YKT6磷酸化对自噬体-溶酶体融合的调控作用

Autophagy reports Pub Date : 2023-05-10 eCollection Date: 2023-01-01 DOI:10.1080/27694127.2023.2210946
Pablo Sánchez-Martín, Claudine Kraft
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引用次数: 0

摘要

YKT6是一种可溶性n -乙基马来酰亚胺敏感融合蛋白附着蛋白受体(SNARE)蛋白,调控多种细胞器的膜融合事件。在自噬过程中,YKT6参与早期吞噬体的形成,并直接参与自噬体与溶解室的融合过程。最近我们在酵母、哺乳动物细胞和线虫中发现YKT6在自噬中的功能可以通过磷酸化来调节。Atg1/ULK1 (unc -51样激酶1)依赖于YKT6的磷酸化在早期(自噬体形成)和后期(自噬体-溶酶体融合)阶段都会导致自噬缺陷,最终由于应激诱导的自噬缺陷导致哺乳动物细胞存活率降低。这些发现表明,YKT6不仅在功能上是保守的,而且在调控上也是保守的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Conserved regulation of autophagosome-lysosome fusion through YKT6 phosphorylation.

YKT6 is a SNARE (Soluble N-ethylmaleimide-Sensitive Fusion Protein Attachment Protein Receptor) protein governing membrane fusion events of several cellular organelles. In autophagy, YKT6 is involved in early phagophore formation as well as directly in the fusion process between autophagosomes and the lytic compartment. Recently we showed in yeast, mammalian cells, and nematodes that the function of YKT6 in autophagy can be regulated by phosphorylation. Atg1/ULK1 (Unc-51-like kinase 1)-dependent phosphorylation of YKT6 results in autophagy defects during both early (autophagosome formation) and late (autophagosome-lysosome fusion) steps, ultimately resulting in decreased survival of mammalian cells due to defective stress-induced autophagy. These findings show that not only the function but also the regulation of YKT6 is conserved across species.

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