Evidence map›Paper›PMID 26217012›Full record

ArticleMolecular and cellular biology2015

Bicc1 Polymerization Regulates the Localization and Silencing of Bound mRNA.

Benjamin Rothé, Lucia Leal-Esteban, Florian Bernet, Séverine Urfer, Nicholas Doerr, Thomas Weimbs, Justyna Iwaszkiewicz, Daniel B Constam

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
2.2field-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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 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

8 authors at 3 institutions in 2 countries.

Benjamin RothéEcole Polytechnique Fédérale de Lausanne (EPFL), SV ISREC, Lausanne, Switzerland.
Lucia Leal-EstebanEcole Polytechnique Fédérale de Lausanne (EPFL), SV ISREC, Lausanne, Switzerland.
Florian BernetEcole Polytechnique Fédérale de Lausanne (EPFL), SV ISREC, Lausanne, Switzerland.
Séverine UrferEcole Polytechnique Fédérale de Lausanne (EPFL), SV ISREC, Lausanne, Switzerland.
Nicholas DoerrDepartment of Molecular, Cellular, and Developmental Biology and Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, California, USA.
Thomas WeimbsDepartment of Molecular, Cellular, and Developmental Biology and Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, California, USA.
Justyna IwaszkiewiczSwiss Institute of Bioinformatics, University of Lausanne, Lausanne, Switzerland.
Daniel B ConstamEcole Polytechnique Fédérale de Lausanne (EPFL), SV ISREC, Lausanne, Switzerland Daniel.Constam@epfl.ch.
École Polytechnique Fédérale de Lausanne · CHUniversity of California, Santa Barbara · USUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Loss of the RNA-binding protein Bicaudal-C (Bicc1) provokes renal and pancreatic cysts as well as ectopic Wnt/β-catenin signaling during visceral left-right patterning. Renal cysts are linked to defective silencing of Bicc1 target mRNAs, including adenylate cyclase 6 (AC6). RNA binding of Bicc1 is mediated by N-terminal KH domains, whereas a C-terminal sterile alpha motif (SAM) self-polymerizes in vitro and localizes Bicc1 in cytoplasmic foci in vivo. To assess a role for multimerization in silencing, we conducted structure modeling and then mutated the SAM domain residues which in this model were predicted to polymerize Bicc1 in a left-handed helix. We show that a SAM-SAM interface concentrates Bicc1 in cytoplasmic clusters to specifically localize and silence bound mRNA. In addition, defective polymerization decreases Bicc1 stability and thus indirectly attenuates inhibition of Dishevelled 2 in the Wnt/β-catenin pathway. Importantly, aberrant C-terminal extension of the SAM domain in bpk mutant Bicc1 phenocopied these defects. We conclude that polymerization is a novel disease-relevant mechanism both to stabilize Bicc1 and to present associated mRNAs in specific silencing platforms.

Indexed as

Amino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsHEK293 CellsHumansKidneyLiverMice, Inbred C57BLMice, KnockoutMolecular Docking SimulationMolecular Sequence DataProtein MultimerizationProtein TransportRNA-Binding ProteinsRNA InterferenceBicc1 protein, mouseRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID26217012
PMCPMC4561730
OpenAlexW2114230673

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.