ArticleNature structural & molecular biology2025
Importance of an N-terminal structural switch in the distinction between small RNA-bound and free ARGONAUTE.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The ubiquitin-proteasome pathway mediates selective degradation of unloaded Argonaute proteins in C. elegans.Genetics · 2026Article
- Decoding Argonaute specificity: insights fromRNA (New York, N.Y.) · 2026Review
- Diverse RNA viral effectors converge on facilitation of AGO4 degradation to promote infection.Nucleic acids research · 2025Article
- Oxidative stress: a new player in the regulation of AGO1 homeostasis?Journal of experimental botany · 2025Article
- Structural and evolutionary determinants of Argonaute function.Nucleic acids research · 2025Article
- Dipeptidyl peptidase DPF-3 is a gatekeeper of microRNA Argonaute compensation in animals.Nature communications · 2025Article
- CSDE1 stabilizes AGO2 in embryonic stem cells.Frontiers in molecular biosciences · 2025Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ARGONAUTE (AGO) proteins bind to small non-coding RNAs to form RNA-induced silencing complexes. In the RNA-bound state, AGO is stable while RNA-free AGO turns over rapidly. Molecular features unique to RNA-free AGO that allow its specific recognition and degradation remain unknown. Here, we identify a confined, linear region in Arabidopsis AGO1 and human Ago2, the N-coil, as a structural switch with preferential accessibility in the RNA-free state. RNA-free Arabidopsis AGO1 interacts with the autophagy cargo receptor ATI1 by direct contact with specific N-coil amino acid residues whose mutation reduces the degradation rate of RNA-free AGO1 in vivo. The N-coil of human Ago2 has similar degron activity dependent on residues in positions equivalent to those required for the Arabidopsis AGO1-ATI1 interaction. These results elucidate the molecular basis for specific recognition and degradation of the RNA-free state of eukaryotic AGO proteins.
Indexed as
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39774835What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.