Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an α-helical coiled-coil domain called the SNARE motif []. These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classification scheme defines R-SNAREs and Q-SNAREs, as based on the conserved arginine or glutamine residue in the centre of the SNARE motif []. SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways, and contribute to the specificity of intracellular membrane fusion processes.The t-SNARE domain consists of a 4-helical bundle with a coiled-coil twist. The SNARE motif contributes to the fusion of two membranes. SNARE motifs fall into four classes: homologues of syntaxin 1a (t-SNARE), VAMP-2 (v-SNARE), and the N- and C-terminal SNARE motifs of SNAP-25.This entry represents the N-terminal SNARE motif found in plant SNAP25 homologues, SNAP29, SNAP30 and SNAP33 [, , ], and in the novel plant SNAREs (NPSNs) 11, 12 and 13 from Arabidopsis thaliana [, ]. SNAP33 and NPS11 play a key role in cytokinesis [, ]. SNAP33, the most studied SNAP25 homologue in Arabidopsis, is also involved in triggering innate immune responses. SNAP29 and SNAP30 have not been well-characterised yet [].
