Figure 2.
Schematic of the SNAP25. SNAP25 contributes two of the four SNARE motifs that comprise the prototypical four-helical bundle in neuronal SNARE proteins. The two motifs, SN1 and SN2, are joined by a linker sequence (light blue and yellow line) with four N-terminal cysteines that are sites for palmitoylation. The linker region is divided into N-terminal (blue) and C-terminal (yellow) domains according to the constructs in Shaaban et al. (2019). SN2 contains the cleavage site for botulinum neurotoxin type E (BoNT E). BoNT E was used in an earlier study to inactivate endogenous SNAP25 (Wang et al., 2008). Shaaban et al., (2019) demonstrate that the N- and C-terminal domains have different roles in enabling the function of SNAP25 in exocytosis. The horizontal distances are to scale.

Schematic of the SNAP25. SNAP25 contributes two of the four SNARE motifs that comprise the prototypical four-helical bundle in neuronal SNARE proteins. The two motifs, SN1 and SN2, are joined by a linker sequence (light blue and yellow line) with four N-terminal cysteines that are sites for palmitoylation. The linker region is divided into N-terminal (blue) and C-terminal (yellow) domains according to the constructs in Shaaban et al. (2019). SN2 contains the cleavage site for botulinum neurotoxin type E (BoNT E). BoNT E was used in an earlier study to inactivate endogenous SNAP25 (Wang et al., 2008). Shaaban et al., (2019) demonstrate that the N- and C-terminal domains have different roles in enabling the function of SNAP25 in exocytosis. The horizontal distances are to scale.

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