Redox-sensitivity of the dimerization of occludin

@article{Walter2009RedoxsensitivityOT,
  title={Redox-sensitivity of the dimerization of occludin},
  author={Juliane K Walter and Victor Gonzalez Castro and Martin H Voss and Klaus Gast and Christine Rueckert and J{\"o}rg Piontek and Ingolf E Blasig},
  journal={Cellular and Molecular Life Sciences},
  year={2009},
  volume={66},
  pages={3655-3662}
}
Occludin is a self-associating transmembrane tight junction protein affected in oxidative stress. However, its function is unknown. The cytosolic C-terminal tail contains a coiled coil-domain forming dimers contributing to the self-association. Studying the hypothesis that the self-association is redox-sensitive, we found that the dimerization of the domain depended on the sulfhydryl concentration of the environment in low-millimolar range. Under physiological conditions, monomers and dimers… CONTINUE READING

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