Atg44/Mdi1/mitofissin 可促进 Dnm1 介导的线粒体分裂。

Autophagy Pub Date : 2024-10-01 Epub Date: 2024-06-04 DOI:10.1080/15548627.2024.2360345
Kentaro Furukawa, Manabu Hayatsu, Kentaro Okuyama, Tomoyuki Fukuda, Shun-Ichi Yamashita, Keiichi Inoue, Shinsuke Shibata, Tomotake Kanki
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引用次数: 0

摘要

线粒体会发生裂变和融合,它们之间的协调平衡对于维持线粒体的平衡至关重要。在酵母中,达纳明相关蛋白 Dnm1 是一种从线粒体外部发挥作用的线粒体裂变因子。我们最近报道了线粒体膜间隙蛋白Atg44/mitofissin/Mdi1/Mco8是一种新型裂变因子,但Atg44和Dnm1之间的关系仍然难以捉摸。在这里,我们发现 Atg44 是在平衡条件下完成 Dnm1 介导的线粒体裂变所必需的。Atg44缺陷细胞通常表现出线粒体增大,Dnm1积聚,以及在收缩位点有Dnm1病灶的玫瑰花状线粒体。这些线粒体收缩位点在一个极其狭小的空间内保留了外膜和内膜的连续性,表明如果没有 Atg44,Dnm1 无法完成线粒体分裂。此外,在线粒体收缩位点还观察到累积的 Atg44 蛋白。这些发现表明,Atg44和Dnm1分别从线粒体内部和外部合作执行线粒体分裂。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Atg44/Mdi1/mitofissin facilitates Dnm1-mediated mitochondrial fission.

Mitochondria undergo fission and fusion, and their coordinated balance is crucial for maintaining mitochondrial homeostasis. In yeast, the dynamin-related protein Dnm1 is a mitochondrial fission factor acting from outside the mitochondria. We recently reported the mitochondrial intermembrane space protein Atg44/mitofissin/Mdi1/Mco8 as a novel fission factor, but the relationship between Atg44 and Dnm1 remains elusive. Here, we show that Atg44 is required to complete Dnm1-mediated mitochondrial fission under homeostatic conditions. Atg44-deficient cells often exhibit enlarged mitochondria with accumulated Dnm1 and rosary-like mitochondria with Dnm1 foci at constriction sites. These mitochondrial constriction sites retain the continuity of both the outer and inner membranes within an extremely confined space, indicating that Dnm1 is unable to complete mitochondrial fission without Atg44. Moreover, accumulated Atg44 proteins are observed at mitochondrial constriction sites. These findings suggest that Atg44 and Dnm1 cooperatively execute mitochondrial fission from inside and outside the mitochondria, respectively.Abbreviation: ATG: autophagy related; CLEM: correlative light and electron microscopy; EM: electron microscopy; ER: endoplasmic reticulum; ERMES: endoplasmic reticulum-mitochondria encounter structure; GA: glutaraldehyde; GFP: green fluorescent protein; GTP: guanosine triphosphate: IMM: inner mitochondrial membrane; IMS: intermembrane space; OMM: outer mitochondrial membrane; PB: phosphate buffer; PBS: phosphate-buffered saline; PFA: paraformaldehyde; RFP: red fluorescent protein; WT: wild type.

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