Stomatin-like protein 3 (STOML3)

Stomatin-like protein 3 (STOML3) is an integral membrane protein that belongs to the stomatin-domain family, characterized by a conserved core stomatin domain and a short hydrophobic hairpin responsible for membrane insertion[1][3][4]. STOML3 is predominantly expressed in sensory neurons—including olfactory sensory neurons and dorsal root ganglia—where it is essential for normal touch sensation and mechanosensory transduction[3][4]. It forms complexes with other stomatin-domain proteins and modulates the activity of key mechanosensitive ion channels such as ASICs (acid-sensing ion channels) and Piezo channels, thereby regulating neuronal sensitivity to mechanical and chemical stimuli[1][2][3]. STOML3 acts, at least in part, by binding membrane cholesterol, increasing membrane stiffness, and enabling efficient force transfer to mechanosensitive ion channels[2]. Its loss impairs sensory neuron function and mechanosensation, leading to decreased neuronal excitability and blunted perception of touch or pain, as shown in knockout models[2][4]. STOML3’s role in mechanotransduction and pain pathways makes it a candidate therapeutic target for managing chronic pain syndromes[2]. No specific drugs are yet marketed to target STOML3, but its mechanistic pathway is seen as a potential strategy for modulation of chronic pain[2].

Other names

Stomatin-like protein 3STOML3SLP-3SROEpb7.2lEPB72-like 3protein 7.2Berythrocyte band 7 integral membrane proteinstomatin (EPB72)-like 3

Modulates membrane mechanics by binding cholesterol; Facilitates force transfer to, and tunes, mechanosensitive ion channels (notably Piezo1, Piezo2, ASICs)