Evidence map›Paper›PMID 27386966›Full record

ArticleNature communications2016

Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling.

Antonio Luis Egea-Jimenez, Rodrigo Gallardo, Abel Garcia-Pino, Ylva Ivarsson, Anna Maria Wawrzyniak, Rudra Kashyap, Remy Loris, Joost Schymkowitz, Frederic Rousseau, Pascale Zimmermann

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
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  6. PDZ scaffolds regulate extracellular vesicle production, composition, and uptake.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
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  9. Review
  10. Review
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  12. Dual Function of Par3 in Tumorigenesis.Frontiers in oncology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
    Review
  19. Review
  20. 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

10 authors at 4 institutions in 2 countries.

Antonio Luis Egea-JimenezCentre de Recherche en Cancérologie de Marseille (CRCM), Inserm, U1068-CNRS UMR7258, Aix-Marseille Université, Institut Paoli-Calmettes, 13009 Marseille, France.
Rodrigo GallardoDepartment of Human Genetics, KU Leuven, ON1 Herestraat 49 Box 602, B-3000 Leuven, Belgium.
Abel Garcia-PinoStructural Biology Brussels, Deptartment of Biotechnology (DBIT), Vrije Universiteit Brussel and Molecular Recognition Unit, Structural Biology Research Center, VIB, Pleinlaan 2, B-1050 Brussel, Belgium.
Ylva IvarssonDepartment of Human Genetics, KU Leuven, ON1 Herestraat 49 Box 602, B-3000 Leuven, Belgium.ORCID 0000-0002-7081-3846
Anna Maria WawrzyniakDepartment of Human Genetics, KU Leuven, ON1 Herestraat 49 Box 602, B-3000 Leuven, Belgium.
Rudra KashyapCentre de Recherche en Cancérologie de Marseille (CRCM), Inserm, U1068-CNRS UMR7258, Aix-Marseille Université, Institut Paoli-Calmettes, 13009 Marseille, France.
Remy LorisStructural Biology Brussels, Deptartment of Biotechnology (DBIT), Vrije Universiteit Brussel and Molecular Recognition Unit, Structural Biology Research Center, VIB, Pleinlaan 2, B-1050 Brussel, Belgium.
Joost SchymkowitzVIB Switch Laboratory, Department of Molecular Cellular and Molecular Medicine, VIB-KU Leuven, B-3000 Leuven, Belgium.ORCID 0000-0003-2020-0168
Frederic RousseauVIB Switch Laboratory, Department of Molecular Cellular and Molecular Medicine, VIB-KU Leuven, B-3000 Leuven, Belgium.
Pascale ZimmermannCentre de Recherche en Cancérologie de Marseille (CRCM), Inserm, U1068-CNRS UMR7258, Aix-Marseille Université, Institut Paoli-Calmettes, 13009 Marseille, France.ORCID 0000-0001-8768-1790
Centre National de la Recherche Scientifique · FRVIB-KU Leuven Center for Cancer Biology · BEKU Leuven · BEVrije Universiteit Brussel · BE

Funding

European Research Council 647458
6 · The paper itself

Abstract

PDZ domain-containing proteins work as intracellular scaffolds to control spatio-temporal aspects of cell signalling. This function is supported by the ability of their PDZ domains to bind other proteins such as receptors, but also phosphoinositide lipids important for membrane trafficking. Here we report a crystal structure of the syntenin PDZ tandem in complex with the carboxy-terminal fragment of Frizzled 7 and phosphatidylinositol 4,5-bisphosphate (PIP2). The crystal structure reveals a tripartite interaction formed via the second PDZ domain of syntenin. Biophysical and biochemical experiments establish co-operative binding of the tripartite complex and identify residues crucial for membrane PIP2-specific recognition. Experiments with cells support the importance of the syntenin-PIP2 interaction for plasma membrane targeting of Frizzled 7 and c-jun phosphorylation. This study contributes to our understanding of the biology of PDZ proteins as key players in membrane compartmentalization and dynamics.

Indexed as

Binding SitesCloning, MolecularCrystallography, X-RayFrizzled ReceptorsGene ExpressionGenetic VectorsHumansMCF-7 CellsModels, MolecularPDZ DomainsPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein TransportFrizzled ReceptorsFZD7 protein, humanPhosphatidylinositol 4,5-DiphosphateRecombinant ProteinsSyntenins

Identifiers

PMID27386966
PMCPMC5515355
OpenAlexW2469502271

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.