Evidence map›Paper›PMID 32040695›Full record

ArticleCellular and molecular life sciences : CMLS2020

Beta-arrestins operate an on/off control switch for focal adhesion kinase activity.

Revu Ann Alexander, Isaure Lot, Kusumika Saha, Guillaume Abadie, Mireille Lambert, Eleonore Decosta, Hiroyuki Kobayashi, Alexandre Beautrait, Aurélie Borrull, Atef Asnacios and 4 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

14 authors at 2 institutions in 2 countries.

Revu Ann AlexanderInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Isaure LotInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Kusumika SahaInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Guillaume AbadieInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Mireille LambertInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Eleonore DecostaInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Hiroyuki KobayashiDepartment of Biochemistry and the Institute for Research in Immunology and Cancer, Université de Montréal, Montreal, QC, H3C 3J7, Canada.
Alexandre BeautraitDepartment of Biochemistry and the Institute for Research in Immunology and Cancer, Université de Montréal, Montreal, QC, H3C 3J7, Canada.
Aurélie BorrullInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Atef AsnaciosLaboratoire Matière et Systèmes Complexes, CNRS UMR 7057, Université de Paris, Paris, France.
Michel BouvierDepartment of Biochemistry and the Institute for Research in Immunology and Cancer, Université de Montréal, Montreal, QC, H3C 3J7, Canada.
Mark G H ScottInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Stefano MarulloInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France.
Hervé EnslenInstitut Cochin, Inserm U 1016, CNRS UMR8104, Université de Paris, 27 rue du Faubourg Saint-Jacques, 75014, Paris, France. herve.enslen@inserm.fr.ORCID http://orcid.org/0000-0001-9741-5293
Centre National de la Recherche Scientifique · FRInstitute for Research in Immunology and Cancer · CA

Funding

Comité de l'Oise de la Ligue Contre le Cancer 2015-4756069Comité de l'Oise de la Ligue Contre le Cancer 2017-6751150Fondation pour la Recherche Médicale DEQ20120323720
6 · The paper itself

Abstract

Focal adhesion kinase (FAK) regulates key biological processes downstream of G protein-coupled receptors (GPCRs) in normal and cancer cells, but the modes of kinase activation by these receptors remain unclear. We report that after GPCR stimulation, FAK activation is controlled by a sequence of events depending on the scaffolding proteins β-arrestins and G proteins. Depletion of β-arrestins results in a marked increase in FAK autophosphorylation and focal adhesion number. We demonstrate that β-arrestins interact directly with FAK and inhibit its autophosphorylation in resting cells. Both FAK-β-arrestin interaction and FAK inhibition require the FERM domain of FAK. Following the stimulation of the angiotensin receptor AT

Indexed as

Adaptor Protein Complex 2Animalsbeta-ArrestinsCell MembraneFocal Adhesion Protein-Tyrosine KinasesGTP-Binding ProteinsHEK293 CellsHumansMiceMultiprotein ComplexesNeoplasmsPhosphorylationProtein BindingProtein DomainsReceptor, Angiotensin, Type 1Receptors, G-Protein-CoupledAdaptor Protein Complex 2beta-ArrestinsFocal Adhesion Protein-Tyrosine KinasesGTP-Binding ProteinsMultiprotein ComplexesReceptor, Angiotensin, Type 1Receptors, G-Protein-CoupledVasopressinsAP-2Beta-arrestinFAKG-protein-coupled receptorsG proteinsβ-Arrestin

Identifiers

PMID32040695
PMCPMC11104786
OpenAlexW3006151491

What Socratic holds

Textmetadata
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 Socratic graph.