Ca2+-Activated K+Channels: From Protein Complexes to Function
Abstract
Molecular research on ion channels has demonstrated that many of these integral membrane proteins associate with partner proteins, often versatile in their function, or even assemble into stable macromolecular complexes that ensure specificity and proper rate of the channel-mediated signal transduction. Calcium-activated potassium (K(Ca)) channels that link excitability and intracellular calcium concentration are responsible for a wide variety of cellular processes ranging from regulation of smooth muscle tone to modulation of neurotransmission and control of neuronal firing pattern. Most of these functions are brought about by interaction of the channels' pore-forming subunits with distinct partner proteins. In this review we summarize recent insights into protein complexes associated with K(Ca) channels as revealed by proteomic research and discuss the results available on structure and function of these complexes and on the underlying protein-protein interactions. Finally, the results are related to their significance for the function of K(Ca) channels under cellular conditions.
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The BK channel is an octameric complex of four pore-forming α-subunits and four regulatory β-subunits.
“The BK channel is an octameric complex of four pore-forming α-subunits and four regulatory β-subunits (62).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [62]
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Calcium-activated potassium channels
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Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793 · see citing works
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Cholinergic and Adenosinergic Modulation of Synaptic Release
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- Authors
- Berkefeld, H., Fakler, B., & Schulte, U.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Fakler, Bernd
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2010-10
- Volume
- 90
- Issue
- 4
- Pages
- 1437-1459
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2148652677
- Cited by
- 274
- References
- 5
- Citations by year
- 2026: 9 · 2025: 17 · 2024: 8 · 2023: 12 · 2022: 14 · 2021: 16 · 2020: 13 · 2019: 10 · 2018: 16 · 2017: 16 · 2016: 15 · 2015: 34 · 2014: 25 · 2013: 27 · 2012: 21
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Physiological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Health Sciences › Medicine › Physiology › Erythrocyte Function and Pathophysiology
- Keywords
- calcium-activated potassium channels, protein-protein interaction, smooth muscle tone, neurotransmission, neuronal firing patterns, channel structure and function
- MeSH terms
- Animals, Gene Expression Regulation, Models, Molecular, Protein Conformation, Protein Transport, Potassium Channels, Calcium-Activated, Proteomics, Multiprotein Complexes, Large-Conductance Calcium-Activated Potassium Channels, Small-Conductance Calcium-Activated Potassium Channels
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