Evidence map›Paper›PMID 29045748›Full record

ArticleNucleic acids research2017

Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.

Alex Heyam, Claire E Coupland, Clément Dégut, Ruth A Haley, Nicola J Baxter, Leonhard Jakob, Pedro M Aguiar, Gunter Meister, Michael P Williamson, Dimitris Lagos and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. 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
0.9field-weighted citation impact, top 26% 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, 24 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Alex HeyamDepartment of Biology, University of York, York, YO10 5DD, UK.
Claire E CouplandDepartment of Biology, University of York, York, YO10 5DD, UK.
Clément DégutDepartment of Biology, University of York, York, YO10 5DD, UK.
Ruth A HaleyDepartment of Biology, University of York, York, YO10 5DD, UK.
Nicola J BaxterDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Leonhard JakobBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Pedro M AguiarDepartment of Chemistry, University of York, York, YO10 5DD, UK.
Gunter MeisterBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Michael P WilliamsonDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Dimitris LagosCentre for Immunology and Infection, Department of Biology and Hull York Medical School, University of York, Wentworth Way, York, YO10 5DD, UK.
Michael J PlevinDepartment of Biology, University of York, York, YO10 5DD, UK.
University of York · GBUniversity of Regensburg · DEUniversity of Sheffield · GB

Funding

Medical Research Council MC_U117533887Medical Research Council MR/L008505/1
6 · The paper itself

Abstract

Double-stranded RNA-binding domains (dsRBDs) are commonly found in modular proteins that interact with RNA. Two varieties of dsRBD exist: canonical Type A dsRBDs interact with dsRNA, while non-canonical Type B dsRBDs lack RNA-binding residues and instead interact with other proteins. In higher eukaryotes, the microRNA biogenesis enzyme Dicer forms a 1:1 association with a dsRNA-binding protein (dsRBP). Human Dicer associates with HIV TAR RNA-binding protein (TRBP) or protein activator of PKR (PACT), while Drosophila Dicer-1 associates with Loquacious (Loqs). In each case, the interaction involves a region of the protein that contains a Type B dsRBD. All three dsRBPs are reported to homodimerize, with the Dicer-binding region implicated in self-association. We report that these dsRBD homodimers display structural asymmetry and that this unusual self-association mechanism is conserved from flies to humans. We show that the core dsRBD is sufficient for homodimerization and that mutation of a conserved leucine residue abolishes self-association. We attribute differences in the self-association properties of Loqs, TRBP and PACT to divergence of the composition of the homodimerization interface. Modifications that make TRBP more like PACT enhance self-association. These data are examined in the context of miRNA biogenesis and the protein/protein interaction properties of Type B dsRBDs.

Indexed as

Drosophila ProteinsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein DomainsProtein MultimerizationRNA-Binding ProteinsRNA, Double-StrandedTrans-Activation Responsive RNA-Binding ProteinDrosophila ProteinsLoqs protein, DrosophilaPRKRA protein, humanRNA-Binding ProteinsRNA, Double-StrandedTrans-Activation Responsive RNA-Binding Protein

Identifiers

PMID29045748
PMCPMC5716075
OpenAlexW2767180234

What OpenQuestion holds

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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.