S-Nitrosylation Targets GSNO Reductase for Selective Autophagy during Hypoxia Responses in Plants

文献类型： 外文期刊

第一作者： Zhan, Ni

作者： Zhan, Ni;Wang, Chun;Chen, Lichao;Yang, Huanjie;Feng, Jian;Ren, Bo;Wu, Rong;Mu, Jinye;Li, Yansha;Peng, Juli;Zuo, Jianru;Zhan, Ni;Wang, Chun;Chen, Lichao;Yang, Huanjie;Feng, Jian;Ren, Bo;Wu, Rong;Mu, Jinye;Li, Yansha;Peng, Juli;Zuo, Jianru;Zhan, Ni;Wang, Chun;Chen, Lichao;Yang, Huanjie;Feng, Jian;Wu, Rong;Li, Yansha;Zuo, Jianru;Wang, Chun;Wang, Kejian;Gong, Xinqi;Liu, Zhonghua;Huang, Xun;Zhou, Ying;Xiao, Shi;Zhou, Ying;Xiao, Shi

作者机构：

期刊名称：MOLECULAR CELL （ 影响因子：17.97； 五年影响因子：19.639 ）

ISSN： 1097-2765

年卷期： 2018 年 71 卷 1 期

页码：

收录情况： SCI

摘要： Nitric oxide (NO) regulates diverse cellular signaling through S-nitrosylation of specific Cys residues of target proteins. The intracellular level of S-nitrosoglutathione (GSNO), a major bioactive NO species, is regulated by GSNO reductase (GSNOR), a highly conserved master regulator of NO signaling. However, little is known about how the activity of GSNOR is regulated. Here, we show that S-nitrosylation induces selective autophagy of Arabidopsis GSNOR1 during hypoxia responses. S-nitrosylation of GSNOR1 at Cys-10 induces conformational changes, exposing its AUTOPHAGY-RELATED8 (ATG8)-interacting motif (AIM) accessible by autophagy machinery. Upon binding by ATG8, GSNOR1 is recruited into the autophagosome and degraded in an AIM-dependent manner. Physiologically, the S-nitrosylation-induced selective autophagy of GSNOR1 is relevant to hypoxia responses. Our discovery reveals a unique mechanism by which S-nitrosylation mediates selective autophagy of GSNOR1, thereby establishing a molecular link between NO signaling and autophagy.

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