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- W2810366247 abstract "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." @default.
- W2810366247 created "2018-07-10" @default.
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- W2810366247 date "2018-07-01" @default.
- W2810366247 modified "2023-10-12" @default.
- W2810366247 title "S-Nitrosylation Targets GSNO Reductase for Selective Autophagy during Hypoxia Responses in Plants" @default.
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- W2810366247 doi "https://doi.org/10.1016/j.molcel.2018.05.024" @default.
- W2810366247 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30008318" @default.
- W2810366247 hasPublicationYear "2018" @default.
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