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

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.

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Publication Details

Journal
Nature Communications
Published
2025-02-16
DOI
https://doi.org/10.1038/s41467-025-56938-z
Citations
5
Primary Topic
Neuroscience and Neuropharmacology Research
Type
article
Field-Weighted Citation Impact
4.55

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article

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

Hankui Cheng, Lijun Kang, Wenjuan Zou, Linlu He et al.
5 citations
Nature Communications
Neuroscience and Neuropharmacology Research
4.55
article

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

Hankui Cheng, Lijun Kang, Wenjuan Zou, Linlu He, Yuedan Fan, Guohua Zhao, Huitao Hong, Linhui Zhu, Xiujue Zheng, Umar Al-Sheikh, Yi‐Quan Tang, Shitian Li, Jia Liu, Feng Wang, Rong Li, Yongming Zhang
article en
5 citations

Abstract

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.

Nature CommunicationsVol. 16(1)
Zhejiang Chinese Medical University (CN), Allen Institute for Brain Science (US), Eye & ENT Hospital of Fudan University (CN), Zhejiang Lab (CN), Second Affiliated Hospital of Zhejiang University (CN), First Affiliated Hospital Zhejiang University (CN), Zhejiang University (CN)
National Natural Science Foundation of China, Ministry of Science and Technology of the People's Republic of China, Zhejiang University, Chinese Academy of Medical Sciences, National Institutes of Health, Natural Science Foundation of Zhejiang Province
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Openalex Percentile: Top 6%
Neuroscience and Neuropharmacology Research
4.55
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