1-Sec23 with Atg40 at distinct ER domains to package ER into autophagosomes. Lst1-mediated ER-phagy played a vital role in maintaining cellular homeostasis by preventing the accumulation of an aggregation-prone protein in the ER. Lst1 function appears to be conserved because its mammalian homolog, SEC24C, was also required for ER-phagy.
COPII-货物衔接复合物 Lst1-Sec23 选择性地将蛋白质分拣到从小泡从内质网 (ER) 出芽并运输到高尔基体的小泡中。未折叠的蛋白质被阻止离开 ER 并被降解。内质网自噬是一种利用内质网驻留受体的自噬降解途径。在酵母中，我们发现 Lst1-Sec23 在 ER 自噬中发挥了意想不到的作用，这与其在分泌中的功能无关。应激诱导的内质网自噬受体 Atg40 的上调诱导 Lst1-Sec23 与内质网特定区域的 Atg40 结合，将内质网包装成自噬体。Lst1 介导的 ER 自噬通过防止易聚集蛋白在 ER 中的积累，对维持细胞内稳态起着至关重要的作用。Lst1 的功能似乎是保守的，因为其哺乳动物同源物 SEC24C 也被需要用于 ER 自噬。
Zotero 插件