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. Author manuscript; available in PMC: 2013 Jul 15.
Published in final edited form as: J Neurosci. 2013 Jan 2;33(1):187–200. doi: 10.1523/JNEUROSCI.3214-12.2013

Figure 1.

Figure 1

Synaptotagmin 1 (Syt1) transgenic constructs and sequence similarity. A, Amino acid sequences of human, mouse and Drosophila Syt1 are compared. A single transmembrane domain and two C2 domains, C2A and C2B, are indicated as dark green, blue, and light green blocks, respectively. The five aspartate residues (D) involved in binding Ca2+ ions in each C2 domain are indicated with red asterisks. The third and fourth of these five aspartate residues were mutated to asparagines (N) to disrupt Ca2+-binding ability of each C2 domain (red boxes). B, The design of transgenic UAS-Syt1 constructs used for the analysis is shown. Syt1 consists of a short intraluminal region (blue line), a single transmembrane domain (dark green box), a cytoplasmic linker (red), two C2 domains (C2A-blue, C2B-green) with a short linker between them, and a C-terminal tail. C2 domains containing mutations described in (A) (red boxes) are indicated with asterisks.