Introduction of KCNV2
KCNV2, the full name of which is potassium voltage-gated channel subfamily V member 2, is encoded by the KCNV2 gene in humans. This potassium channel subunit does not form functional channels by itself. It modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Lots of researches have demonstrated that variations in KCNV2 have been reported to be associated with retinal dysfunction.
|Basic Information of KCNV2|
|Protein Name||Potassium voltage-gated channel subfamily V member 2|
|Aliases||Voltage-gated potassium channel subunit Kv8.2|
|Organism||Homo sapiens (Human)|
Function of KCNV2 Membrane Protein
KCNV2 is a potassium channel which is also known as Kv8.2. It belongs to electrically silent KvS subunits. The expression is restricted in testis. This potassium channel subunit does not form functional channels 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 modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Common variations in KCNV2 have been reported to be associated with retinal dysfunction. The structure and function are both complicated for this channel. The various functions not only include neuronal excitability, regulating neurotransmitter release, but also include insulin secretion, heart rate, epithelial electrolyte transport, smooth muscle contraction, and cell volume. The subunit of this channel is known as a silent subunit. Furthermore, KCNV2 displays its role in function-altering effect on other K+ channel subunits.
Fig.1 Topological scheme of hKv8.2 (Smith, 2012)
Application of KCNV2 Membrane Protein in Literature
This article shows that Kv8.2 subunit interacts with different Kv2 channels to induce potassium currents with different functional properties. It also indicates that mutations in KCNV2 are the cause of retinal dysfunction in patients.
This article suggests that KCNA1, KCNA2, and KCNV2 variants may not be involved in the risk/drug resistance of GGEs.
This study shows that two-pore mutations in KCNV2 can result in the formation of nonconducting heteromeric Kv2.1/Kv8.2 channels. The mutations prevent heteromer generation and lead to the formation of homomeric Kv2.1 channels only.
This article shows that KCNV2 mutations cause a unique form of retinal disorder illustrating the importance of K(+)-channels for the resting potential, activation and deactivation of photoreceptors, while phototransduction remains unchanged.
This article demonstrates that the transcriptional regulation of Kcnv2 and Kv2.1 is a way through which the retinal clock system drives the functional adaptation of visual function to the marked daily changes in environmental lighting conditions.
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