The 'SNARE hypothesis' is a model explaining the process of
docking and fusion of vesicles to their target membranes.
According to this model, membrane proteins from the vesicle
(v-SNAREs) and proteins from the target membrane (t-SNAREs)
govern the specificity of vesicle targeting and docking through
mutual recognition. Once the 2 classes of SNAREs bind to each
other, they form a complex that recruits the general elements of
the fusion apparatus, namely NSF (N-ethylmaleimide-sensitive
factor) and SNAPs (soluble NSF-attachment proteins), to the site
of membrane fusion, thereby forming the 20S fusion complex.
Alpha- and gamma-SNAP are found in a wide range of tissues and
act synergistically in intra-Golgi transport. The sequence of
the predicted 295-amino acid human protein encoded by NAPA
shares 37%, 60%, and 67% identity with the sequences of yeast,
Drosophila, and squid alpha-SNAP, respectively. Platelets
contain some of the same proteins, including NSF, p115/TAP,
alpha-SNAP, gamma-SNAP, and the t-SNAREs syn