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:23217709, PubMed:25686604, PubMed:28265073). VAMP8 is a v-SNARE that forms a SNARE complex with the t-SNARE STX11 and SNAP23. This SNARE complex plays a critical role in the regulated exocytosis of cytotoxic granules by natural killer (NK) cells and cytotoxic T- lymphocytes (PubMed:28265073). VAMP8 plays a role in autophagy where it controls organelle-organelle membrane fusion through a VAMP8, SNAP29 and STX17 SNARE complex that mediates the fusion of autophagosome and lysososome membranes (PubMed:23217709, PubMed:25686604). VAMP8 is required for dense-granule secretion in platelets (PubMed:12130530). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Also participates in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (PubMed:31694946). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:12130530, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:28265073, ECO:0000269|PubMed:31694946}. This is the function of VAMP8 (vesicle associated membrane protein 8, ENSG00000118640).