Kir2.1

Last updated
KCNJ2
Protein KCNJ2 PDB 1u4f.png
Identifiers
Aliases KCNJ2 , ATFB9, HHBIRK1, HHIRK1, IRK1, KIR2.1, LQT7, SQT3, potassium voltage-gated channel subfamily J member 2, potassium inwardly rectifying channel subfamily J member 2
External IDs OMIM: 600681 MGI: 104744 HomoloGene: 20249 GeneCards: KCNJ2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000891

NM_008425

RefSeq (protein)

NP_000882

NP_032451

Location (UCSC) Chr 17: 70.17 – 70.18 Mb Chr 11: 110.96 – 110.97 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

The Kir2.1 inward-rectifier potassium channel is a lipid-gated ion channel encoded by the KCNJ2 gene. [5] [6] [7] [8]

Contents

Clinical significance

A defect in this gene is associated with Andersen-Tawil syndrome. [9]

A mutation in the KCNJ2 gene has also been shown to cause short QT syndrome. [10]

In research

In neurogenetics, Kir2.1 is used in Drosophila research to inhibit neurons, as overexpression of this channel will hyperpolarize cells.

In optogenetics, a trafficking sequence from Kir2.1 has been added to halorhodopsin to improve its membrane localization. The resulting protein eNpHR3.0 is used in optogenetic research to inhibit neurons with light. [11]

Expression of Kir2.1 gene in human HEK293 cells induce a transient outward current, creating a steady membrane potential close to the reversal potential of potassium. [12]

Interactions

Kir2.1 has been shown to interact with:

Related Research Articles

<span class="mw-page-title-main">Andersen–Tawil syndrome</span> Rare autosomal dominant genetic disorder

Andersen–Tawil syndrome, also called Andersen syndrome and long QT syndrome 7, is a rare genetic disorder affecting several parts of the body. The three predominant features of Andersen–Tawil syndrome include disturbances of the electrical function of the heart characterised by an abnormality seen on an electrocardiogram and a tendency to abnormal heart rhythms, physical characteristics including low-set ears and a small lower jaw, and intermittent periods of muscle weakness known as hypokalaemic periodic paralysis.

<span class="mw-page-title-main">ROMK</span> Potassium channel

The renal outer medullary potassium channel (ROMK) is an ATP-dependent potassium channel (Kir1.1) that transports potassium out of cells. It plays an important role in potassium recycling in the thick ascending limb (TAL) and potassium secretion in the cortical collecting duct (CCD) of the nephron. In humans, ROMK is encoded by the KCNJ1 gene. Multiple transcript variants encoding different isoforms have been found for this gene.

<span class="mw-page-title-main">Inward-rectifier potassium channel</span> Group of transmembrane proteins that passively transport potassium ions

Inward-rectifier potassium channels (Kir, IRK) are a specific lipid-gated subset of potassium channels. To date, seven subfamilies have been identified in various mammalian cell types, plants, and bacteria. They are activated by phosphatidylinositol 4,5-bisphosphate (PIP2). The malfunction of the channels has been implicated in several diseases. IRK channels possess a pore domain, homologous to that of voltage-gated ion channels, and flanking transmembrane segments (TMSs). They may exist in the membrane as homo- or heterooligomers and each monomer possesses between 2 and 4 TMSs. In terms of function, these proteins transport potassium (K+), with a greater tendency for K+ uptake than K+ export. The process of inward-rectification was discovered by Denis Noble in cardiac muscle cells in 1960s and by Richard Adrian and Alan Hodgkin in 1970 in skeletal muscle cells.

K<sub>ir</sub>6.2 Protein-coding gene in the species Homo sapiens

Kir6.2 is a major subunit of the ATP-sensitive K+ channel, a lipid-gated inward-rectifier potassium ion channel. The gene encoding the channel is called KCNJ11 and mutations in this gene are associated with congenital hyperinsulinism.

<span class="mw-page-title-main">DLG4</span> Mammalian protein found in Homo sapiens

PSD-95 also known as SAP-90 is a protein that in humans is encoded by the DLG4 gene.

<span class="mw-page-title-main">KCNJ6</span> Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 2 is a protein that in humans is encoded by the KCNJ6 gene. Mutation in KCNJ6 gene has been proposed to be the cause of Keppen-Lubinsky Syndrome (KPLBS).

<span class="mw-page-title-main">KCNJ4</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 4, also known as KCNJ4 or Kir2.3, is a human gene.

<span class="mw-page-title-main">KCNJ8</span> Protein-coding gene in humans

Potassium inwardly-rectifying channel, subfamily J, member 8, also known as KCNJ8, is a human gene encoding the Kir6.1 protein. A mutation in KCNJ8 has been associated with cardiac arrest in the early repolarization syndrome.

<span class="mw-page-title-main">KCNJ5</span> Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 4(GIRK-4) is a protein that in humans is encoded by the KCNJ5 gene and is a type of G protein-gated ion channel.

<span class="mw-page-title-main">KCNJ12</span> Protein-coding gene in the species Homo sapiens

ATP-sensitive inward rectifier potassium channel 12 is a lipid-gated ion channel that in humans is encoded by the KCNJ12 gene.

