Two-pore-domain potassium channel

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The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak channels which possess Goldman-Hodgkin-Katz (open) rectification. [1] These channels are regulated by several mechanisms including signaling lipids, oxygen tension, pH, mechanical stretch, and G-proteins. [2] Two-pore-domain potassium channels correspond structurally to a inward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of two transmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into a tetramer forming the complete channel. [3] The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together. [4]

Contents

Each single channel does not have two pores; the name of the channel comes from the fact that each subunit has two P (pore) domains in its primary sequence. [5] To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels". [6]

A decrease in these leak channels activity is known as 'channel arrest', which reduces oxygen consumption [7] and allows animals to survive anoxia [8] .

Below is a list of the 15 known two-pore-domain human potassium channels: [1]

GeneChannel [9] FamilyAliases
KCNK1 K2p1.1 TWIK [2] [10] TWIK-1
KCNK2 K2p2.1 TREK [2] [10] TREK-1
KCNK3 K2p3.1 TASK [2] [10] TASK-1
KCNK4 K2p4.1 TREK [2] [10] TRAAK [11]
KCNK5 K2p5.1 TASK [2] [10] TASK-2 [12]
KCNK6 K2p6.1 TWIK [2] [10] TWIK-2
KCNK7 K2p7.1 TWIK [2] [10]
KCNK9 K2p9.1 TASK [2] [10] TASK-3
KCNK10 K2p10.1 TREK [2] [10] TREK-2
KCNK12 K2p12.1 THIKTHIK-2
KCNK13 K2p13.1 THIKTHIK-1
KCNK15 K2p15.1 TASK [2] [10] TASK-5
KCNK16 K2p16.1 TALK [2] [10] TALK-1
KCNK17 K2p17.1 TALK [2] [10] TALK-2, TASK-4
KCNK18 K2p18.1 TRIK, TRESK [2] [10] [13] [14]
K2P1
Two-pore domain potassium channel K2P1 PDB-3ukm.png
Human K2P1 PDB: 3UKM ​
Identifiers
SymbolK2P1
HGNC 6272
RefSeq NP_002236.1
UniProt O00180
Search for
Structures Swiss-model
Domains InterPro
K2P2
Two-pore domain potassium channel K2P2 PDB-4twk.png
Human K2P2 PDB: 4TWK ​
Identifiers
SymbolK2P2
HGNC 6277
RefSeq NP_055032.1
UniProt O95069
Search for
Structures Swiss-model
Domains InterPro
K2P3
Two-pore domain potassium channel K2P3 PDB-6rv3.png
Human K2P3 PDB: 6RV3 ​
Identifiers
SymbolK2P3
HGNC 6278
RefSeq NP_002237.1
UniProt O14649
Search for
Structures Swiss-model
Domains InterPro

See also

Related Research Articles

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<span class="mw-page-title-main">Potassium channel</span> Ion channel that selectively passes K+

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<span class="mw-page-title-main">Voltage-gated ion channel</span> Type of ion channel transmembrane protein

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<span class="mw-page-title-main">Voltage-gated potassium channel</span> Class of transport proteins

Voltage-gated potassium channels (VGKCs) are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential. During action potentials, they play a crucial role in returning the depolarized cell to a resting state.

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

K+ channel tetramerisation domain is the N-terminal, cytoplasmic tetramerisation domain (T1) of voltage-gated K+ channels. It defines molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. It is distantly related to the BTB/POZ domain Pfam PF00651.

<span class="mw-page-title-main">KCNK2</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 2, also known as TREK-1, is a protein that in humans is encoded by the KCNK2 gene.

<span class="mw-page-title-main">KCNK3</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.

<span class="mw-page-title-main">KCNK1</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 1 is a protein that in humans is encoded by the KCNK1 gene.

<span class="mw-page-title-main">KCNK9</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 9 is a protein that in humans is encoded by the KCNK9 gene.

<span class="mw-page-title-main">KCNK4</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 4 is a protein that in humans is encoded by the KCNK4 gene. KCNK4 protein channels are also called TRAAK channels.

<span class="mw-page-title-main">KCNK6</span> Protein-coding gene in humans

Potassium channel subfamily K member 6 is a protein that in humans is encoded by the KCNK6 gene.

<span class="mw-page-title-main">KCNK5</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 5 is a protein that in humans is encoded by the KCNK5 gene.

<span class="mw-page-title-main">KCNK15</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 15 is a protein that in humans is encoded by the KCNK15 gene.

<span class="mw-page-title-main">KCNK17</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 17 is a protein that in humans is encoded by the KCNK17 gene.

<span class="mw-page-title-main">KCNK7</span> Protein-coding gene in the species Homo sapiens

Potassium channel, subfamily K, member 7, also known as KCNK7 or K2P7.1 is a protein which is encoded in humans by the KCNK7 gene. K2P7.1 is a potassium channel containing two pore-forming P domains. Multiple transcript variants encoding different isoforms have been found for this gene.

