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

Wenjuan Zou (), Yuedan Fan, Jia Liu, Hankui Cheng, Huitao Hong, Umar Al-Sheikh, Shitian Li, Linhui Zhu, Rong Li, Longyuan He, Yi-Quan Tang, Guohua Zhao, Yongming Zhang, Feng Wang, Renya Zhan, Xiujue Zheng and Lijun Kang ()
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Wenjuan Zou: Zhejiang University School of Medicine
Yuedan Fan: Zhejiang University School of Medicine
Jia Liu: Zhejiang University
Hankui Cheng: Zhejiang University School of Medicine
Huitao Hong: Zhejiang University School of Medicine
Umar Al-Sheikh: Zhejiang University
Shitian Li: Zhejiang University
Linhui Zhu: Zhejiang University School of Medicine
Rong Li: Zhejiang University School of Medicine
Longyuan He: Zhejiang University School of Medicine
Yi-Quan Tang: Fudan University
Guohua Zhao: Zhejiang University School of Medicine
Yongming Zhang: Zhejiang University School of Medicine
Feng Wang: Zhejiang University School of Medicine
Renya Zhan: Zhejiang University School of Medicine
Xiujue Zheng: Zhejiang University School of Medicine
Lijun Kang: Zhejiang University School of Medicine

Nature Communications, 2025, vol. 16, issue 1, 1-19

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-56938-z

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