The ESCRT‐III complex contributes to macromitophagy in yeast
The ESCRT‐III complex contributes to macromitophagy in yeast
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ESCRT-III 复合物有助于酵母的巨线粒体自噬
DOI：
10.1111/tra.12805
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发表时间：
2021-06
期刊：
影响因子：
4.5
通讯作者：
Yongheng Liang
中科院分区：
文献类型：
--
作者：
Zulin Wu;Haiqian Xu;Junze Liu;Fan Zhou;Yongheng Liang
线粒体在真核细胞的能量产生和稳态维持中起重要作用。线粒体自噬可以通过自噬/溶酶体途径非选择性或选择性地去除受损或多余的线粒体。根据降解线粒体的分子机制，选择性去除的线粒体可以通过大线粒体自噬或小线粒体自噬发生。在这项研究中，我们表明，在芽殖酵母中转运III（ESCRT-III）所需的内体分选复合物调节氮饥饿诱导的巨噬细胞，但不是通过监测线粒体标记Om 45在乳酸盐培养基中的对数后生长期。首先，ESCRT-III亚基Snf 7或Vps 4-Vta 1复合物亚基Vps 4（ESCRT复合物的两个代表性亚基）的缺失抑制Om 45-GFP向空泡的递送和降解。其次，我们表明，线粒体标记Om 45和线粒体自噬受体Atg 32积累在ESCRT突变体中标记有Atg 8的自噬体（线粒体自噬体，MP）上。此外，蛋白酶保护测定表明Snf 7和Vps 4参与MP闭合。最后，Snf 7与Atg 11相互作用，这通过两种方式检测，谷胱甘肽-S-转移酶（GST）下拉和双分子荧光互补（BiFC）测定，并且这种BiFC相互作用发生在线粒体网状物上。因此，我们提出ESCRT-III机制通过Snf 7和Atg 11之间的相互作用介导氮饥饿诱导的巨噬细胞吞噬，使得Snf 7通过已知的Atg 11-Atg 32相互作用被招募到Atg 32标记的MP中以密封它们。这些结果表明，ESCRT-III复合物在酵母的巨噬细胞吞噬中发挥着新的作用。
Mitochondria play important roles in energy generation and homeostasis maintenance in eukaryotic cells. The damaged or superfluous mitochondria can be nonselectively or selectively removed through the autophagy/lysosome pathway, which was referred as mitophagy. According to the molecular machinery for degrading mitochondria, the selectively removed mitochondria can occur through macromitophagy or micromitophagy. In this study, we show that the endosomal sorting complex required for transport III (ESCRT‐III) in budding yeast regulates macromitophagy induced by nitrogen starvation, but not by the post‐logarithmic phase growth in lactate medium by monitoring a mitochondrial marker, Om45. Firstly, loss of ESCRT‐III subunit Snf7 or Vps4‐Vta1 complex subunit Vps4, two representative subunits of the ESCRT complex, suppresses the delivery and degradation of Om45‐GFP to vacuoles. Secondly, we show that the mitochondrial marker Om45 and mitophagy receptor Atg32 accumulate on autophagosomes marked with Atg8 (mitophagosomes, MPs) in ESCRT mutants. Moreover, the protease‐protection assay indicates that Snf7 and Vps4 are involved in MP closure. Finally, Snf7 interacts with Atg11, which was detected by two ways, glutathione‐S‐transferase (GST) pulldown and bimolecular fluorescence complementation (BiFC) assay, and this BiFC interaction happens on mitochondrial reticulum. Therefore, we proposed that the ESCRT‐III machinery mediates nitrogen starvation‐induced macromitophagy by the interaction between Snf7 and Atg11 so that Snf7 is recruited to Atg32‐marked MPs by the known Atg11–Atg32 interaction to seal them. These results reveal that the ESCRT‐III complex plays a new role in yeast on macromitophagy.
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DOI：
10.1083/jcb.201611029
发表时间：
2017-10-02
期刊：
The Journal of cell biology
影响因子：
--
作者：
Oku M;Maeda Y;Kagohashi Y;Kondo T;Yamada M;Fujimoto T;Sakai Y
通讯作者：
Sakai Y
影响因子：
16.6
作者：
Takahashi Y;He H;Tang Z;Hattori T;Liu Y;Young MM;Serfass JM;Chen L;Gebru M;Chen C;Wills CA;Atkinson JM;Chen H;Abraham T;Wang HG
通讯作者：
Wang HG
DOI：
10.1074/jbc.m110.173906
发表时间：
2011-02
期刊：
The Journal of Biological Chemistry
影响因子：
--
作者：
Masaki Yuga;K. Gomi;D. Klionsky;T. Shintani
通讯作者：
Masaki Yuga;K. Gomi;D. Klionsky;T. Shintani
影响因子：
4.8
作者：
Leber, R;Silles, E;Mazón, MJ
通讯作者：
Mazón, MJ
ATG32是一种线粒体蛋白，在线粒体过程中赋予了选择性。
影响因子：
11.8
作者：
Kanki, Tomotake;Wang, Ke;Cao, Yang;Baba, Misuzu;Klionsky, Daniel J.
通讯作者：
Klionsky, Daniel J.