ArticleThe Journal of general physiology2003
Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues.
Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 82 citations in OpenAlex.
- Lipid trapping slows ball-and-chain inactivation in a calcium-activated potassium channel.Nature communications · 2026Article
- BK channels are indispensable for endothelial function in small pulmonary arteries.Cell communication and signaling : CCS · 2025Article
- Disruption of a side portal pathway permits closed-state inactivation by BK β subunit N termini.The Journal of general physiology · 2025Article
- Ball-and-chain inactivation of a human large conductance calcium-activated potassium channel.Nature communications · 2025Article
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- Mapping the functional expression of auxiliary subunits of KScientific reports · 2022Article
- Effect of an autism-associatedCurrent research in physiology · 2022Article
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- Comparison of KHandbook of experimental pharmacology · 2021Article
- LINGO1 is a regulatory subunit of large conductance, CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chromaffin Cells of the Adrenal Medulla: Physiology, Pharmacology, and Disease.Comprehensive Physiology · 2019Article
- Voltage- and calcium-gated ion channels of neurons in the vertebrate retina.Progress in retinal and eye research · 2019Review
- Regulation of BK Channels by Beta and Gamma Subunits.Annual review of physiology · 2019Review
- A Novel Peptide Restricts Ethanol Modulation of the BK Channel In Vitro and In Vivo.The Journal of pharmacology and experimental therapeutics · 2018Article
- Regulatory γ1 subunits defy symmetry in functional modulation of BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Roles of NaPflugers Archiv : European journal of physiology · 2018Review
- Overexpression ofFrontiers in cellular neuroscience · 2018Article
- The Slo(w) path to identifying the mitochondrial channels responsible for ischemic protection.The Biochemical journal · 2017Review
- A voltage-dependent KThe Journal of cell biology · 2017Article
- Deletion of cytosolic gating ring decreases gate and voltage sensor coupling in BK channels.The Journal of general physiology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
An auxiliary beta2 subunit, when coexpressed with Slo alpha subunits, produces inactivation of the resulting large-conductance, Ca(2+) and voltage-dependent K(+) (BK-type) channels. Inactivation is mediated by the cytosolic NH(2) terminus of the beta2 subunit. To understand the structural requirements for inactivation, we have done a mutational analysis of the role of the NH(2) terminus in the inactivation process. The beta2 NH(2) terminus contains 46 residues thought to be cytosolic to the first transmembrane segment (TM1). Here, we address two issues. First, we define the key segment of residues that mediates inactivation. Second, we examine the role of the linker between the inactivation segment and TM1. The results show that the critical determinant for inactivation is an initial segment of three amino acids (residues 2-4: FIW) after the initiation methionine. Deletions that scan positions from residue 5 through residue 36 alter inactivation, but do not abolish it. In contrast, deletion of FIW or combinations of point mutations within the FIW triplet abolish inactivation. Mutational analysis of the three initial residues argues that inactivation does not result from a well-defined structure formed by this epitope. Inactivation may be better explained by linear entry of the NH(2)-terminal peptide segment into the permeation pathway with residue hydrophobicity and size influencing the onset and recovery from inactivation. Examination of the ability of artificial, polymeric linkers to support inactivation suggests that a variety of amino acid sequences can serve as adequate linkers as long as they contain a minimum of 12 residues between the first transmembrane segment and the FIW triplet. Thus, neither a specific distribution of charge on the linker nor a specific structure in the linker is required to support the inactivation process.
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Registered trials
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.