Evidence map›Paper›PMID 35836927›Full record

ArticleFrontiers in molecular biosciences2022

Deciphering the Molecular Interaction Between the Adhesion G Protein-Coupled Receptor ADGRV1 and its PDZ-Containing Regulator PDZD7.

Baptiste Colcombet-Cazenave, Florence Cordier, Yanlei Zhu, Guillaume Bouvier, Eleni Litsardaki, Louise Laserre, Marie S Prevost, Bertrand Raynal, Célia Caillet-Saguy, Nicolas Wolff

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Liquid-liquid phase separation in hair cell stereocilia development and maintenance.Computational and structural biotechnology journal · 2023
    Review
  5. 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

10 authors at 4 institutions in 1 country.

Baptiste Colcombet-CazenaveChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Florence CordierStructural Bioinformatics Unit, UMR CNRS 3528, Institut Pasteur, Université de Paris, Paris, France.
Yanlei ZhuChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Guillaume BouvierStructural Bioinformatics Unit, UMR CNRS 3528, Institut Pasteur, Université de Paris, Paris, France.
Eleni LitsardakiChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Louise LaserreChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Marie S PrevostChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Bertrand RaynalMolecular Biophysics Platform-C2RT, UMR CNRS 3528, Institut Pasteur, Université de Paris, Paris, France.
Célia Caillet-SaguyChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Nicolas WolffChannel Receptors Unit, UMR CNRS 3571, Institut Pasteur, Université de Paris, Paris, France.
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FRUniversité Paris Cité · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hearing relies on the transduction of sound-evoked vibrations into electrical signals, occurring in the stereocilia bundle of inner ear hair cells. The G protein-coupled receptor (GPCR) ADGRV1 and the multi-PDZ protein PDZD7 play a critical role in the formation and function of stereocilia through their scaffolding and signaling properties. During hair cell development, the GPCR activity of ADGRV1 is specifically inhibited by PDZD7 through an unknown mechanism. Here, we describe the key interactions mediated by the two N-terminal PDZ domains of PDZD7 and the cytoplasmic domain of ADGRV1. Both PDZ domains can bind to the C-terminal PDZ binding motif (PBM) of ADGRV1 with the critical contribution of atypical C-terminal β extensions. The two PDZ domains form a supramodule in solution, stabilized upon PBM binding. Interestingly, we showed that the stability and binding properties of the PDZ tandem are affected by two deafness-causing mutations located in the binding grooves of PDZD7 PDZ domains.

Indexed as

ADGRV1deafnessG protein-coupled receptorPDZ-containing proteinPDZD7PDZ tandem

Identifiers

PMID35836927
PMCPMC9274004
OpenAlexW4283646738

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.