C53 is a cross-kingdom conserved reticulophagy receptor that bridges the gap betweenselective autophagy and ribosome stalling at the endoplasmic reticulum
| Autor: | Yasin F. Dagdas, Lorenzo Picchianti, Madlen Stephani |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
ribosome stalling Receptor complex ER-phagy ATG8 Reticulophagy Arabidopsis Autophagy-Related Proteins Endoplasmic Reticulum Ribosome 03 medical and health sciences ufmylation ER-quality control Autophagy Homeostasis Humans Molecular Biology Adaptor Proteins Signal Transducing selective autophagy 030102 biochemistry & molecular biology biology Arabidopsis thaliana CDK5RAP3 Endoplasmic reticulum Autophagosomes Signal transducing adaptor protein Autophagy-Related Protein 8 Family Cell Biology Endoplasmic Reticulum Stress selective autophagy receptor Autophagic Punctum Ubiquitin ligase Cell biology 030104 developmental biology Unfolded protein response biology.protein Carrier Proteins Ribosomes Article Commentary |
| Zdroj: | Autophagy article-version (VoR) Version of Record |
| ISSN: | 1554-8635 1554-8627 |
| Popis: | Reticulophagy, the autophagic degradation of the endoplasmic reticulum, is crucial to maintain ER homeostasis during stress. Although several reticulophagy receptors have been discovered recently, most of them have been studied using nutrient starvation. How macroautophagy/autophagy cross-talks with other ER-quality control mechanisms is largely unknown. Using ATG8-based affinity proteomics in the model plant Arabidopsis thaliana, we identified AT5G06830/C53, a soluble protein that directly interacts with ATG8. Biochemical and biophysical characterization of C53-ATG8 interaction using both human (CDK5RAP3) and Arabidopsis proteins revealed that C53 binds ATG8 via shuffled Atg8-family interacting motifs (sAIMs) located at its intrinsically disordered region (IDR). C53 is recruited to phagophores, precursors to autophagosomes, during ER stress in an autophagy-dependent manner. Consistently, c53 mutants are highly sensitive to ER stress treatments. C53 senses ER stress by forming a tripartite receptor complex that involves UFL1, the E3 ligase that mediates ufmylation, and its ER-resident adaptor protein DDRGK1. C53 activity is regulated by another ubiquitin-like protein, UFM1, which is transferred from C53 to the ribosomes upon ribosome collision/stalling at the ER, thereby activating the C53 pathway to recycle stalled nascent chains. Altogether our findings suggest C53 forms an ancient quality control pathway that links ribosome-associated quality control with selective autophagy at the ER. |
| Databáze: | OpenAIRE |
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