Evidence map›Paper›PMID 29290488›Full record

ArticleStructure (London, England : 1993)2018

Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6.

Benjamin Rothé, Catherine N Leettola, Lucia Leal-Esteban, Duilio Cascio, Simon Fortier, Manuela Isenschmid, James U Bowie, Daniel B Constam

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. mRNA (New York, N.Y.) · 2025
    Article
  8. Article
  9. TheBiomedicines · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Bicaudal-C Post-transcriptional regulator of cell fates and functions.Frontiers in cell and developmental biology · 2022
    Review
  15. Article
  16. Article
  17. Molecular and cellular basis of left-right asymmetry in vertebrates.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2020
    Review
  18. Metabolic perturbations caused by depletion of nephronophthisis factor Anks6 in mIMCD3 cells.Metabolomics : Official journal of the Metabolomic Society · 2019
    Article
  19. Article
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 2 institutions in 2 countries.

Benjamin RothéEcole Polytechnique Fédérale de Lausanne (EPFL), School of Life Sciences, SV ISREC, Station 19, 1015 Lausanne, Switzerland.
Catherine N LeettolaDepartment of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, Boyer Hall, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.
Lucia Leal-EstebanEcole Polytechnique Fédérale de Lausanne (EPFL), School of Life Sciences, SV ISREC, Station 19, 1015 Lausanne, Switzerland.
Duilio CascioDepartment of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, Boyer Hall, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.
Simon FortierEcole Polytechnique Fédérale de Lausanne (EPFL), School of Life Sciences, SV ISREC, Station 19, 1015 Lausanne, Switzerland.
Manuela IsenschmidEcole Polytechnique Fédérale de Lausanne (EPFL), School of Life Sciences, SV ISREC, Station 19, 1015 Lausanne, Switzerland.
James U BowieDepartment of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, Boyer Hall, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.
Daniel B ConstamEcole Polytechnique Fédérale de Lausanne (EPFL), School of Life Sciences, SV ISREC, Station 19, 1015 Lausanne, Switzerland. Electronic address: daniel.constam@epfl.ch.
École Polytechnique Fédérale de Lausanne · CHUniversity of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
A SAM domain network in Polycystic Kidney DiseaseR01DK100482 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2014 to 2017
$1.1M
NCRR NIH HHS S10 RR029205NIDDK NIH HHS R01 DK100482NIGMS NIH HHS P41 GM103403NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Head-to-tail polymers of sterile alpha motifs (SAM) can scaffold large macromolecular complexes. Several SAM-domain proteins that bind each other are mutated in patients with cystic kidneys or laterality defects, including the Ankyrin (ANK) and SAM domain-containing proteins ANKS6 and ANKS3, and the RNA-binding protein Bicc1. To address how their interactions are regulated, we first determined a high-resolution crystal structure of a Bicc1-SAM polymer, revealing a canonical SAM polymer with a high degree of flexibility in the subunit interface orientations. We further mapped interactions between full-length and distinct domains of Bicc1, ANKS3, and ANKS6. Neither ANKS3 nor ANKS6 alone formed macroscopic homopolymers in vivo. However, ANKS3 recruited ANKS6 to Bicc1, and the three proteins together cooperatively generated giant macromolecular complexes. Thus, the giant assemblies are shaped by SAM domains, their flanking sequences, and SAM-independent protein-protein and protein-mRNA interactions.

Indexed as

Carrier ProteinsCiliopathiesCrystallography, X-RayHEK293 CellsHeLa CellsHumansNuclear ProteinsPolymersProtein ConformationRNA-Binding ProteinsSterile Alpha MotifANKS3 protein, humanANKS6 protein, humanBicc1 protein, humanCarrier ProteinsNuclear ProteinsPolymersRNA-Binding ProteinsANKS3ANKS6Bicaudal-Cciliaciliopathiespolycystic kidneypolymerizationSAMsterile alpha motifX-ray structure

Identifiers

PMID29290488
PMCPMC6258031
OpenAlexW2780973115

What OpenQuestion holds

Textmetadata
LicenceTDM
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.