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<p>In <i>Candida albicans</i>, potassium (K<sup>+</sup>) 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 <i>C. albicans</i> (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<sup>+</sup> channels, while the K<sup>+</sup> 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.</p>

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Molecular architecture of the fungal-specific potassium channel TOK1

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年4月27日

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

摘要

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.