Inwardly rectifying potassium channels (K<sub>IR</sub>) in GtoPdb v.2023.1

Authors

  • John P. Adelman Oregon Health & Science University https://orcid.org/0000-0002-1135-1549
  • David E. Clapham Harvard Medical School
  • Hiroshi Hibino Osaka University
  • Atsushi Inanobe Osaka University
  • Lily Y. Jan University of California San Francisco
  • Andreas Karschin University of Würzburg
  • Yoshihiro Kubo National Institute for Physiological Sciences
  • Yoshihisa Kurachi Osaka University
  • Michel Lazdunski CNRS Valbonne
  • Takashi Miki Kobe University
  • Colin G. Nichols Washington University
  • Lawrence G. Palmer Weill-Cornell Medical College
  • Wade L. Pearson Washington University
  • Henry Sackin Rosalind Franklin University
  • Susumu Seino Kobe University
  • Paul A. Slesinger Icahn School of Medicine at Mount Sinai
  • Stephen Tucker University of Oxford https://orcid.org/0000-0001-8996-2000
  • Carol A. Vandenberg University of California Santa Barbara

DOI:

https://doi.org/10.2218/gtopdb/F74/2023.1

Abstract

The 2TM domain family of K channels are also known as the inward-rectifier K channel family. This family includes the strong inward-rectifier K channels (Kir2.x) that are constitutively active, the G-protein-activated inward-rectifier K channels (Kir3.x) and the ATP-sensitive K channels (Kir6.x, which combine with sulphonylurea receptors (SUR1-3)). The pore-forming α subunits form tetramers, and heteromeric channels may be formed within subfamilies (e.g. Kir3.2 with Kir3.3).

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Published

26-Apr-2023

How to Cite

Adelman, J. P. (2023) “Inwardly rectifying potassium channels (K<sub>IR</sub>) in GtoPdb v.2023.1”, IUPHAR/BPS Guide to Pharmacology CITE, 2023(1). doi: 10.2218/gtopdb/F74/2023.1.

Issue

Vol. 2023 No. 1 (2023)

Section

Summaries