Slow inactivation conserved in heteromultimeric voltage-dependent K+ channels between Shaker (Kv1) and Shaw (Kv3) subfamilies.
Single K+ channels were recorded under the cell-attached mode in Xenopus oocytes injected with an equal amount of mRNAs coding for NGK1 (Kv1.2) and NGK2 (Kv3.1a) voltage-dependent K+ channels. A new class of channels of 20 pS in conductance with three degrees of inactivation was observed. The results suggest that voltage-dependent NGK1 Shaker and NGK2 Shaw K+ channels, from different subfamilies, assemble to form heteromultimeric K+ channels in Xenopus oocytes and show characteristics inherited from two parental channels.
Shahidullah
M
M
Department of Biophysics, Kanazawa University School of Medicine, Japan.
Hoshi
N
N
Yokoyama
S
S
Kawamura
T
T
Higashida
H
H
D000818:Animals; D004553:Electric Conductivity; D051663:Kv1.2 Potassium Channel; D009865:Oocytes / Q000378:metabolism; D015221:Potassium Channels / Q000235:genetics / Q000378:metabolism*; D024642:Potassium Channels, Voltage-Gated; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D051637:Shaker Superfamily of Potassium Channels; D051670:Shaw Potassium Channels; D014982:Xenopus laevis
C496972:Kcna2 protein, rat; C098254:Kcnc1 protein, rat; D051663:Kv1.2 Potassium Channel; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D012333:RNA, Messenger; D051637:Shaker Superfamily of Potassium Channels; D051670:Shaw Potassium Channels