Evidence map›Paper›PMID 37733651›Full record

ArticlePLoS biology2023

Bicc1 ribonucleoprotein complexes specifying organ laterality are licensed by ANKS6-induced structural remodeling of associated ANKS3.

Benjamin Rothé, Yayoi Ikawa, Zhidian Zhang, Takanobu A Katoh, Eriko Kajikawa, Katsura Minegishi, Sai Xiaorei, Simon Fortier, Matteo Dal Peraro, Hiroshi Hamada and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Science advances · 2026
    Article
  4. Article
  5. Article
  6. mRNA (New York, N.Y.) · 2025
    Article
  7. Review
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.

Benjamin RothéEcole Polytechnique Fédérale de Lausanne (EPFL) SV ISREC, Lausanne, Switzerland.ORCID 0000-0002-3191-445X
Yayoi IkawaLaboratory for Organismal Patterning, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Zhidian ZhangEcole Polytechnique Fédérale de Lausanne (EPFL) SV IBI, Lausanne, Switzerland.
Takanobu A KatohLaboratory for Organismal Patterning, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Eriko KajikawaLaboratory for Organismal Patterning, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Katsura MinegishiDepartment of Molecular Therapy, National Institutes of Neuroscience, National Center of Neurology and Psychiatry (NCNP), Tokyo, Japan.
Sai XiaoreiDepartment of Molecular Therapy, National Institutes of Neuroscience, National Center of Neurology and Psychiatry (NCNP), Tokyo, Japan.
Simon FortierEcole Polytechnique Fédérale de Lausanne (EPFL) SV ISREC, Lausanne, Switzerland.
Matteo Dal PeraroEcole Polytechnique Fédérale de Lausanne (EPFL) SV IBI, Lausanne, Switzerland.
Hiroshi HamadaLaboratory for Organismal Patterning, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Daniel B ConstamEcole Polytechnique Fédérale de Lausanne (EPFL) SV ISREC, Lausanne, Switzerland.ORCID 0000-0002-6256-3891
École Polytechnique Fédérale de Lausanne · CHRIKEN Center for Biosystems Dynamics Research · JPNational Center of Neurology and Psychiatry · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organ laterality of vertebrates is specified by accelerated asymmetric decay of Dand5 mRNA mediated by Bicaudal-C1 (Bicc1) on the left side, but whether binding of this or any other mRNA to Bicc1 can be regulated is unknown. Here, we found that a CRISPR-engineered truncation in ankyrin and sterile alpha motif (SAM)-containing 3 (ANKS3) leads to symmetric mRNA decay mediated by the Bicc1-interacting Dand5 3' UTR. AlphaFold structure predictions of protein complexes and their biochemical validation by in vitro reconstitution reveal a novel interaction of the C-terminal coiled coil domain of ANKS3 with Bicc1 that inhibits binding of target mRNAs, depending on the conformation of ANKS3 and its regulation by ANKS6. The dual regulation of RNA binding by mutually opposing structured protein domains in this multivalent protein network emerges as a novel mechanism linking associated laterality defects and possibly other ciliopathies to perturbed dynamics in Bicc1 ribonucleoparticle (RNP) formation.

Indexed as

Clustered Regularly Interspaced Short Palindromic RepeatsFunctional LateralityAnimalsProtein DomainsRibonucleoproteinsRNA, MessengerRibonucleoproteinsRNA, Messenger

Identifiers

PMID37733651
PMCPMC10513324
OpenAlexW4386922057

What OpenQuestion holds

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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.