Abstract
BPS2025 - Co-assembly of β2 and β3a subunits in BK channel
Biophysical journal, Vol.124(3 Suppl 1), pp.345a-345a
02/13/2025
DOI: 10.1016/j.bpj.2024.11.1887
Abstract
Non-pore forming β subunits (KCNMB1–4) can influence a variety of BK channel functional properties, including gating shifts, activation and deactivation kinetics, inactivation (β2, β3a–c), pharmacology, and current rectification. As different isoforms of β-subunits may be co-expressed in the same cell, more than one type of β-subunit may co-assemble with the BK pore-forming α-subunit, which may add an additional layer of complexity and specificity to the regulation of this physiologically and pathologically important K+ channel. Here, taking advantage of different tail current properties conferred by β2 and β3a subunits and the differences in trypsin removal of β2 and β3a inactivation, we used trinomial distribution-based models to show that the results are better explained by a model in which β2 and β3a subunits co-assemble with α-subunit rather than being segregated among different channels. We further recorded single channel currents to confirm the occurrence of mixed assembly and multiple stoichiometry of β2/β3a subunits. In addition, our biochemical results also support the co-assembly of β2/β3a subunits in BK channels. The work was supported in part by the R35GM118114 from NIGMS.
Details
- Title: Subtitle
- BPS2025 - Co-assembly of β2 and β3a subunits in BK channel
- Creators
- Yu Zhou - Washington University in St. LouisXiaoming Xia - Washington University in St. LouisGopal Kallure - University of IowaSandipan Chowdhury - University of IowaChris Lingle - Washington University in St. Louis School of Medicine
- Resource Type
- Abstract
- Publication Details
- Biophysical journal, Vol.124(3 Suppl 1), pp.345a-345a
- Publisher
- Elsevier Inc
- DOI
- 10.1016/j.bpj.2024.11.1887
- ISSN
- 0006-3495
- Language
- English
- Date published
- 02/13/2025
- Academic Unit
- Molecular Physiology and Biophysics
- Record Identifier
- 9984790997002771
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