SNAP47 is a SNARE protein containing dual Qb and Qc domains that mediates intracellular membrane fusion, particularly in autophagy-lysosomal pathways 1. As a member of the SNAP-25 protein family, SNAP47 functions distinctly from other family members, unable to cross-rescue SNAP-25 or SNAP-23 functions 1. Mechanistically, SNAP47 is recruited to autophagosomes via its Pleckstrin homology domain, which detects ATG8s and PI(4,5)P2 2. SNAP47 forms the STX17-SNAP47-VAMP7/VAMP8 SNARE complex, the default machinery mediating autophagosome-lysosome fusion in both selective autophagy under non-starvation conditions and starvation-induced bulk autophagy 2. Notably, deacetylated SNAP47 recruits HOPS components to facilitate fusion independently of STX17 interactions, while acetylation by CBP inhibits this process, with deacetylation by HDAC2 restoring function 3. Additionally, SNAP47 promotes viral replication through interactions with ATG14 and facilitates CVB3 propagation via VP1 capsid assembly 4. Clinically, SNAP47 loss correlates with cognitive decline in neurodegenerative diseases including Alzheimer's disease, Parkinson's disease dementia, and dementia with Lewy bodies 5, with synaptic SNAP47 levels predicting disease severity 6. In cancer, circular RNA-derived SNAP47 dysregulation contributes to chemoresistance in lung cancer 7, while SPIB-mediated SNAP47 activation promotes anoikis resistance 8.