ArticleNeuron2024
Sequence variations and accessory proteins adapt TMC functions to distinct sensory modalities.
Article in Neuron, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Hierarchical Channel System Drives Stimulus Specificity and Polymodal Encoding in A Mechano-Cold Sensory Neuron.Neuroscience bulletin · 2026Article
- Molecular identity of the mechanotransduction machinery in inner ear hair cells and mechanotransduction-linked hearing loss.Fundamental research · 2026Review
- Evolutionary tuning of an auditory transduction channel.Current biology : CB · 2026Article
- LHFPL5 is required for maximal activation of the mechanotransduction channel in cochlear hair cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Research Progress on MET, Tip Link, and Stereocilia Complex with Special Reference to Zebrafish.International journal of molecular sciences · 2025Review
- Ankyrins are dispensable for mechanotransduction by cochlear hair cells.Hearing research · 2025Article
- The Diverse Functions of the Calcium- and Integrin-Binding Protein Family.International journal of molecular sciences · 2025Review
- Anoctamin-1 is a core component of a mechanosensory anion channel complex in C. elegans.Nature communications · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Transmembrane channel-like (TMC) proteins are expressed throughout the animal kingdom and are thought to encode components of ion channels. Mammals express eight TMCs (mTMC1-8), two of which (mTMC1 and mTMC2) are subunits of mechanotransduction channels. C. elegans expresses two TMCs (TMC-1 and TMC-2), which mediate mechanosensation, egg laying, and alkaline sensing. The mechanisms by which nematode TMCs contribute to such diverse physiological processes and their functional relationship to mammalian mTMCs is unclear. Here, we show that association with accessory proteins tunes nematode TMC-1 to divergent sensory functions. In addition, distinct TMC-1 domains enable touch and alkaline sensing. Strikingly, these domains are segregated in mammals between mTMC1 and mTMC3. Consistent with these findings, mammalian mTMC1 can mediate mechanosensation in nematodes, while mTMC3 can mediate alkaline sensation. We conclude that sequence diversification and association with accessory proteins has led to the emergence of TMC protein complexes with diverse properties and physiological functions.
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