KCNMB1 Membrane Protein Introduction

Introduction of KCNMB1

KCNMB1 is encoded by the KCNMB1 gene which is located on the chromosome 5q34 in humans. And the molecular mass of KCNMB1 is about 21 kDa. It is highly expressed in smooth muscle, but relatively low in other tissues. Relatively high levels found in corpus callosum and hippocampus. KCNMB1 belongs to the KCNMB1 subfamily. Structurally, KCNMB1 contains several transmembrane helixes, and it is a multi-pass membrane protein.

Function of KCNMB1 Membrane Protein

KCNMB1 is a calcium-activated potassium channel subunit in human. And it is a regulatory subunit of the KCNMA1, which is a calcium-activated potassium channel. KCNMB1 plays an important role in regulating the Ca²⁺ sensitivity and modulating the gating kinetics of KCNMA1. KCNMB1 is associated with pharmacological properties, and functions as a negative regulator of smooth muscle contraction. Of course, KCNMB1 itself owns potassium channel regulator activity. At the same time, KCNMB1 also takes part in many other biological processes, such as cellular response to bile acid, positive regulation of blood vessel diameter, positive regulation of potassium ion transmembrane transport and even aging. Besides, the mutation of KCNMB1 has an impact on the severity of diastolic hypertension which is a universal risk factor for cardiovascular diseases. According to the article published in 2011, hypoxia increases KCNMB1 level in human pulmonary artery smooth muscle cells. KCNMB1 can response to bile acid, ethanol and hypoxia in vivo.

Fig.1 The action of ethanol on slo1 versus heteromeric slo1 + β1 channels. (Kuntamallappanavar, 2017)

Application of KCNMB1 Membrane Protein in Literature

1. Kuntamallappanavar G. and Dopico A.M. BK β1 subunit-dependent facilitation of ethanol inhibition of BK current and cerebral artery constriction is mediated by the β1 transmembrane domain 2. Br J Pharmacol. 2017, 174(23):4430-4448. PubMed ID: 28940182
   
   

   The authors in this article reveal that BK β1 subunit (also named KCNMB1) but not β4 subunit mediates the ethanol inhibition of BK current, furthermore, β1 TM2 itself but not other β regions are necessary for ethanol-induced cerebral artery constriction.

2. Ahn Y.T., et al. Hypoxia-inducible factor-1α regulates KCNMB1 expression in human pulmonary artery smooth muscle cells. Am J Physiol Lung Cell Mol Physiol. 2011, 302(3): L352-9. PubMed ID: 22114151
   
   

   According to the previous finding, hypoxia increases the expression of KCNMB1 in the calcium-sensitive potassium channel, and the authors in this article reveal the mechanism of the phenomenon. Besides KCNMB1, the expression of another transcriptional factor, hypoxia-inducible factor 1-α (HIF-1α), is also found to be increased in human pulmonary artery smooth muscle cells.

3. Grimm P.R., et al. Hypertension of Kcnmb1^-/- is linked to deficient K secretion and aldosteronism. Proc Natl Acad Sci U S A. 2009, 106(28):11800-5. PubMed ID: 19556540
   
   

   Through a mouse model with deletions of KCNMB1, the authors in this article find that most of the hypertension of KCNMB1^-/- is due to aldosteronism, resulting from renal potassium retention and hyperkalemia. By the way, it has been revealed that KCNMB1^-/- mice are hypertensive, volume expanded, and have reduced urinary K⁺ and Na⁺ clearances.

4. Chen Y., et al. Common charge-shift mutation Glu65Lys in K⁺ channel β_₁-Subunit KCNMB1: pleiotropic consequences for glomerular filtration rate and progressive renal disease. Am J Nephrol. 2010, 32(5):414-24. PubMed ID: 20861615
   
   

   This article reveals that the Glu65Lys mutation of KCNMB1 is associated with glomerular filtration rate (GFR) which is a heritable trait. Profiling patients with Glu65Lys is much easier to gauge renal prognosis and select rational therapy.

5. Fernández-Fernández., et al. Gain-of-function mutation in the KCNMB1 potassium channel subunit is associated with low prevalence of diastolic hypertension. Journal of Clinical Investigation. 2004, 113(7):1032-9. PubMed ID: 15057310
   
   

   Authors in this article find an E65K mutation in KCNMB1, which is related to the increased Ca²⁺ sensitivity. And the mutation influences diastolic hypertension. This result may contribute to the treatment of cardiovascular diseases.

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Reference

1. Kuntamallappanavar G and Dopico A M. (2017). BK β1 subunit-dependent facilitation of ethanol inhibition of BK current and cerebral artery constriction is mediated by the β1 transmembrane domain 2. British journal of pharmacology. 174(23): 4430-4448.

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