KCNV1 Membrane Protein Introduction

Introduction of KCNV1

KCNV1, potassium voltage-gated channel subfamily V member 1, is a protein that in humans is encoded by the KCNV1 gene. This potassium channel subunit cannot form functional channel by itself. It can modulate KCNB1 and KCNB2 channel activity by shifting the threshold for inactivation to more negative values and by slowing the rate of inactivation. Common variations in KCNV1 have been reported to be associated with schizophrenia.

Basic Information of KCNV1
Protein Name Potassium voltage-gated channel subfamily V member 1
Gene Name KCNV1
Aliases Neuronal potassium channel alpha subunit HNKA, Voltage-gated potassium channel subunit Kv8.1
Organism Homo sapiens (Human)
UniProt ID Q6PIU1
Transmembrane Times 6
Length (aa) 500

Function of KCNV1 Membrane Protein

KCNV1 is a potassium channel which is also known as Kv8.1. It belongs to electrically silent KvS subunits and its expression is limited in the brain. This potassium channel subunit does not form functional channel by itself. It can form functional heterotetrametric Kv2/KvS channels which possess unique biophysical properties and display a more tissue-specific expression pattern, making them more desirable pharmacological and therapeutic targets. It can modulate KCNB1 and KCNB2 channel activity by shifting the threshold for inactivation to more negative values and by slowing the rate of inactivation. It can down-regulate the channel activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in intracellular membranes. Common variations in KCNV1 have been reported to be associated with schizophrenia. Moreover, Kv8.1 plays function through its N-terminal domain by interacting with other subunits. Except for these functions, Kv8.1 can specifically inhibit Shab and Shaw channels. Furthermore, the various functions include neuronal excitability, regulating neurotransmitter release, insulin secretion, heart rate, epithelial electrolyte transport, smooth muscle contraction, and cell volume.

Subfamily-specific assembly into functional Kv channels Fig.1 Subfamily-specific assembly into functional Kv channels (Bocksteins, 2016)

Application of KCNV1 Membrane Protein in Literature

  1. Stas J.I., et al. Modulation of Closed-State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4-AP Induced Potentiation. PLoS One. 2015, 10(10):e0141349. PubMed ID: 26505474

    This article shows that the different activities of Kv2 and homotetramers’ currents, and demonstrates that Kv5.1, Kv8.1 and Kv9.3 currents are inhibited differently by the channel blocker 4-AP.

  2. Bocksteins E., et al. Kv2.1 and silent Kv subunits underlie the delayed rectifier K+ current in cultured small mouse DRG neurons. Am J Physiol Cell Physiol. 2009, 296(6):C1271-8. PubMed ID: 19357235

    This article reports that Kv subunits have different physiological roles in small DRG neurons.

  3. Ebihara M., et al. Structural characterization and promoter analysis of human potassium channel Kv8.1 (KCNV1) gene. Gene. 2004, 325:89-96. PubMed ID: 14697513

    This study investigates the molecular structure of KCNV1, and indicates the structural characterization and promoter analysis of human KCNV1 gene. It provides useful information in developing KCNV1 screening for epileptic disease.

  4. Salinas M., et al. Modes of regulation of shab K+ channel activity by the Kv8.1 subunit. J Biol Chem. 1997, 272(13):8774-80. PubMed ID: 9079713

    This article reveals that Kv8.1 displays different channel activities under different concentrations. The S6 segment of Kv8.1 contributes to the activity modulation of Kv2 channels.

  5. Hugnot J.P., et al. Kv8.1, a new neuronal potassium channel subunit with specific inhibitory properties towards Shab and Shaw channels. EMBO J. 1996, 15(13):3322-31. PubMed ID: 8670833

    This article indicates that the association of Kv8.1 with other types of subunits is via its N-terminal domain.

KCNV1 Preparation Options

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  1. Bocksteins E, et al. (2016). Kv5, Kv6, Kv8, and Kv9 subunits: No simple silent bystanders. J Gen Physiol. 147(2):105-25.

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