Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR.

@article{Stevers2016CharacterizationAS,
  title={Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR.},
  author={Loes M. Stevers and Chan Vinh Lam and Seppe Leysen and Femke A. Meijer and Daphne S van Scheppingen and Rens M J M de Vries and Graeme W. Carlile and Lech G Milroy and David Y. Thomas and Luc Brunsveld and Christian Ottmann},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 9},
  pages={
          E1152-61
        }
}
  • Loes M. Stevers, Chan Vinh Lam, +8 authors Christian Ottmann
  • Published in
    Proceedings of the National…
    2016
  • Medicine, Biology
  • Cystic fibrosis is a fatal genetic disease, most frequently caused by the retention of the CFTR (cystic fibrosis transmembrane conductance regulator) mutant protein in the endoplasmic reticulum (ER). The binding of the 14-3-3 protein to the CFTR regulatory (R) domain has been found to enhance CFTR trafficking to the plasma membrane. To define the mechanism of action of this protein-protein interaction, we have examined the interaction in vitro. The disordered multiphosphorylated R domain… CONTINUE READING

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    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 55 REFERENCES

    Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis

    VIEW 8 EXCERPTS
    HIGHLY INFLUENTIAL

    Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3.

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