Inwardly rectifying potassium channels: Their structure, function, and physiological roles

Hiroshi Hibino, Atsushi Inanobe, Kazuharu Furutani, Shingo Murakami, Ian Findlay, Yoshihisa Kurachi

Research output: Contribution to journalReview article

787 Scopus citations

Abstract

Inwardly rectifying K+ (Kir) channels allow K+ to move more easily into rather than out of the cell. They have diverse physiological functions depending on their type and their location. There are seven Kir channel subfamilies that can be classified into four functional groups: classical Kir channels (Kir2.x) are constitutively active, G protein-gated Kir channels (Kir3.x) are regulated by G protein-coupled receptors, ATP-sensitive K+ channels (Kir6.x) are tightly linked to cellular metabolism, and K+ transport channels (Kir1.x, Kir4.x, Kir5.x, and Kir7.x). Inward rectification results from pore block by intracellular substances such as Mg2+ and polyamines. Kir channel activity can be modulated by ions, phospholipids, and binding proteins. The basic building block of a Kir channel is made up of two transmembrane helices with cytoplasmic NH2 and COOH termini and an extracellular loop which folds back to form the pore-lining ion selectivity filter. In vivo, functional Kir channels are composed of four such subunits which are either homo- or heterotetramers. Gene targeting and genetic analysis have linked Kir channel dysfunction to diverse pathologies. The crystal structure of different Kir channels is opening the way to understanding the structure-function relationships of this simple but diverse ion channel family.

Original languageEnglish (US)
Pages (from-to)291-366
Number of pages76
JournalPhysiological Reviews
Volume90
Issue number1
DOIs
StatePublished - Jan 29 2010
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)
  • Physiology
  • Molecular Biology
  • Physiology (medical)

Fingerprint Dive into the research topics of 'Inwardly rectifying potassium channels: Their structure, function, and physiological roles'. Together they form a unique fingerprint.

  • Cite this

    Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y. (2010). Inwardly rectifying potassium channels: Their structure, function, and physiological roles. Physiological Reviews, 90(1), 291-366. https://doi.org/10.1152/physrev.00021.2009