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 language | English (US) |
|---|---|
| Pages (from-to) | 291-366 |
| Number of pages | 76 |
| Journal | Physiological Reviews |
| Volume | 90 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 29 2010 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Medicine(all)
- Physiology
- Molecular Biology
- Physiology (medical)
Cite this
Inwardly rectifying potassium channels : Their structure, function, and physiological roles. / Hibino, Hiroshi; Inanobe, Atsushi; Furutani, Kazuharu; Murakami, Shingo; Findlay, Ian; Kurachi, Yoshihisa.
In: Physiological Reviews, Vol. 90, No. 1, 29.01.2010, p. 291-366.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Inwardly rectifying potassium channels
T2 - Their structure, function, and physiological roles
AU - Hibino, Hiroshi
AU - Inanobe, Atsushi
AU - Furutani, Kazuharu
AU - Murakami, Shingo
AU - Findlay, Ian
AU - Kurachi, Yoshihisa
PY - 2010/1/29
Y1 - 2010/1/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=74949143771&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=74949143771&partnerID=8YFLogxK
U2 - 10.1152/physrev.00021.2009
DO - 10.1152/physrev.00021.2009
M3 - Review article
C2 - 20086079
AN - SCOPUS:74949143771
VL - 90
SP - 291
EP - 366
JO - Physiological Reviews
JF - Physiological Reviews
SN - 0031-9333
IS - 1
ER -