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<p>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 <i>C. elegans</i> 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 <i>C. elegans</i>. Ectopic expression of either <i>C. elegans</i> 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.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年2月16日

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  • 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,
  • Lijun Kang

摘要

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.