STX11

SNAREs (soluble N-ethylmaleimide-sensitive factor-attachment protein receptors) are essential proteins for intracellular membrane fusion. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four-helix bundle whose assembly releases energy that drives membrane fusion. The core SNARE complex typically consists of four alpha-helical domains, three from target membrane SNAREs (t-SNAREs) and one from a vesicle SNARE (v-SNARE). Syntaxin-11/STX11 is an atypical lipid-anchored t-SNARE that forms a SNARE complex with the t-SNARE SNAP23 and the v-SNARE VAMP8. This SNARE complex plays a critical role in the regulated exocytosis of cytotoxic granules by natural killer (NK) cells and cytotoxic T-lymphocytes. In macrophages, STX11 regulates stimulus-dependent vesicular transport of TLR4 from recycling endosomes to the plasma membrane by cooperating with SNAP23, thereby playing a critical role in microbial component recognition and the induction of innate and adaptive immunity (By similarity). In skeletal muscle satellite cells, STX11 cooperates with its cognate SNAREs VAMP4 and SNAP23 to facilitate CD36 vesicular transport from endosomes to the plasma membrane, an essential step in muscle regeneration (By similarity). In another proposed mechanism, STX11 may function as a regulator of the SNARE VTI1B on late endosomes to regulate trafficking from late endosomes to lysosomes..

Function from UniProtKB (O75558), read 2026-09-23. CC BY 4.0.