Kv6.2
Description: potassium voltage-gated channel, subfamily G, member 2 Gene: Kcng2 Alias: Kv6.2, kcng2
Kv6.2, encoded by the gene KCNG2, is a member is a gamma subunit of the voltage-gated potassium channel, subfamily G. Kv6.2 is thought to be a delayed-rectifier type channels that may contribute to cardiac action potential repolarization. NCBI
Experimental data
Rat Kv6.2 gene in CHO host cells |
||
Click for details 15 °Cshow 61 cells |
Click for details 25 °Cshow 57 cells |
Click for details 35 °Cshow 84 cells |
Gene
Transcript
Species | NCBI accession | Length (nt) | |
---|---|---|---|
Human | NM_012283.2 | 1876 | |
Mouse | NM_001190373.1 | 2815 | |
Rat | NM_001107372.1 | 1838 |
Protein Isoforms
Isoforms
Post-Translational Modifications
Visual Representation of Kv6.2 Structure
Methodology for visual representation of structure available here
Yeast two-hybrid reporter assays indicated that Kv6.2 amino-termini are able to interact specifically with the Kv2.1 amino-terminus. It is proposed that this protein protein interaction underlies Kv2.1/Kv6.2 subunit assembly and the expression of functional heteromultimeric Kv2.1/Kv6.2 channels. [661]
Kv6.2 predicted AlphaFold size
Methodology for AlphaFold size prediction and disclaimer are available here
Kv6.2
Rat and human Kv6.2 subunits appear to be unable to form functional Kv channels in a heterologous expression system, but, when coexpressed with Kv2.1 alpha subunits, heteromultimeric Kv channels were formed mediating voltage-activated delayed-rectifier type outward currents. Their kinetics and conductance-voltage relationship were different from those mediated by homomultimeric Kv2.1 channels [661]
Effects of heteromerization with Kv6 subunits on the time course of inactivation of Kv2. 1 channels
Co-expression of Kv6 with Kv2.1 Subunits—Kv6.x and/or Kv2.1 subunits were expressed in CHO-K1 cells and the amplitude and kinetics of the resulting currents were analyzed with the whole cell patch-clamp technique. Expression of Kv6.1, Kv6.3, or Kv6.4 subunits alone did not produce any voltage-dependent K+ current (not illustrated), confirming that these subunits are silent. To test for possible formation of heteromeric Kv6.x/Kv2.1 channels we then co-expressed Kv6.1, Kv6.3, or Kv6.4 subunits with Kv2.1 using an IRES-based expression vector in which the transcription of both channel subunits was under the control of the same promoter. This vector induced the translation of two open reading frames from one mRNA transcript. However, the translation of the second open reading frame (Kv2.1) was about 10-fold lower than that of the first one (Kv6), which minimized the formation of homomeric Kv2.1 channels. The time course of inactivation of the heteromeric channels was much slower than that of homotetrameric Kv2.1 channels [1708]
Kv6.2 Expressed in Heart
Kv6.2 mRNA is preferentially expressed in rat and human myocard. [661]
Kv6.2 Expressed in Rat Brain
According to the Mus musculus potassium voltage-gated channel, subfamily G, member 2 (Kcng2) mRNA expression as been seen in the visual cortex NCBI
Rat and human Kv6.2 subunits appear to be unable to form functional Kv channels in a heterologous expression system, but, when coexpressed with Kv2.1 alpha subunits, heteromultimeric Kv channels were formed mediating voltage-activated delayed-rectifier type outward currents. [661]
Delayed-rectifier type channels containing Kv6.2 subunits may contribute to cardiac action potential repolarization. [661]
Kv2.1/Kv6.2 channels display submicromolar sensitivity to the antiarrhythmic drug propafenone. [661]
References
Rettig J
et al.
Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit.
Nature,
1994
May
26
, 369 (289-94).
Kramer JW
et al.
Modulation of potassium channel gating by coexpression of Kv2.1 with regulatory Kv5.1 or Kv6.1 alpha-subunits.
Am. J. Physiol.,
1998
Jun
, 274 (C1501-10).
Isacoff EY
et al.
Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes.
Nature,
1990
Jun
7
, 345 (530-4).
Jegla T
et al.
A novel subunit for shal K+ channels radically alters activation and inactivation.
J. Neurosci.,
1997
Jan
1
, 17 (32-44).
Namba N
et al.
Kir2.2v: a possible negative regulator of the inwardly rectifying K+ channel Kir2.2.
FEBS Lett.,
1996
May
20
, 386 (211-4).
Chen TY
et al.
A new subunit of the cyclic nucleotide-gated cation channel in retinal rods.
Nature,
1993
Apr
22
, 362 (764-7).
Liman ER
et al.
A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP.
Neuron,
1994
Sep
, 13 (611-21).
Bradley J
et al.
Heteromeric olfactory cyclic nucleotide-gated channels: a subunit that confers increased sensitivity to cAMP.
Proc. Natl. Acad. Sci. U.S.A.,
1994
Sep
13
, 91 (8890-4).
Biel M
et al.
Molecular cloning and expression of the Modulatory subunit of the cyclic nucleotide-gated cation channel.
J. Biol. Chem.,
1996
Mar
15
, 271 (6349-55).
Zhu XR
et al.
Structural and functional characterization of Kv6.2 a new gamma-subunit of voltage-gated potassium channel.
Recept. Channels,
1999
, 6 (337-50).
Ottschytsch N
et al.
Domain analysis of Kv6.3, an electrically silent channel.
J. Physiol. (Lond.),
2005
Nov
1
, 568 (737-47).
Contributors: Rajnish Ranjan, Michael Schartner, Katherine Johnston
To cite this page: [Contributors] Channelpedia https://channelpedia.epfl.ch/wikipages/20/ , accessed on 2024 Dec 02