Evidence map›Paper›PMID 20855527›Full record

ArticleMolecular and cellular biology2010

Spatial regulation of cyclic AMP-Epac1 signaling in cell adhesion by ERM proteins.

Martijn Gloerich, Bas Ponsioen, Marjolein J Vliem, Zhongchun Zhang, Jun Zhao, Matthijs R Kooistra, Leo S Price, Laila Ritsma, Fried J Zwartkruis, Holger Rehmann and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. All Roads Lead to Cytosol:Frontiers in cellular and infection microbiology · 2021
    Review
  8. Review
  9. Article
  10. Knockout ofTranslational cancer research · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. From Ras to Rap and Back, a Journey of 35 Years.Cold Spring Harbor perspectives in medicine · 2018
    Review
  17. Article
  18. The role of Epac in the heart.Cellular and molecular life sciences : CMLS · 2017
    Review
  19. Article
  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

12 authors at 3 institutions in 1 country.

Martijn GloerichDepartment of Physiological Chemistry, Center for Biomedical Genetics, and Cancer Genomics Center, University Medical Center Utrecht, Utrecht, Netherlands.
Bas Ponsioen
Marjolein J Vliem
Zhongchun Zhang
Jun Zhao
Matthijs R Kooistra
Leo S Price
Laila Ritsma
Fried J Zwartkruis
Holger Rehmann
Kees Jalink
Johannes L Bos
University Medical Center Utrecht · NLCancer Genomics Centre · NLThe Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epac1 is a guanine nucleotide exchange factor for the small G protein Rap and is involved in membrane-localized processes such as integrin-mediated cell adhesion and cell-cell junction formation. Cyclic AMP (cAMP) directly activates Epac1 by release of autoinhibition and in addition induces its translocation to the plasma membrane. Here, we show an additional mechanism of Epac1 recruitment, mediated by activated ezrin-radixin-moesin (ERM) proteins. Epac1 directly binds with its N-terminal 49 amino acids to ERM proteins in their open conformation. Receptor-induced activation of ERM proteins results in increased binding of Epac1 and consequently the clustered localization of Epac1 at the plasma membrane. Deletion of the N terminus of Epac1, as well as disruption of the Epac1-ERM interaction by an interfering radixin mutant or small interfering RNA (siRNA)-mediated depletion of the ERM proteins, impairs Epac1-mediated cell adhesion. We conclude that ERM proteins are involved in the spatial regulation of Epac1 and cooperate with cAMP- and Rap-mediated signaling to regulate adhesion to the extracellular matrix.

Indexed as

AnimalsCell AdhesionCell LineCell MembraneCyclic AMPCytoskeletal ProteinsExtracellular MatrixEzrinGuanine Nucleotide Exchange FactorsHumansMembrane ProteinsMicrofilament Proteinsrap1 GTP-Binding ProteinsReceptors, G-Protein-CoupledRecombinant Fusion ProteinsSignal TransductionCyclic AMPCytoskeletal ProteinsEzrinGuanine Nucleotide Exchange FactorsMembrane ProteinsMicrofilament Proteinsmoesinradixinrap1 GTP-Binding ProteinsRAPGEF3 protein, humanRAPGEF4 protein, humanReceptors, G-Protein-CoupledRecombinant Fusion Proteins

Identifiers

PMID20855527
PMCPMC2976368
OpenAlexW2141261480

What OpenQuestion 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 OpenQuestion graph.