Journal
EMBO JOURNAL
Volume 40, Issue 15, Pages -Publisher
WILEY
DOI: 10.15252/embj.2021108050
Keywords
autophagy; peptide; plant virus; RNA silencing; SGS3
Categories
Funding
- Natural Science Foundation of China [31872920, 31571978]
- Fundamental Research Funds for the Central Universities (CAU) [2020TC163]
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Selective autophagy mediates the degradation of unwanted cytoplasmic components, maintaining cellular homeostasis. VISP1, a small peptide discovered in Arabidopsis during virus infection, interacts with SGS3 and plays a role in regulating the autophagic degradation of SGS3/RDR6 bodies, affecting viral siRNA amplification.
Selective autophagy mediates specific degradation of unwanted cytoplasmic components to maintain cellular homeostasis. The suppressor of gene silencing 3 (SGS3) and RNA-dependent RNA polymerase 6 (RDR6)-formed bodies (SGS3/RDR6 bodies) are essential for siRNA amplification in planta. However, whether autophagy receptors regulate selective turnover of SGS3/RDR6 bodies is unknown. By analyzing the transcriptomic response to virus infection in Arabidopsis, we identified a virus-induced small peptide 1 (VISP1) composed of 71 amino acids, which harbor a ubiquitin-interacting motif that mediates interaction with autophagy-related protein 8. Overexpression of VISP1 induced selective autophagy and compromised antiviral immunity by inhibiting SGS3/RDR6-dependent viral siRNA amplification, whereas visp1 mutants exhibited opposite effects. Biochemistry assays demonstrate that VISP1 interacted with SGS3 and mediated autophagic degradation of SGS3/RDR6 bodies. Further analyses revealed that overexpression of VISP1, mimicking the sgs3 mutant, impaired biogenesis of endogenous trans-acting siRNAs and up-regulated their targets. Collectively, we propose that VISP1 is a small peptide receptor functioning in the crosstalk between selective autophagy and RNA silencing.
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