Evidence map›Paper›PMID 41797376›Full record

ArticleFEBS letters2026

The planar cell polarity protein Vangl2 interacts with the PDZ-domains of Scribble but not with a unique PDZ-like domain in Inturned.

Stephan Wilmes, Jan Brysch, Carmen Gelze, Lilli Meier, Daniel Kümmel

Abstract read
In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Stephan WilmesDepartment of Chemistry and Pharmacy, Institute of Biochemistry, University of Münster, Germany.ORCID https://orcid.org/0000-0003-1084-2300
Jan BryschDepartment of Chemistry and Pharmacy, Institute of Biochemistry, University of Münster, Germany.
Carmen GelzeDepartment of Chemistry and Pharmacy, Institute of Biochemistry, University of Münster, Germany.
Lilli MeierDepartment of Chemistry and Pharmacy, Institute of Biochemistry, University of Münster, Germany.
Daniel KümmelDepartment of Chemistry and Pharmacy, Institute of Biochemistry, University of Münster, Germany.ORCID https://orcid.org/0000-0003-3950-5914

Funding

Deutsche Forschungsgemeinschaft SFB1557-P10
6 · The paper itself

Abstract

The proteins Inturned and Fuzzy are members of the tri-longin domain (TLD) RabGEF family and activate the GTPase Rab23 downstream of the core planar cell polarity (PCP) proteins Vangl2 and Prickle. To gain insight into the function of a predicted PDZ domain unique to Inturned among TLD proteins, we performed structural and biochemical characterisations. We show that this domain does not interact with membranes or Vangl2. Instead, we find a phosphorylation-dependent interaction between Vangl2 and a PDZ domain of the apical-basal polarity protein Scribble. A crystal structure of Intu-PDZ reveals a unique PDZ-like fold lacking an interaction site for PDZ-binding motifs. Our data provide new insight into the role of PDZ domains in coordinating cell polarity downstream of Vangl2.

Indexed as

Cell PolarityIntracellular Signaling Peptides and ProteinsMembrane ProteinsPDZ DomainsTumor Suppressor ProteinsAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayHumansModels, MolecularNerve Tissue ProteinsPhosphorylationProtein BindingIntracellular Signaling Peptides and ProteinsMembrane ProteinsNerve Tissue ProteinsSCRIB protein, humanTumor Suppressor ProteinsVANGL2 protein, humanVangl2 protein, ratIntuPDZ domainprotein–protein interactionScribVangX‐ray crystallography

Identifiers

PMID41797376
PMCPMC13618291

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.