title: Slow inactivation conserved in heteromultimeric voltage-dependent K+ channels between Shaker (Kv1) and Shaw (Kv3) subfamilies.
abstract: 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.
authors.affiliation: Department of Biophysics, Kanazawa University School of Medicine, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Shahidullah
authors.forename: N
authors.initials: N
authors.lastname: Hoshi
authors.forename: S
authors.initials: S
authors.lastname: Yokoyama
authors.forename: T
authors.initials: T
authors.lastname: Kawamura
authors.forename: H
authors.initials: H
authors.lastname: Higashida
mesh_terms: 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
chemical_list: 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