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Originally published In Press as doi:10.1074/jbc.M910187199 on April 13, 2000

J. Biol. Chem., Vol. 275, Issue 30, 23211-23218, July 28, 2000
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Cloning and Functional Expression of Two Families of beta -Subunits of the Large Conductance Calcium-activated K+ Channel*

Victor N. UebeleDagger , Armando Lagrutta, Theresa Wade, David J. Figueroa, Yuan Liu, Edward McKenna, Christopher P. Austin, Paul B. Bennett, and Richard Swanson

From the Merck Research Laboratories, West Point, Pennsylvania 19486

We report here a characterization of two families of calcium-activated K+ channel beta -subunits, beta 2 and beta 3, which are encoded by distinct genes that map to 3q26.2-27. A single beta 2 family member and four alternatively spliced variants of beta 3 were investigated. These subunits have predicted molecular masses of 27.1-31.6 kDa, share ~30-44% amino acid identity with beta 1, and exhibit distinct but overlapping expression patterns. Coexpression of the beta 2 or beta 3a-c subunits with a BK alpha -subunit altered the functional properties of the current expressed by the alpha -subunit alone. The beta 2 subunit rapidly and completely inactivated the current and shifted the voltage dependence for activation to more polarized membrane potentials. In contrast, coexpression of the beta 3a-c subunits resulted in only partial inactivation of the current, and the beta 3b subunit conferred an apparent inward rectification. Furthermore, unlike the beta 1 and beta 2 subunits, none of the beta 3 subunits increased channel sensitivity to calcium or voltage. The tissue-specific expression of these beta -subunits may allow for the assembly of a large number of distinct BK channels in vivo, contributing to the functional diversity of native BK currents.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF204159-AF204162.

Dagger To whom correspondence should be addressed: Merck Research Laboratories, WP26-265, West Point, PA 19486. E-mail: victor_uebele@merck.com.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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