Camougrand Nadine, Vigié Pierre, Dompierre Jim, Massoni-Laporte Aurélie, Lasserre Jean Paul, Bhatia-Kiššová Ingrid
CNRS, UMR5095, 1 rue Camille Saint-Saëns, 33077, Bordeaux cedex, France; Université de Bordeaux, UMR5095, 1 rue Camille Saint-Saëns, 33077, Bordeaux cedex, France.
CNRS, UMR5095, 1 rue Camille Saint-Saëns, 33077, Bordeaux cedex, France.
Biochem Biophys Res Commun. 2022 Dec 20;635:218-226. doi: 10.1016/j.bbrc.2022.10.052. Epub 2022 Oct 19.
Mitochondria play a crucial role in most eukaryotic cells. Mitophagy is a process that controls their quality and quantity within the cells. The outer mitochondrial membrane protein, Atg32, serves as the mitophagic receptor. It interacts with the Atg11 protein to initiate mitophagy and with the Atg8 protein to ensure the engulfment of mitochondria into the autophagosomes for elimination. The Atg32 protein is regulated at the transcriptional level but also by posttranslational modifications. In this study, we described a new regulator of mitophagy, the protein Dep1, identified as a part of the Rpd3L histone deacetylase complex. We showed that the Dep1 protein is localized in the nucleus and associated with mitochondria. This protein is needed for mitophagy and to regulate the transcription and expression of the Atg32 protein. The absence of this protein affects the mitophagy process induced by either starvation for nitrogen or the stationary phase of growth.
线粒体在大多数真核细胞中起着至关重要的作用。线粒体自噬是一个控制细胞内线粒体质量和数量的过程。线粒体外膜蛋白Atg32作为线粒体自噬受体。它与Atg11蛋白相互作用以启动线粒体自噬，并与Atg8蛋白相互作用以确保线粒体被吞噬到自噬体中以便清除。Atg32蛋白在转录水平以及翻译后修饰水平均受到调控。在本研究中，我们描述了一种线粒体自噬的新调节因子，即Dep1蛋白，它被鉴定为Rpd3L组蛋白去乙酰化酶复合物的一部分。我们发现Dep1蛋白定位于细胞核并与线粒体相关。这种蛋白对于线粒体自噬以及调节Atg32蛋白的转录和表达是必需的。该蛋白的缺失会影响由氮饥饿或生长稳定期诱导的线粒体自噬过程。
