Evidence map›Paper›PMID 24872509›Full record

ArticleThe EMBO journal2014

Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation.

Jana Wolf, Eugene Valkov, Mark D Allen, Birthe Meineke, Yuliya Gordiyenko, Stephen H McLaughlin, Tayla M Olsen, Carol V Robinson, Mark Bycroft, Murray Stewart and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 69 citations in OpenAlex.

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  20. Prospects for pharmacological targeting of pseudokinases.Nature reviews. Drug discovery · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Jana WolfMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Eugene ValkovMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Mark D AllenMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Birthe MeinekeMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Yuliya GordiyenkoChemistry Research Laboratory, University of Oxford, Oxford, UK.
Stephen H McLaughlinMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Tayla M OlsenMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Carol V RobinsonChemistry Research Laboratory, University of Oxford, Oxford, UK.
Mark BycroftMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Murray StewartMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.
Lori A PassmoreMedical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK passmore@mrc-lmb.cam.ac.uk.
Medical Research Council · GBMRC Laboratory of Molecular Biology · GBUniversity of Oxford · GB

Funding

European Research Council 261151Medical Research Council MC_U105178939Medical Research Council MC_U105192715Wellcome Trust 080522/Z/60/ZWellcome Trust 088150Wellcome Trust 088150/B/09/Z
6 · The paper itself

Abstract

The conserved eukaryotic Pan2-Pan3 deadenylation complex shortens cytoplasmic mRNA 3' polyA tails to regulate mRNA stability. Although the exonuclease activity resides in Pan2, efficient deadenylation requires Pan3. The mechanistic role of Pan3 is unclear. Here, we show that Pan3 binds RNA directly both through its pseudokinase/C-terminal domain and via an N-terminal zinc finger that binds polyA RNA specifically. In contrast, isolated Pan2 is unable to bind RNA. Pan3 binds to the region of Pan2 that links its N-terminal WD40 domain to the C-terminal part that contains the exonuclease, with a 2:1 stoichiometry. The crystal structure of the Pan2 linker region bound to a Pan3 homodimer shows how the unusual structural asymmetry of the Pan3 dimer is used to form an extensive high-affinity interaction. This binding allows Pan3 to supply Pan2 with substrate polyA RNA, facilitating efficient mRNA deadenylation by the intact Pan2-Pan3 complex.

Indexed as

Models, MolecularBase SequenceChaetomiumChromatography, AffinityCloning, MolecularElectrophoretic Mobility Shift AssayExoribonucleasesMagnetic Resonance SpectroscopyMass SpectrometryMolecular Sequence DataMultiprotein ComplexesPoly(A)-Binding ProteinsProtein BindingProtein MultimerizationRNA, MessengerSaccharomyces cerevisiaeExoribonucleasesMultiprotein Complexespab1 protein, S cerevisiaePAN3 protein, S cerevisiaePoly(A)-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSepharosegene expressionmRNA deadenylationPan2–Pan3polyA tailprotein structure

Identifiers

PMID24872509
PMCPMC4158885
OpenAlexW2171682992

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.