Our ability to feel a touch relies on the activity of sensory neurons located within the skin. These neurons are able to detect nanometer-scale mechanical displacements at the skin surface and to transduce them into electrical signals. All mechanotransduction complexes identified so far rely on tethering mechanisms. We hypothesize that, similarly, mechanotransduction in the skin requires coupling between the mechanosensitive ion channels and the extracellular matrix mediated by protein tethers. In sensory neurons cultured on a laminin matrix and imaged either with TEM or FIB/SEM, these tethers appear as electron-dense, 100 nm long extracellular protein filaments located between the neurites and the laminin. Notably, acute treatment of cultured sensory neurons with specific proteases leads to the disruption of these tethers, accompanied by loss of rapidly adapting mechanosensitive currents. This supports our tether model of skin mechanotransduction. Despite the molecular identity of these tethers still remains elusive, we have restricted the number of potential candidates to just a few proteins, including TENM4, which we recently demonstrated being critically required for touch sensation, possibly by being part of such tethers. We are therefore using TENM4 as bait to search for additional potential components of mechanosensitive tethers. For this, we are developing a pipeline to broaden the applications of Protein A-TurboID proximity biotinylation – a methodology currently restricted to cell lines – to more complex systems, including the mouse skin. Notably, this would open up avenues to investigate the molecular identity of mechanotransduction complexes in other systems as well.