Evidence map›Paper›PMID 18270268›Full record

ArticleJournal of cell science2008

Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells.

Flavia A Wald, Andrea S Oriolo, Anastasia Mashukova, Nevis L Fregien, Amber H Langshaw, Pedro J I Salas

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Inhibition of protein kinase C-α and activation of ezrin byAmerican journal of physiology. Endocrinology and metabolism · 2023
    Article
  6. Review
  7. EnteropathogenicInternational journal of molecular sciences · 2020
    Article
  8. Ezrin Mediates Invasion and Metastasis in Tumorigenesis: A Review.Frontiers in cell and developmental biology · 2020
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Plasticity of the brush border - the yin and yang of intestinal homeostasis.Nature reviews. Gastroenterology & hepatology · 2016
    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

6 authors at 1 institution in 1 country.

Flavia A WaldDepartment of Cell Biology and Anatomy, University of Miami Miller School of Medicine, Miami, FL 33135, USA.
Andrea S Oriolo
Anastasia Mashukova
Nevis L Fregien
Amber H Langshaw
Pedro J I Salas
University of Miami · US

Funding

Apical Polarity Complex Signaling in Inflammation in Intestinal EpitheliaR01DK076652 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SALAS, PEDRO · 2007 to 2015
$2.9M
Apical intermediate filament (IF) mediated post ischemia recovery in epitheliaR01DK057805 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SALAS, PEDRO · 2001 to 2009
$2.2M
NIDDK NIH HHS R01 DK057805NIDDK NIH HHS R01DK057805NIDDK NIH HHS R01 DK076652NIDDK NIH HHS R01DK076652
6 · The paper itself

Abstract

Atypical protein kinase iota (PKCiota) is a key organizer of the apical domain in epithelial cells. Ezrin is a cytosolic protein that, upon activation by phosphorylation of T567, is localized under the apical membrane where it connects actin filaments to membrane proteins and recruits protein kinase A (PKA). To identify the kinase that phosphorylates ezrin T567 in simple epithelia, we analyzed the expression of active PKC and the appearance of T567-P during enterocyte differentiation in vivo. PKCiota phosphorylated ezrin on T567 in vitro, and in Sf9 cells that do not activate human ezrin. In CACO-2 human intestinal cells in culture, PKCiota co-immunoprecipitated with ezrin and was knocked down by shRNA expression. The resulting phenotype showed a modest decrease in total ezrin, but a steep decrease in T567 phosphorylation. The PKCiota-depleted cells showed fewer and shorter microvilli and redistribution of the PKA regulatory subunit. Expression of a dominant-negative form of PKCiota also decreased T567-P signal, and expression of a constitutively active PKCiota mutant showed depolarized distribution of T567-P. We conclude that, although other molecular mechanisms contribute to ezrin activation, apically localized phosphorylation by PKCiota is essential for the activation and normal distribution of ezrin at the early stages of intestinal epithelial cell differentiation.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCaco-2 CellsCell DifferentiationCell MembraneCell PolarityCytoskeletal ProteinsDown-RegulationEnzyme ActivationEzrinHumansInsectaIntestinal MucosaIsoenzymesMembrane MicrodomainsCytoskeletal ProteinsEzrinIsoenzymesProtein Kinase CProtein Kinase C-lambdaProtein SubunitsRNA, Small InterferingTyrosine

Identifiers

PMID18270268
PMCPMC2293289
OpenAlexW2166734267

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.