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Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
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Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
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Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans

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Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans
Journal Article

Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans

2025
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Overview
Mechanotransduction channels are widely expressed in both vertebrates and invertebrates, mediating various physiological processes such as touch, hearing and blood-pressure sensing. While previously known mechanotransduction channels in metazoans are primarily cation-selective, we identified Anoctamin-1 (ANOH-1), the C. elegans homolog of mammalian calcium-activated chloride channel ANO1/TMEM16A, as an essential component of a mechanosensory channel complex that contributes to the nose touch mechanosensation in C. elegans . Ectopic expression of either C. elegans or human Anoctamin-1 confers mechanosensitivity to touch-insensitive neurons, suggesting a cell-autonomous role of ANOH-1/ANO1 in mechanotransduction. Additionally, we demonstrated that the mechanosensory function of ANOH-1/ANO1 relies on CIB (calcium- and integrin- binding) proteins. Thus, our results reveal an evolutionarily conserved chloride channel involved in mechanosensory transduction in metazoans, highlighting the importance of anion channels in mechanosensory processes. Mechanotransduction channels play key roles in various sensory processes. Here, the authors identify the chloride channel ANOH-1/ANO1 as a core component of a mechanosensory channel complex, highlighting its evolutionary conservation.