Structural determinants of M-type KCNQ (Kv7) K+ channel assembly.

@article{Schwake2006StructuralDO,
  title={Structural determinants of M-type KCNQ (Kv7) K+ channel assembly.},
  author={Michael Schwake and Despina Athanasiadu and Christian Beimgraben and Judith Blanz and Christian Beck and Thomas J Jentsch and Paul Saftig and Thomas Friedrich},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2006},
  volume={26 14},
  pages={3757-66}
}
The ability of KCNQ (Kv7) channels to form hetero-oligomers is of high physiological importance, because heteromers of KCNQ3 with KCNQ2 or KCNQ5 underlie the neuronal M-current, which modulates neuronal excitability. In KCNQ channels, we recently identified a C-terminal subunit interaction (si) domain that determines their subunit-specific assembly. Within this si domain, there are two motifs that comprise approximately 30 amino acid residues each and that exhibit a high probability for coiled… CONTINUE READING

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