Cytoskeletal keratin glycosylation protects epithelial tissue from injury

@article{Ku2010CytoskeletalKG,
  title={Cytoskeletal keratin glycosylation protects epithelial tissue from injury},
  author={Nam-On Ku and D M Toivola and Pavel Strnad and M. Bishr Omary},
  journal={Nature Cell Biology},
  year={2010},
  volume={12},
  pages={876-885}
}
Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia. Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis. K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49. We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18–Gly−), and… CONTINUE READING
45 Citations
50 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 45 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 50 references

implications for multiple signaling pathways

  • Q. Zeidan, Hart, G. W. The intersections between O‐GlcNAcylation, phosphoryla‐ tion
  • J. Cell Sci. 123, 13–22
  • 2010

race and ethnic associations

  • Strnad, P. et al. Keratin variants predispose acute liver failure, adverse outcome
  • Gastroenterology 139, 828–835
  • 2010

Similar Papers

Loading similar papers…