SNAP23 (synaptosome associated protein 23) is an essential SNARE protein that mediates membrane fusion events across multiple cellular contexts. As a key component of SNARE complexes, SNAP23 regulates vesicle fusion with the plasma membrane through its interaction with syntaxins and VAMPs 1. The protein undergoes dynamic post-translational modifications, including palmitoylation by ZDHHC17, which targets it to lipid rafts and is crucial for cytotoxic granule exocytosis in immune cells 2. SNAP23 also participates in fatty acid uptake regulation through STX11/SNAP23/VAMP4 complexes in muscle stem cells 3. In disease contexts, SNAP23 plays pathological roles in pancreatitis through IKKβ-mediated phosphorylation at specific serine residues, promoting both basolateral exocytosis and autolysosome formation that leads to trypsinogen activation 4. Additionally, PTP1B deletion enhances SNAP23 phosphorylation, promoting endothelial exocytosis and venous thromboinflammation 5. SNAP23 is also involved in secretory autophagy in cancer-associated fibroblasts 6 and appears in neuronal contexts related to pain-associated anxiety 7. These findings position SNAP23 as a critical regulator of exocytosis with significant therapeutic potential across inflammatory, thrombotic, and neoplastic diseases.