KCNB2 Membrane Protein Introduction

Introduction of KCNB2

KCNB2, also known as Kv2.2, is a member of the potassium channel, voltage-gated, shab-related subfamily which regulates the transportation of potassium ions across the membrane in accordance with their electrochemical gradient. KCNB2 is encoded by the KCNB2 gene and has 911 amino acid residues. KCNB2 protein contains 6 transmembrane segments (S1-S6) with a voltage-sensor in S4. The functional Kv channels are composed of 4 identical Kv2.2 to form homotetrameric channels or consist of Kv2.2 and other alpha subunits to form heterotetrameric channels.

Function of KCNB2 Membrane Protein

KCNB2 is primarily in the brain and smooth muscle cells. It functions as a delayed rectifier voltage-gated potassium channel that mediates potassium ion permeability of excitable membranes. The channels can alter its opened or closed conformations in accordance with the voltage difference across the membrane thereby controlling potassium ions pass across the membrane. It has been revealed that homotetrameric channels can regulate the outward potassium current that shows rapid activation and slow inactivation in the membrane depolarization reaction. In cortical pyramidal neurons and smooth muscle cells, KCNB2 is responsible for the delayed-rectifier voltage-gated potassium current. In gastrointestinal smooth muscles, KCNB2 regulates a slowly activating potassium current. KCNB2 is involved in the regulation of many biological processes via mediating delayed-rectifier voltage-gated potassium current. KCNB2 has been revealed the association with many neurological disorders such as schizophrenia and cognitive dysfunction. Moreover, KCNB2 can act as a therapeutic target for some diseases. For example, stromatoxin-1 (ScTx1), a selective inhibitor of K(v)2-containing channels, can regulate the excitability and contractility of human urinary bladder smooth muscle, which has been applied for the treatment of bladder dysfunction.

Fig.1 Structural determinants for the voltage sensitivity in voltage-gated K⁺ channels. (González, 2012)

Application of KCNB2 Membrane Protein in Literature

1. Hristov K.L., et al. Expression and function of K(v)2-containing channels in human urinary bladder smooth muscle. Am J Physiol Cell Physiol. 2012, 302(11): C1599-608. PubMed ID: 22422395
   
   

   The study shows that stromatoxin-1 (ScTx1), a selective inhibitor of K(v)2-containing channels, can regulate the excitability and contractility of human urinary bladder smooth muscle. K(v)2-containing channels can be regarded as the potential therapeutic targets for bladder dysfunction.

2. Regnier G., et al. The contribution of Kv2.2-mediated currents decreases during the postnatal development of mouse dorsal root ganglion neurons. Physiological Reports. 2016, pii: e12731. PubMed ID: 27033450
   
   

   The study shows that both Kv2 and KvS subunits play important roles in the postnatal maturation of dorsal root ganglion (DRG) neurons.

3. Stepanov V.A., et al. Replicative study of susceptibility to childhood-onset schizophrenia in Kazakhs. Genetika. 2015, 51(2):227-235. PubMed ID: 25966588
   
   

   The study indicates the association between early-onset schizophrenia and genetic markers in three genes (VRK2, KCNB2, and CPVL) in Kazakhs.

4. Juang J.M., et al. Disease-targeted sequencing of ion channel genes identifies de novo mutations in patients with non-familial Brugada syndrome. Sci Rep. 2014, 4:6733. PubMed ID: 25339316
   
   

   The authors identify five de novo mutations in four genes (SCNN1A, KCNJ16, KCNB2, and KCNT1) in three Brugada syndrome patients.

5. Yan L., et al. Expression of voltage-gated potassium channels in human and rhesus pancreatic islets. Diabetes. 2004, 53(3):597-607. PubMed ID: 14988243
   
   

   The results suggest that more than one Kv channel subtype may cause the beta-cell delayed rectifier current which can be formed by both active and passive heterotetramers.

KCNB2 Preparation Options

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Reference

1. González C, et al. (2012). K⁺ channels: function-structural overview. Comprehensive Physiology. 2(3): 2087-149.

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