Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.

@article{Rajan2002InteractionW1,
  title={Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.},
  author={Sindhu K. Rajan and Regina Preisig-m{\"u}ller and Erhard Wischmeyer and Ralf B. Nehring and Peter J. Hanley and Vijay Renigunta and Boris Musset and G{\"u}nter Schlichth{\"o}rl and Christian Derst and Andreas Karschin and J{\"u}rgen Daut},
  journal={The Journal of physiology},
  year={2002},
  volume={545 1},
  pages={
          13-26
        }
}
The two-pore-domain potassium channels TASK-1, TASK-3 and TASK-5 possess a conserved C-terminal motif of five amino acids. Truncation of the C-terminus of TASK-1 strongly reduced the currents measured after heterologous expression in Xenopus oocytes or HEK293 cells and decreased surface membrane expression of GFP-tagged channel proteins. Two-hybrid analysis showed that the C-terminal domain of TASK-1, TASK-3 and TASK-5, but not TASK-4, interacts with isoforms of the adapter protein 14-3-3. A… CONTINUE READING

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