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

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Listed:
  • Wenjuan Zou

    (Zhejiang University School of Medicine
    Zhejiang University School of Medicine
    Zhejiang University)

  • Yuedan Fan

    (Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

  • Jia Liu

    (Zhejiang University
    Zhejiang University)

  • Hankui Cheng

    (Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

  • Huitao Hong

    (Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

  • Umar Al-Sheikh

    (Zhejiang University
    Zhejiang University)

  • Shitian Li

    (Zhejiang University
    Zhejiang University)

  • Linhui Zhu

    (Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

  • Rong Li

    (Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

  • 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
    Zhejiang University School of Medicine
    Zhejiang University
    Zhejiang University)

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.

Suggested Citation

  • 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 Zha, 2025. "Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56938-z
    DOI: 10.1038/s41467-025-56938-z
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