High impact information on KCNV1

• Although Kv8.1 has the hallmarks of functional subunits of outward rectifier K+ channels, injection of its cRNA in Xenopus oocytes does not produce K+ currents [1].
• The Kv8.1 gene is in the 8q22.3-8q24.1 region of the human genome [1].
• Present results indicate that Kv8.1 when expressed at low concentrations acts as a modifier of Kv2.1 and Kv2.2 activity, while when expressed at high concentrations in oocytes it completely abolishes Kv2.1, Kv2.2, or Kv3.4 K+ channel activity [2].
• In these cells, Kv8.1 expressed alone remains in intracellular compartments, but it can reach the plasma membrane when it associates with Kv2.2, and it then also forms new types of Kv8.1/Kv2 [2].
• The present study investigated the molecular structure of KCNV1 [3].

Biological context of KCNV1

• The gene for Kv8.1 (KCNV1) maps onto chromosome 8q23.3, a locus for benign adult familial myoclonic epilepsy [3].
• In this study, we identified the sequence of human cDNA encoding Kv8.1, a neuronal modulatory alpha-subunit of the voltage-gated potassium channel, mapped to human chromosome 8q22.3-8q24 [4].
• 1. Human Kv8.1 cDNA had a 1,500-nucleotide open reading frame encoding a polypeptide of 500 amino acids, in which six hydrophobic transmembrane segments were well conserved, and its overall amino acids homology as compared with those of rat and golden hamster was 95.0% and 95.0% [4].

Anatomical context of KCNV1

• Despite sequence identity with other K(+) channel genes, KCNV1 does not display K(+) channel activity when expressed in Xenopus oocytes, instead inhibiting activity of Kv2 and Kv3 channels [3].

Other interactions of KCNV1

• The same effects have been seen by coexpressing the Kv8.1 subunit and the Kv2.2 subunit in COSm6 cells [2].

Analytical, diagnostic and therapeutic context of KCNV1

• Immunoprecipitation studies have demonstrated that inhibition occurs by formation of heteropolymeric channels, and results obtained with Kv8.1 chimeras have indicated that association of Kv8.1 with other types of subunits is via its N-terminal domain [1].

References