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Cited by 373

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Molecular basis of fast inactivation in voltage and Ca 2+ -activated K + channels: A transmembrane β-subunit homolog

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Wallner, Martin, Meera, Pratap, Toro, Ligia·1999·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.96.7.4137
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Abstract

Voltage-dependent and calcium-sensitive K + (MaxiK) channels are key regulators of neuronal excitability, secretion, and vascular tone because of their ability to sense transmembrane voltage and intracellular Ca 2+ . In most tissues, their stimulation results in a noninactivating hyperpolarizing K + current that reduces excitability. In addition to noninactivating MaxiK currents, an inactivating MaxiK channel phenotype is found in cells like chromaffin cells and hippocampal neurons. The molecular determinants underlying inactivating MaxiK channels remain unknown. Herein, we report a transmembrane β subunit (β2) that yields inactivating MaxiK currents on coexpression with the pore-forming α subunit of MaxiK channels. Intracellular application of trypsin as well as deletion of 19 N-terminal amino acids of the β2 subunit abolished inactivation of the α subunit. Conversely, fusion of these N-terminal amino acids to the noninactivating smooth muscle β1 subunit leads to an inactivating phenotype of MaxiK channels. Furthermore, addition of a synthetic N-terminal peptide of the β2 subunit causes inactivation of the MaxiK channel α subunit by occluding its K + -conducting pore resembling the inactivation caused by the “ball” peptide in voltage-dependent K + channels. Thus, the inactivating phenotype of MaxiK channels in native tissues can result from the association with different β subunits.

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Metadata

Authors
Wallner, M., Meera, P., & Toro, L.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
1999-03-30
Volume
96
Issue
7
Pages
4137-4142
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.96.7.4137
OpenAlex
W2063845237
Cited by
373
References
30
FWCI
6.42
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Molecular basis of fast inactivation in voltage and Ca 2+ -activated K + channels: A transmembrane β-subunit homolog. https://app.cochat.ai/papers/10.1073/pnas.96.7.4137
The paper
Wallner, M., Meera, P., & Toro, L. (1999). Molecular basis of fast inactivation in voltage and Ca 2+ -activated K + channels: A transmembrane β-subunit homolog. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.7.4137

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.