Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells

@article{Grune2002EzrinTA,
  title={Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells},
  author={Tilman Grune and Thomas Reinheckel and James A. North and Rui Li and P. Bermejo Besc{\'o}s and Reshma Shringarpure and Kelvin J.A. Davies},
  journal={The FASEB Journal},
  year={2002},
  volume={16},
  pages={1602 - 1610}
}
We find that ezrin, a cytoskeletal protein involved in anchoring actin to the cell membrane, is preferentially degraded and resynthesized after oxidative stress. Ezrin was identified using 2‐dimensional gels and amino‐terminal microsequencing as one of a select few [35S]methionine prelabeled proteins degraded in clone 9 rat liver cells exposed to hydrogen peroxide (H2O2). Metabolic labeling of cellular proteins with [35S]methionine after oxidative stress showed that resynthesis of ezrin rose… 
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41 Citations
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41 Citations

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The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes.
TLDR
Direct comparison of purified 20S proteasome and immunoproteasome demonstrated that the immunoproteinasome can selectively degrade oxidized proteins, which is important during transient (reversible) adaptation, to oxidative stress in murine embryonic fibroblasts.
Ecm29-dependent proteasome localization regulates cytoskeleton remodeling at the immune synapse
TLDR
These findings support a model where B the asymmetric distribution of the proteasome, mediated by Ecm29, coordinates actin dynamics at the centrosome and the IS, promoting lysosome recruitment and cell spreading.
Ecm29-Dependent Proteasome Localization Regulates Cytoskeleton Remodeling at the Immune Synapse
TLDR
These findings support a model where B the asymmetric distribution of the proteasome, mediated by Ecm29, coordinates actin dynamics at the centrosome and the IS, promoting lysosome recruitment and cell spreading.
Phosphorylation of ezrin enhances microvillus length via a p38 MAP-kinase pathway in an immortalized mouse hepatic cell line.
Selective degradation of oxidatively modified protein substrates by the proteasome.
Distinct protease pathways control cell shape and apoptosis in v-src-transformed quail neuroretina cells.
Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells
TLDR
It is concluded that, although other molecular mechanisms contribute to eZrin activation, apically localized phosphorylation by PKCι is essential for the activation and normal distribution of ezrin at the early stages of intestinal epithelial cell differentiation.
Ubiquitin‐dependent lysosomal degradation of the HNE‐modified proteins in lens epithelial cells
  • C. Marques, P. Pereira, +4 authors F. Shang
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2004
TLDR
Findings show that HNE‐modified proteins are degraded via a novel ubiquitin and lysosomal‐dependent but proteasome‐independent pathway.
The proteasomal system.
Clustered PI(4,5)P2 accumulation and ezrin phosphorylation in response to CLIC5A
ABSTRACT CLIC5A (encoded by CLIC5) is a component of the ezrin–NHERF2–podocalyxin complex in renal glomerular podocyte foot processes. We explored the mechanism(s) by which CLIC5A regulates ezrin…
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