<span class="mw-page-title-main">KCNK10</span> Protein-coding gene in the species Homo sapiens

Potassium channel, subfamily K, member 10, also known as KCNK10 is a human gene. The protein encoded by this gene, K2P10.1, is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">KCNK13</span> Protein-coding gene in the species Homo sapiens

Potassium channel, subfamily K, member 13, also known as KCNK13 is a human gene. The protein encoded by this gene, K2P13.1 is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">KCNK16</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 16 is a protein that in humans is encoded by the KCNK16 gene. The protein encoded by this gene, K2P16.1, is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">KCNK18</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 18 (KCNK18), also known as TWIK-related spinal cord potassium channel (TRESK) or K2P18.1 is a protein that in humans is encoded by the KCNK18 gene. K2P18.1 is a potassium channel containing two pore-forming P domains.

A potassium channel opener is a type of drug which facilitates ion transmission through potassium channels.

References

  1. 1 2 Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (December 2005). "International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels". Pharmacological Reviews. 57 (4): 527–540. doi:10.1124/pr.57.4.12. PMID   16382106. S2CID   7356601.
  2. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 Enyedi P, Czirják G (April 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels". Physiological Reviews. 90 (2): 559–605. doi:10.1152/physrev.00029.2009. PMID   20393194.
  3. ↑ Doyle DA, Morais Cabral J, Pfuetzner RA, Kuo A, Gulbis JM, Cohen SL, et al. (April 1998). "The structure of the potassium channel: molecular basis of K+ conduction and selectivity". Science. 280 (5360): 69–77. Bibcode:1998Sci...280...69D. doi:10.1126/science.280.5360.69. PMID   9525859.
  4. ↑ Miller AN, Long SB (January 2012). "Crystal structure of the human two-pore domain potassium channel K2P1". Science. 335 (6067): 432–436. Bibcode:2012Sci...335..432M. doi:10.1126/science.1213274. PMID   22282804. S2CID   206537279.
  5. ↑ Baggetta AM, Bayliss DA, Czirják G, Enyedi P, Goldstein SA, Lesage F, Minor Jr DL, Plant LD, Sepúlveda F. "Two P domain potassium channels". GtoPdb v.2023.1. IUPHAR/BPS Guide to Pharmacology . Retrieved 2019-05-28.
  6. ↑ Rang HP (2003). Pharmacology (8 ed.). Edinburgh: Churchill Livingstone. p. 59. ISBN   978-0-443-07145-4.
  7. ↑ Lutz, Peter L.; Milton, Sarah L. (2004-08-15). "Negotiating brain anoxia survival in the turtle". Journal of Experimental Biology. 207 (18): 3141–3147. doi:10.1242/jeb.01056. ISSN   1477-9145.
  8. ↑ Welker, Alexis F.; Moreira, Daniel C.; Campos, Élida G.; Hermes-Lima, Marcelo (August 2013). "Role of redox metabolism for adaptation of aquatic animals to drastic changes in oxygen availability". Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 165 (4): 384–404. doi:10.1016/j.cbpa.2013.04.003. PMID   23587877.
  9. ↑ Gutman GA, Chandy KG, Adelman JP, Aiyar J, Bayliss DA, Clapham DE, et al. (December 2003). "International Union of Pharmacology. XLI. Compendium of voltage-gated ion channels: potassium channels". Pharmacological Reviews. 55 (4): 583–586. doi:10.1124/pr.55.4.9. PMID   14657415. S2CID   34963430.
  10. 1 2 3 4 5 6 7 8 9 10 11 12 13 Lotshaw DP (2007). "Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels". Cell Biochemistry and Biophysics. 47 (2): 209–256. doi:10.1007/s12013-007-0007-8. PMID   17652773. S2CID   12759521.
  11. ↑ Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M (June 1998). "A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids". The EMBO Journal. 17 (12): 3297–3308. doi:10.1093/emboj/17.12.3297. PMC   1170668 . PMID   9628867.
  12. ↑ Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (March 2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nature Reviews. Neuroscience. 2 (3): 175–184. doi:10.1038/35058574. PMID   11256078. S2CID   9682396.
  13. ↑ Sano Y, Inamura K, Miyake A, Mochizuki S, Kitada C, Yokoi H, et al. (July 2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord". The Journal of Biological Chemistry. 278 (30): 27406–27412. doi: 10.1074/jbc.M206810200 . PMID   12754259.
  14. ↑ Czirják G, Tóth ZE, Enyedi P (April 2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin". The Journal of Biological Chemistry. 279 (18): 18550–18558. doi: 10.1074/jbc.M312229200 . PMID   14981085.
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