Evidence map›Paper›PMID 26188511›Full record

ArticleBiochemical and biophysical research communications2015

SUMOylation of Argonaute-2 regulates RNA interference activity.

Fernando Josa-Prado, Jeremy M Henley, Kevin A Wilkinson

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. MicroRNA biogenesis proteins follow tissue-dependent expression during freezing in Dryophytes versicolor.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Regulation of microRNA function in animals.Nature reviews. Molecular cell biology · 2019
    Review
  10. Review
  11. Article
  12. Drosophila Argonaute2 turnover is regulated by the ubiquitin proteasome pathway.Biochemical and biophysical research communications · 2017
    Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Fernando Josa-PradoSchool of Biochemistry, Medical Sciences Building, University Walk, University of Bristol, Bristol, BS8 1TD, United Kingdom.
Jeremy M HenleySchool of Biochemistry, Medical Sciences Building, University Walk, University of Bristol, Bristol, BS8 1TD, United Kingdom.
Kevin A WilkinsonSchool of Biochemistry, Medical Sciences Building, University Walk, University of Bristol, Bristol, BS8 1TD, United Kingdom. Electronic address: Kevin.Wilkinson@bristol.ac.uk.
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K014358/1Medical Research Council MR/L003791/1Wellcome Trust
6 · The paper itself

Abstract

Post-translational modification of substrate proteins by small ubiquitin-like modifier (SUMO) regulates a vast array of cellular processes. SUMOylation occurs through three sequential enzymatic steps termed E1, E2 and E3. Substrate selection can be determined through interactions between the target protein and the SUMO E2 conjugating enzyme Ubc9 and specificity can be enhanced by substrate interactions with E3 ligase enzymes. We used the putative substrate recognition (PINIT) domain from the SUMO E3 PIAS3 as bait to identify potential SUMO substrates. One protein identified was Argonaute-2 (Ago2), which mediates RNA-induced gene silencing through binding small RNAs and promoting degradation of complimentary target mRNAs. We show that Ago2 can be SUMOylated in mammalian cells by both SUMO1 and SUMO2. SUMOylation occurs primarily at K402, and mutation of the SUMO consensus site surrounding this lysine reduces Ago2-mediated siRNA-induced silencing in a luciferase-based reporter assay. These results identify SUMOylation as a potential regulator of Ago2 activity and open new avenues for research into the mechanisms underlying the regulation of RNA-induced gene silencing.

Indexed as

RNA InterferenceSumoylationAmino Acid SequenceAnimalsArgonaute ProteinsBinding SitesCells, CulturedConsensus SequenceGene Knockout TechniquesHumansMiceMutagenesis, Site-DirectedProtein Inhibitors of Activated STATProtein Interaction Domains and MotifsRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsAGO2 protein, humanAgo2 protein, mouseArgonaute ProteinsProtein Inhibitors of Activated STATRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinArgonautePIAS3RNAiSUMOylationUbc9

Identifiers

PMID26188511
PMCPMC4624959
OpenAlexW1626423022

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 OpenQuestion graph.