Evidence map›Paper›PMID 41288509›Full record

ArticleThe Journal of general physiology2026

β2 and β3a regulatory subunits can coassemble in the same BK channels.

Yu Zhou, Vivian Gonzalez-Perez, Xiao-Ming Xia, Gopal S Kallure, Sandipan Chowdhury, Christopher J Lingle

Abstract read
In one paragraph

Article in The Journal of general physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Yu ZhouDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0002-1407-6140
Vivian Gonzalez-PerezDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0002-5093-6769
Xiao-Ming XiaDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0009-0006-5000-7683
Gopal S KallureDepartment of Physiology and Biophysics, University School of Medicine, Iowa City, IA, USA.ORCID 0000-0002-5215-5069
Sandipan ChowdhuryDepartment of Physiology and Biophysics, University School of Medicine, Iowa City, IA, USA.ORCID 0000-0002-0695-7968
Christopher J LingleDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0002-9916-3795

Funding

SLO family potassium channels: function and physiologyR35GM118114 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2016 to 2025
$6.9M
Mechanisms of voltage regulation of membrane transportR01GM145719 · NIGMS · UNIVERSITY OF IOWA · PI Sandipan Chowdhury · 2022 to 2026
$1.7M
NIGMS NIH HHS R01 GM145719NIGMS NIH HHS R35 GM118114NIH HHS GM-118114NIH HHS GM-145719University of Iowa
6 · The paper itself

Abstract

Ca2+- and voltage-activated BK-type K+ channels are influenced profoundly by associated regulatory subunits, including β subunits (Kcnmb1-4; β1-β4). Although overlap in expression of different BK β subunits occurs in native tissues, whether they can coassemble in the same channel complex is not known. We coexpress β2 and β3a subunits together with BK α and, through a combination of macroscopic and single-channel recordings, along with quantitative pull-down of tagged subunits, test whether coassembly can occur. We evaluate two models: (1) random mixing in which β2 and β3a subunits coassemble in the same channels, and (2) segregation in which β2 and β3a are found in separate complexes. Our results support the view that, for β2 and β3a, BK currents arise from the random, independent assembly of both subunits in the same channels. Single-channel recordings directly confirm coassembly of β2 and β3a subunits in the same channels. Quantitative biochemical analysis of coexpression of tagged β2, β3a, and BK α subunits also reveals that β2:β3a:α ternary complexes form.

Indexed as

Large-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsAnimalsHEK293 CellsHumansProtein SubunitsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsProtein Subunits

Identifiers

PMID41288509
PMCPMC12646051

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.