<span class="mw-page-title-main">KCNJ3</span> Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 1(GIRK-1) is encoded in the human by the gene KCNJ3.

<span class="mw-page-title-main">KCNJ10</span> Protein-coding gene in the species Homo sapiens

ATP-sensitive inward rectifier potassium channel 10 is a protein that in humans is encoded by the KCNJ10 gene.

<span class="mw-page-title-main">KCNJ15</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 15, also known as KCNJ15 is a human gene, which encodes the Kir4.2 protein.

<span class="mw-page-title-main">LIN7A</span> Protein-coding gene in humans

Lin-7 homolog A is a protein that in humans is encoded by the LIN7A gene.

<span class="mw-page-title-main">LIN7B</span> Protein-coding gene in humans

Lin-7 homolog B is a protein that in humans is encoded by the LIN7B gene.

<span class="mw-page-title-main">KCNJ16</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 16 (KCNJ16) is a human gene encoding the Kir5.1 protein.

<span class="mw-page-title-main">KCNJ14</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 14 (KCNJ14), also known as Kir2.4, is a human gene.

<span class="mw-page-title-main">KCNJ9</span> Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 3 is a protein that in humans is encoded by the KCNJ9 gene.

<span class="mw-page-title-main">KCNJ13</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 13 (KCNJ13) is a human gene encoding the Kir7.1 protein.

The Kir2.6 also known as inward rectifier potassium channel 18 is a protein that in humans is encoded by the KCNJ18 gene. Kir2.6 is an inward-rectifier potassium ion channel.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000123700 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041695 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Hansen SB (May 2015). "Lipid agonism: The PIP2 paradigm of ligand-gated ion channels". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1851 (5): 620–8. doi:10.1016/j.bbalip.2015.01.011. PMC   4540326 . PMID   25633344.
  6. Raab-Graham KF, Radeke CM, Vandenberg CA (1994). "Molecular cloning and expression of a human heart inward rectifier potassium channel". NeuroReport. 5 (18): 2501–5. doi:10.1097/00001756-199412000-00024. PMID   7696590.
  7. Derst C, Karschin C, Wischmeyer E, Hirsch JR, Preisig-Müller R, Rajan S, Engel H, Grzeschik K, Daut J, Karschin A (2001). "Genetic and functional linkage of Kir5.1 and Kir2.1 channel subunits". FEBS Lett. 491 (3): 305–11. doi:10.1016/S0014-5793(01)02202-5. PMID   11240146. S2CID   14452157.
  8. Kubo Y, Adelman JP, Clapham DE, Jan LY, Karschin A, Kurachi Y, Lazdunski M, Nichols CG, Seino S, Vandenberg CA (2005). "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels". Pharmacol. Rev. 57 (4): 509–26. doi:10.1124/pr.57.4.11. PMID   16382105. S2CID   11588492.
  9. Donaldson MR, Yoon G, Fu YH, Ptacek LJ (2004). "Andersen-Tawil syndrome: a model of clinical variability, pleiotropy, and genetic heterogeneity". Ann. Med. 36 (Suppl 1): 92–7. doi:10.1080/17431380410032490. PMID   15176430. S2CID   7362563.
  10. Priori SG, Pandit SV, Rivolta I, Berenfeld O, Ronchetti E, Dhamoon A, Napolitano C, Anumonwo J, di Barletta MR, Gudapakkam S, Bosi G, Stramba-Badiale M, Jalife J (April 2005). "A novel form of short QT syndrome (SQT3) is caused by a mutation in the KCNJ2 gene". Circ. Res. 96 (7): 800–7. doi: 10.1161/01.RES.0000162101.76263.8c . PMID   15761194.
  11. Gradinaru V, Zhang F, Ramakrishnan C, Mattis J, Prakash R, Diester I, Goshen I, Thompson KR, Deisseroth K (April 2010). "Molecular and cellular approaches for diversifying and extending optogenetics". Cell. 141 (1): 154–65. doi:10.1016/j.cell.2010.02.037. PMC   4160532 . PMID   20303157.
  12. Zhang D, Lau C, Li G (2009-04-01). "Human Kir2.1 channel carries a transient outward potassium current with inward rectification". Pflügers Archiv: European Journal of Physiology. 457 (6): 1275–1285. doi:10.1007/s00424-008-0608-0. ISSN   1432-2013. PMID   19002489. S2CID   3120804.
  13. Nehring RB, Wischmeyer E, Döring F, Veh RW, Sheng M, Karschin A (2000). "Neuronal inwardly rectifying K(+) channels differentially couple to PDZ proteins of the PSD-95/SAP90 family". J. Neurosci. 20 (1): 156–62. doi:10.1523/JNEUROSCI.20-01-00156.2000. PMC   6774109 . PMID   10627592.
  14. Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. doi:10.1523/JNEUROSCI.19-18-07770.1999. PMC   6782450 . PMID   10479680.
  15. Grishin A, Li H, Levitan ES, Zaks-Makhina E (2006). "Identification of gamma-aminobutyric acid receptor-interacting factor 1 (TRAK2) as a trafficking factor for the K+ channel Kir2.1". J. Biol. Chem. 281 (40): 30104–11. doi: 10.1074/jbc.M602439200 . PMID   16895905.

Further reading