Molecular architecture of the fungal-specific potassium channel TOK1

Brice Durocher; Rían W Manville; Rui Yan; Zhiheng Yu; Geoffrey W Abbott; Alexandria N Miller

doi:10.1038/s41467-026-72232-y

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Molecular architecture of the fungal-specific potassium channel TOK1

Journal article

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Molecular architecture of the fungal-specific potassium channel TOK1

Brice Durocher, Rían W Manville, Rui Yan, Zhiheng Yu, Geoffrey W Abbott and Alexandria N Miller

Nature communications

04/27/2026

DOI: 10.1038/s41467-026-72232-y

PMID: 42045187

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Abstract

In Candida albicans, potassium (K+) channels fine-tune ionic balance under stress, contributing to host colonization. Fungal two-pore domain, outwardly rectifying potassium (TOK) channels remain insufficiently characterized despite evidence implicating them in growth and viability. Here, we describe the atomic-resolution structure of a fungal potassium channel, TOK1 from C. albicans (CaTOK), revealing an architecture defined by eight transmembrane helices and a membrane topology distinct from previously characterized K⁺ channel classes. The first four helices form a tetraspanin-like bundle resembling auxiliary subunits of human neuronal ion channels. The pore features an inner helical gating movement analogous to mammalian dimeric K+ channels, while the K+ selectivity filter exhibits atypical ion coordination. A cytosolic C-terminal bundle forms an intramolecular network that likely stabilizes CaTOK and may mediate gating. These findings provide a framework for understanding TOK channel function and facilitate future studies of fungal ion homeostasis, pathogenicity, and therapeutic development.

Details

Title: Subtitle: Molecular architecture of the fungal-specific potassium channel TOK1
Creators: Brice Durocher - University of Iowa
Rían W Manville - University of California, Irvine
Rui Yan - Janelia Research Campus
Zhiheng Yu - Janelia Research Campus
Geoffrey W Abbott - University of California, Irvine
Alexandria N Miller - University of Iowa
Resource Type: Journal article
Publication Details: Nature communications
DOI: 10.1038/s41467-026-72232-y
PMID: 42045187
ISSN: 2041-1723
eISSN: 2041-1723
Publisher: Springer Nature
Language: English
Electronic publication date: 04/27/2026
Academic Unit: Molecular Physiology and Biophysics
Record Identifier: 9985157602102771

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