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) (PubMed:10036234, PubMed:11354632, PubMed:8663154, PubMed:9070898). SNAP23 is a t-SNARE (target-SNARE) that resides on target membrane and functions in the fusion of transport vesicles with the plasma membrane in immune cells (PubMed:30811271). In macrophages, regulates the stimulus-dependent vesicular transport of TLR4 from recycling endosomes to the plasma membrane by cooperating with STX11 and thereby plays a critical role in the recognition of microbial components and the induction of innate and adaptive immunity (PubMed:30811271). In skeletal muscle satellite cells, SNAP23 cooperates with its cognate SNAREs VAMP4 and STX11 to facilitate CD36 vesicular transport from endosomes to the plasma membrane, an essential step in muscle regeneration (By similarity). {ECO:0000250|UniProtKB:O09044, ECO:0000269|PubMed:10036234, ECO:0000269|PubMed:11354632, ECO:0000269|PubMed:30811271, ECO:0000269|PubMed:8663154, ECO:0000269|PubMed:9070898}. This is the function of SNAP23 (synaptosome associated protein 23, ENSG00000092531).