ArticleJournal of cell science2008
Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells.
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.
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Who cites it
44 citing papers in PubMed, 73 citations in OpenAlex.
- The unphosphorylated, closed form of ezrin binds to RNA to maintain a metastatic phenotype in osteosarcoma cells.Science signaling · 2026Article
- The PKCι-β-arrestin2 axis disrupts SORLA retrograde trafficking, driving its degradation and amyloid pathology in Alzheimer's disease.Molecular neurodegeneration · 2025Article
- Radixin: Roles in the Nervous System and Beyond.Biomedicines · 2024Review
- Loss of polarity regulators initiates gasdermin-E-mediated pyroptosis in syncytiotrophoblasts.Life science alliance · 2023Article
- Inhibition of protein kinase C-α and activation of ezrin byAmerican journal of physiology. Endocrinology and metabolism · 2023Article
- A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.Biophysical reviews · 2022Review
- EnteropathogenicInternational journal of molecular sciences · 2020Article
- Ezrin Mediates Invasion and Metastasis in Tumorigenesis: A Review.Frontiers in cell and developmental biology · 2020Review
- Perspectives for Ezrin and Radixin in Astrocytes: Kinases, Functions and Pathology.International journal of molecular sciences · 2019Review
- Intestinal epithelial cell polarity defects in disease: lessons from microvillus inclusion disease.Disease models & mechanisms · 2018Review
- Role of Polarity Proteins in the Generation and Organization of Apical Surface Protrusions.Cold Spring Harbor perspectives in biology · 2018Review
- The role of intestinal oxalate transport in hyperoxaluria and the formation of kidney stones in animals and man.Urolithiasis · 2017Review
- Down-regulation of protein kinase C alpha/ezrin signals in light-induced phagocytic crisis of retinal pigment epithelium cells.International journal of ophthalmology · 2017Article
- Prkci is required for a non-autonomous signal that coordinates cell polarity during cavitation.Developmental biology · 2016Article
- Review
- Conditional knockout of polarity complex (atypical) PKCι reveals an anti-inflammatory function mediated by NF-κB.Molecular biology of the cell · 2016Article
- Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation.Biophysical journal · 2016Article
- Lens placode planar cell polarity is dependent on Cdc42-mediated junctional contraction inhibition.Developmental biology · 2016Article
- Plasticity of the brush border - the yin and yang of intestinal homeostasis.Nature reviews. Gastroenterology & hepatology · 2016Review
- Resistin, a fat-derived secretory factor, promotes metastasis of MDA-MB-231 human breast cancer cells through ERM activation.Scientific reports · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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.
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