Evidence map›Paper›PMID 22157759›Full record

ArticleThe Journal of biological chemistry2012

Regulation of the ligand-dependent activation of the epidermal growth factor receptor by calmodulin.

Hongbing Li, Svetlana Panina, Amandeep Kaur, María J Ruano, Pablo Sánchez-González, Jonas M la Cour, Alexander Stephan, Uffe H Olesen, Martin W Berchtold, Antonio Villalobo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The complexities of PKCα signaling in cancer.Advances in biological regulation · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019
    Review
  10. Review
  11. Article
  12. Betacellulin ameliorates hyperglycemia in obese diabetic db/db mice.Journal of molecular medicine (Berlin, Germany) · 2015
    Article
  13. Article
  14. Review
  15. Inactive ERBB receptors cooperate with reactive oxygen species to suppress cancer progression.Molecular therapy : the journal of the American Society of Gene Therapy · 2013
    Article
  16. 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

10 authors at 3 institutions in 2 countries.

Hongbing LiInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Arturo Duperier 4, E-28029 Madrid, Spain.
Svetlana Panina
Amandeep Kaur
María J Ruano
Pablo Sánchez-González
Jonas M la Cour
Alexander Stephan
Uffe H Olesen
Martin W Berchtold
Antonio Villalobo
Universidad Autónoma de Madrid · ESUniversity of Copenhagen · DKNovo Nordisk (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM) is the major component of calcium signaling pathways mediating the action of various effectors. Transient increases in the intracellular calcium level triggered by a variety of stimuli lead to the formation of Ca(2+)/CaM complexes, which interact with and activate target proteins. In the present study the role of Ca(2+)/CaM in the regulation of the ligand-dependent activation of the epidermal growth factor receptor (EGFR) has been examined in living cells. We show that addition of different cell permeable CaM antagonists to cultured cells or loading cells with a Ca(2+) chelator inhibited ligand-dependent EGFR auto(trans)phosphorylation. This occurred also in the presence of inhibitors of protein kinase C, CaM-dependent protein kinase II and calcineurin, which are known Ca(2+)- and/or Ca(2+)/CaM-dependent EGFR regulators, pointing to a direct effect of Ca(2+)/CaM on the receptor. Furthermore, we demonstrate that down-regulation of CaM in conditional CaM knock out cells stably transfected with the human EGFR decreased its ligand-dependent phosphorylation. Substitution of six basic amino acid residues within the CaM-binding domain (CaM-BD) of the EGFR by alanine resulted in a decreased phosphorylation of the receptor and of its downstream substrate phospholipase Cγ1. These results support the hypothesis that Ca(2+)/CaM regulates the EGFR activity by directly interacting with the CaM-BD of the receptor located at its cytosolic juxtamembrane region.

Indexed as

AnimalsCalcineurinCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCell LineErbB ReceptorsGene Knockdown TechniquesHumansMicePhospholipase C gammaPhosphorylationCalcineurinCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinEGFR protein, humanEGFR protein, mouseErbB ReceptorsPhospholipase C gamma

Identifiers

PMID22157759
PMCPMC3270982
OpenAlexW2002856612

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.