Channelpedia

Kv6.2

Description: potassium voltage-gated channel, subfamily G, member 2
Gene: Kcng2
Alias: Kv6.2, kcng2

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Introduction

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

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15 °C
show 61 cells

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25 °C
show 57 cells

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35 °C
show 84 cells
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Gene

Species NCBI gene ID Chromosome Position
Human 26251 18 102162
Mouse 240444 18 69738
Rat 307234 18 68196
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Transcript

Species NCBI accession Length (nt)
Human NM_012283.2 1876
Mouse NM_001190373.1 2815
Rat NM_001107372.1 1838
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Protein Isoforms

Species Uniprot ID Length (aa)
Human Q9UJ96 466
Mouse F7A6P6 480
Rat Q9QYU3 480

Isoforms

Transcript
Length (nt)
Protein
Length (aa)
Variant
Isoform
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Post-Translational Modifications

PTM
Position
Type
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Structure

Kv6.2
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

Species Area (Å2) Reference
Human 5920.04 source
Mouse 5802.55 source
Rat 5866.37 source

Methodology for AlphaFold size prediction and disclaimer are available here

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Kinetics

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

Kv1.1 structure 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]

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Expression and Distribution

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

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Function

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]

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Interaction

Kv2.1/Kv6.2 channels display submicromolar sensitivity to the antiarrhythmic drug propafenone. [661]

References

312

Rettig J et al. Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit.
Nature, 1994 May 26 , 369 (289-94).

649

Isacoff EY et al. Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes.
Nature, 1990 Jun 7 , 345 (530-4).

651

Jegla T et al. A novel subunit for shal K+ channels radically alters activation and inactivation.
J. Neurosci., 1997 Jan 1 , 17 (32-44).

652

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).

653

Chen TY et al. A new subunit of the cyclic nucleotide-gated cation channel in retinal rods.
Nature, 1993 Apr 22 , 362 (764-7).

655

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).

1708

Ottschytsch N et al. Domain analysis of Kv6.3, an electrically silent channel.
J. Physiol. (Lond.), 2005 Nov 1 , 568 (737-47).

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Credits

Contributors: Rajnish Ranjan, Michael Schartner, Katherine Johnston

To cite this page: [Contributors] Channelpedia https://channelpedia.epfl.ch/wikipages/20/ , accessed on 2024 Dec 30


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