Evidence map›Paper›PMID 19913059›Full record

ArticleBiochimica et biophysica acta2010

G protein-coupled receptor kinase 2 activates radixin, regulating membrane protrusion and motility in epithelial cells.

Alem W Kahsai, Shoutian Zhu, Gabriel Fenteany

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. The roles of G protein-coupled receptor kinase 2 in renal diseases.Journal of cellular and molecular medicine · 2024
    Review
  4. Article
  5. The GRKs Reactome: Role in Cell Biology and Pathology.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. PEBP1/RKIP behavior: a mirror of actin-membrane organization.Cellular and molecular life sciences : CMLS · 2020
    Article
  9. Review
  10. Review
  11. Article
  12. Proteome Profiling in Lung Injury after Hematopoietic Stem Cell Transplantation.Biology of blood and marrow transplantation : journal of the American Society for Blood and Marrow Transplantation · 2016
    Article
  13. A glimpse of the ERM proteins.Journal of biomedical science · 2016
    Review
  14. Review
  15. Review
  16. Review
  17. Epidermal growth factor-induced cellular invasion requires sphingosine-1-phosphate/sphingosine-1-phosphate 2 receptor-mediated ezrin activation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  18. Article
  19. G-protein-coupled receptor kinase 2 and hypertension: molecular insights and pathophysiological mechanisms.High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2013
    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

3 authors at 1 institution in 1 country.

Alem W KahsaiDepartment of Chemistry, University of Connecticut, Storrs, CT 06269, USA.
Shoutian Zhu
Gabriel Fenteany
University of Connecticut · US

Funding

Mechanism of Action of New Inhibitors of Cell MigrationR01GM077622 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI FENTEANY, GABRIEL · 2006 to 2010
$1.6M
NIGMS NIH HHS GM077622NIGMS NIH HHS R01 GM077622
6 · The paper itself

Abstract

Ezrin/radixin/moesin (ERM) proteins are membrane-cytoskeleton linkers that also have roles in signal transduction. Here we show that G protein-coupled receptor kinase 2 (GRK2) regulates membrane protrusion and cell migration during wound closure in Madin-Darby canine kidney (MDCK) epithelial cell monolayers at least partly through activating phosphorylation of radixin on a conserved, regulatory C-terminal Thr residue. GRK2 phosphorylated radixin exclusively on Thr 564 in vitro. Expression of a phosphomimetic (Thr-564-to-Asp) mutant of radixin resulted in increased Rac1 activity, membrane protrusion and cell motility in MDCK cells, suggesting that radixin functions "upstream" of Rac1, presumably as a scaffolding protein. Phosphorylation of ERM proteins was highest during the most active phase of epithelial cell sheet migration over the course of wound closure. In view of these results, we explored the mode of action of quinocarmycin/quinocarcin analog DX-52-1, an inhibitor of cell migration and radixin function with considerable selectivity for radixin over the other ERM proteins, finding that its mechanism of inhibition of radixin does not appear to involve binding and antagonism at the site of regulatory phosphorylation.

Indexed as

Animalscdc42 GTP-Binding ProteinCell LineCell MovementCell Surface ExtensionsCytoskeletal ProteinsDogsEpithelial CellsGene SilencingG-Protein-Coupled Receptor Kinase 2IsoquinolinesMembrane ProteinsMutagenesis, Site-Directedrac1 GTP-Binding ProteinRecombinant Fusion Proteinscdc42 GTP-Binding ProteinCytoskeletal ProteinsDX 52-1G-Protein-Coupled Receptor Kinase 2IsoquinolinesMembrane Proteinsrac1 GTP-Binding ProteinradixinRecombinant Fusion Proteins

Identifiers

PMID19913059
PMCPMC2838949
OpenAlexW1985296918

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.