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| Item Type: | Preprint |
|---|---|
| Title: | TENM4 is an essential transduction component for touch |
| Creators Name: | Khallaf, Mohammed A., Huang, Angela Tzu-Lun, Dalmasso, Letizia, Chakrabarti, Sampurna, Groeneveld, Rowena, Sierra, Yinth Andrea Bernal, Garcia-Contreras, Jonathan Alexis, Nello, Emilie, Schütz, Anja, Bégay, Valérie, Santuz, Alessandro, Hedtrich, Sarah, Zhong, Wei, Schiel, Christina, Middleton, Steven J., Popp, Oliver, Zampieri, Niccolò, Mertins, Philipp, Kunz, Severine and Lewin, Gary R. |
| Abstract: | Gentle touch is conveyed to the brain by fast-conducting sensory fibers. Mechanosensitive ion channels at the terminals of these neurons are thought to be gated by extracellular tethers that transmit force from the surrounding matrix to the channel complex, but the molecular identity of such tethers has remained unknown. Here, we identify Teneurin-4 (TENM4) as an essential extracellular linker protein for mechanotransduction in mechanoreceptors. Sensory neuron-specific deletion of Tenm4 in mice caused profound touch insensitivity, while acute and reversible proteolytic disassembly of TENM4 at sensory endings confirmed its direct role in force transduction. Ultrastructural analyses revealed TENM4 localization to filamentous structures at the neurite-laminin interface, defining it as a structural component of the mechanosensory tether. These findings identify TENM4 as a core element of fast somatic sensation and provide molecular insight into how extracellular forces are coupled to ion channel activation. |
| Keywords: | Animals, Mice |
| Source: | bioRxiv |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Article Number: | 2024.10.10.617546v2 |
| Date: | 18 January 2026 |
| Additional Information: | ProteomeXchange dataset PXD050952 has been reserved by the PRIDE repository for a dataset that has been deposited, but is not yet publicly released and announced to ProteomeXchange. |
| Official Publication: | https://doi.org/10.1101/2024.10.10.617546 |
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