KCNMB2 Membrane Protein Introduction

Introduction of KCNMB2

KCNMB2 is encoded by the KCNMB2 gene which is located on 3q26.2-q27.1 in humans. And the molecular mass of KCNMB2 is about 27 kDa. KCNMB2 is highly expressed in the ovary, and it is found relatively high in kidney, heart and brain, but it’s expressed with low levels in other tissues. KCNMB2 belongs to the KCNMB subfamily. Structurally, KCNMB2 contains the ball and chain domain which mediates the interaction with KCNMA1. And the protein contains two transmembrane domains with intracellular N- and C-termini.

Basic Information of KCNMB2
Protein Name Calcium-activated potassium channel subunit beta-2
Gene Name KCNMB2
Aliases BK channel subunit beta-2, BKbeta2, Hbeta2, Calcium-activated potassium channel, subfamily M subunit beta-2, Charybdotoxin receptor subunit beta-2, Hbeta3, K(VCA)beta-2, Maxi K channel subunit beta-2, Slo-beta-2
Organism Homo sapiens (Human)
UniProt ID Q9Y691
Transmembrane Times Multi-pass membrane
Length (aa) 235

Function of KCNMB2 Membrane Protein

KCNMB2 is essentially a regulator subunit of KCNMA1, a calcium-activated potassium channel. Just like KCNMB1, KCNMB2 is also associated with the calcium sensitivity and gating kinetics of KCNMA1. In vivo, KCNMB2 can negatively regulate the activity of KCNMA1, rapidly and completely inactivating the KCNMA1 channel complex. The regulatory activity is mainly mediated by the N-termini. At the same time, KCNMB2 also participates in many other biological processes, for example, neuronal action potential, regulation of vasoconstriction and action potential. It has been revealed that KCNMB2 can limit KCNMA1 surface expression levels through the endocytic trafficking signals at the C-terminus, and coexpression with KCNMA1 causes a shift of KCNMA1’s cytoplasmic distribution. KCNMB2 knockdown mice excrete fewer K+ into the urine and display hyperaldosteronism, but they can achieve K+ balance through an aldosterone-mediated, KCNMB2-independent mechanism.

Ball-and-chain domains of KCNMB2. Fig.1 Ball-and-chain domains of KCNMB2. (Detlef l, 2001)

Application of KCNMB2 Membrane Protein in Literature

  1. Yu M., et al. Overexpression of Kcnmb2 in Dorsal CA1 of Offspring Mice Rescues Hippocampal Dysfunction Caused by a Methyl Donor-Rich Paternal Diet. Front Cell Neurosci. 2018, 12:360. PubMed ID: 30405352

    According to the previous finding that a paternal methyl donor-rich diet can negatively regulate expression of KCNMB, authors in this article explore the synaptic and intrinsic properties of CA1 pyramidal neurons of the F1 offspring mice, and they try to reveal the mechanisms of the phenomenon.

  2. Larsen C.K., et al. Intact colonic KCa1.1 channel activity in KCNMB2 knockout mice. Physiol Rep. 2017, 5(5): e13179. PubMed ID: 28292889

    Accordingly, the physiological importance of KCNMB2 as an auxiliary subunit of large conductance Ca2+-activated K+ channel has not been revealed entirely. Authors in this article report that colonic K+ secretion is intact or even increased in KCNMB2 knockout mice.

  3. Martinez-Espinosa P.L., et al. Knockout of the BK β2 subunit abolishes inactivation of BK currents in mouse adrenal chromaffin cells and results in slow-wave burst activity. J Gen Physiol. 2014, 144(4):275-95. PubMed ID: 25267913

    It has been reported that KCNMB2 can influence the range of BK channel activation. In order to confirm this idea, authors in this article use KCNMB2 mice to test. They finally reveal that the idea is solid, at the same time, they find that the particular properties of BK channels in the absence of KCNMB2 perhaps predispose to burst firing.

  4. Zarei M.M., et al. Endocytic trafficking signals in KCNMB2 regulate surface expression of a large conductance voltage and Ca (2+)-activated K+ channel. Neuroscience. 2007, 147(1):80-89. PubMed ID: 17521822

    This article reveals that KCNMB2 can negatively regulate the surface expression levels of KCNMA1 through an endocytic mechanism. The endocytic trafficking signals in C-terminus of KCNMB2 may function in the process.

KCNMB2 Preparation Options

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  1. Bentrop D., et al. (2001). Nmr structure of the “ball-and-chain” domain of kcnmb2, the β2-subunit of large conductance Ca2+- and voltage-activated potassium channels. Journal of Biological Chemistry. 276(45): 42116-21.

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