@article{WalterCastroVossetal.2009,
  author    = {Walter, Juliane K. and Castro, Victor Manuel and Voss, Martin and Gast, Klaus and Rueckert, Christine and Piontek, J{\"o}rg and Blasig, Ingolf E.},
  title     = {Redox-sensitivity of the dimerization of occludin},
  issn      = {1420-682X},
  doi       = {10.1007/s00018-009-0150-z},
  year      = {2009},
  abstract  = {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 were detected. Masking the sulfhydryl residues in the domain prevented the dimerization but affected neither its helical structure nor cylindric shape. Incubation of cell extracts containing full-length occludin with sulfhydryl reagents prevented the dimerization; a cysteine/alanine exchange mutant also did not show dimer formation. This demonstrates, for the first time, that disulfide bridge formation of the domain is involved in the occludin dimerization. It is concluded that the redox-dependent dimerization of occludin may play a regulatory role in the tight junction assembly under physiological and pathological conditions.},
  language  = {en}
}
@article{BlasigWinklerLassowskietal.2006,
  author    = {Blasig, Ingolf E. and Winkler, Lars and Lassowski, Birgit and M{\"u}ller, Sandra L. and Zuleger, Nikolaj and Krause, Eberhard and Krause, Gerd and Gast, Klaus and Kolbe, Michael and Piontek, J{\"o}rg},
  title     = {On the self-association potential of transmembrane tight junction proteins},
  issn      = {1420-682X},
  doi       = {10.1007/s00018-005-5472-x},
  year      = {2006},
  abstract  = {Tight junctions seal intercellular clefts via membrane-related strands, hence, maintaining important organ functions. We investigated the self-association of strand-forming transmembrane tight junction proteins. The regulatory tight junction protein occludin was differently tagged and cotransfected in eucaryotic cells. These occludins colocalized within the plasma membrane of the same cell, coprecipitated and exhibited fluorescence resonance energy transfer. Differently tagged strand-forming claudin-5 also colocalized in the plasma membrane of the same cell and showed fluorescence resonance energy transfer. This demonstrates self-association in intact cells both of occludin and claudin-5 in one plasma membrane. In search of dimerizing regions of occludin, dimerization of its cytosolic C-terminal coiled-coil domain was identified. In claudin-5, the second extracellular loop was detected as a dimer. Since the transmembrane junctional adhesion molecule also is known to dimerize, the assumption that homodimerization of transmembrane tight junction proteins may serve as a common structural feature in tight junction assembly is supported},
  language  = {en}
}