High impact information on Snap25

• The neuronal SNARE complex is formed via the interaction of synaptobrevin with syntaxin and SNAP-25 [1].
• We have isolated a SNAP-25 temperature-sensitive paralytic mutant in Drosophila, SNAP-25(ts) [2].
• In neurons, the t-SNARE SNAP-25 is essential for synaptic vesicle fusion but its exact role in this process is unknown [2].
• Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones [3].
• None of the SNAP-25 sequences has a membrane-spanning region, but all contain a cluster of cysteine residues that can be palmitoylated for membrane attachment [3].

Biological context of Snap25

• In this study, we performed a mutagenesis screen to identify new SNAP-25 alleles that fail to complement our previously isolated recessive temperature-sensitive allele of SNAP-25, SNAP-25(ts) [4].

Anatomical context of Snap25

• In situ hybridization showed that SNAP-25 mRNA is exclusively found in brain and ganglia in Drosophila with a pattern suggesting expression in most neurons [3].
• For fusion at the plasma membrane, the t-SNARE SNAP-25 is essential [5].
• SNAP-24, a Drosophila SNAP-25 homologue on granule membranes, is a putative mediator of secretion and granule-granule fusion in salivary glands [5].
• At the third instar larval stage, SNAP-25 nulls exhibit nearly normal neurotransmitter release at the neuromuscular junction [4].
• These data suggest that this lipid modification of cysteine string proteins is relatively more stable than that observed for other nerve ending proteins, like SNAP-25 [6].

Analytical, diagnostic and therapeutic context of Snap25

• In situ hybridization and immunocytochemistry to whole mount embryos show that SNAP-25 mRNA and protein are detected in stage 14 and later developmental stages, and are mainly localized to the ventral nerve cord [7].

References