Cloning and expression of a human voltage-gated potassium channel. A novel 
member of the RCK potassium channel family.

Grupe, A.; Schroter, K. H.; Ruppersberg, J. P.; Stocker, M.; Drewes, T.; Beckh, S.; Pongs, O.

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Cloning and expression of a human voltage-gated potassium channel. A novel member of the RCK potassium channel family.

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Beckh, S.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Pongs, O.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Grupe, A., Schroter, K. H., Ruppersberg, J. P., Stocker, M., Drewes, T., Beckh, S., et al. (1990). Cloning and expression of a human voltage-gated potassium channel. A novel member of the RCK potassium channel family. EMBO Journal, 9(6), 1749-1756.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-0DB8-9

Abstract

We have isolated and characterized a human cDNA (HBK2) that is homologous to novel member (RCK2) of the K+ channel RCK gene family expressed in rat brain. RCK2 mRNA was detected predominantly in midbrain areas and brainstem. The primary sequences of the HBK2/RCK2 K+ channel proteins exhibit major differences to other members of the RCK gene family. The bend region between segments S1 and S2 is unusually long and does not contain the N-glycosylation site commonly found in this region. They might be O-glycosylated instead. Functional characterization of the HBK2/RCK2 K+ channels in Xenopus laevis oocytes following micro-injection in in vitro transcribed HBK2 or RCK2 cRNA showed that the HBK2/RCK2 proteins form voltage-gated K+ channels with novel functional and pharmacological properties. These channels are different to RCK1, RCK3, RCK4 and RCK5 K+ channels.