Evidence map›Paper›PMID 28165457›Full record

ArticleNature communications2017

A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin.

Annamaria Sgromo, Tobias Raisch, Praveen Bawankar, Dipankar Bhandari, Ying Chen, Duygu Kuzuoğlu-Öztürk, Oliver Weichenrieder, Elisa Izaurralde

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
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  3. Phosphorylation-dependent tuning of mRNA deadenylation rates.Nature structural & molecular biology · 2026
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  19. Unrestrained cleavage of Roquin-1 by MALT1 induces spontaneous T cell activation and the development of autoimmunity.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Annamaria SgromoDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Tobias RaischDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Praveen BawankarDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Dipankar BhandariDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Ying ChenDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Duygu Kuzuoğlu-ÖztürkDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.
Oliver WeichenriederDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.ORCID 0000-0001-5818-6248
Elisa IzaurraldeDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen 72076, Germany.ORCID 0000-0001-7365-2649
Max Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human (Hs) Roquin1 and Roquin2 are RNA-binding proteins that promote mRNA target degradation through the recruitment of the CCR4-NOT deadenylase complex and are implicated in the prevention of autoimmunity. Roquin1 recruits CCR4-NOT via a C-terminal region that is not conserved in Roquin2 or in invertebrate Roquin. Here we show that Roquin2 and Drosophila melanogaster (Dm) Roquin also interact with the CCR4-NOT complex through their C-terminal regions. The C-terminal region of Dm Roquin contains multiple motifs that mediate CCR4-NOT binding. One motif binds to the CAF40 subunit of the CCR4-NOT complex. The crystal structure of the Dm Roquin CAF40-binding motif (CBM) bound to CAF40 reveals that the CBM adopts an α-helical conformation upon binding to a conserved surface of CAF40. Thus, despite the lack of sequence conservation, the C-terminal regions of Roquin proteins act as an effector domain that represses the expression of mRNA targets via recruitment of the CCR4-NOT complex.

Indexed as

AnimalsBinding SitesCarrier ProteinsConserved SequenceCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsGene Knockdown TechniquesHEK293 CellsHumansRecombinant ProteinsRibonucleasesRNA-Binding ProteinsRNA, MessengerRNA StabilityTranscription FactorsCarrier ProteinsCNOT1 protein, humanDrosophila ProteinsmRNA deadenylaseNOT1 protein, DrosophilaRC3H1 protein, humanRecombinant ProteinsRibonucleasesRNA-Binding ProteinsRNA, MessengerTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID28165457
PMCPMC5303829
OpenAlexW2587653817

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.