The SNARE protein family is the core molecular apparatus mediating all membrane fusion events in eukaryotic cells. By assembling to form trans-SNARE complexes, they drive the docking and fusion process between vesicles and target membranes, ensuring the orderly transport of intracellular materials among various components of the membrane system. YKT6, a structurally unique and evolutionarily conserved member of this family, has been highly regarded by researchers since its discovery due to its atypical membrane anchoring mode and broad biological functions. Unlike most SNARE proteins that possess transmembrane domains, YKT6 does not contain a transmembrane segment. Its membrane localization depends on the lipid covalent modification of two cysteine residues near the C-terminus, specifically farnesylation and geranylgeranylation. This unique dual prenylation modification pattern is the key structural basis for the realization of its biological functions.