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. 2021 Feb 22;78(9):4335–4364. doi: 10.1007/s00018-021-03788-9

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Function of SYT1 in SV fusion. a Syt1 null mutants reduce synchronous fusion and enhance asynchronous release and mini frequency. Rescue with a Syt1 transgene with defective Ca²⁺ binding to C2A(*) and C2B(*) fails to support synchronous fusion and causes higher rates of spontaneous release. b Overexpression of a C2B Ca²⁺ binding mutant (D1,2N) suppresses release compared to overexpression of wildtype SYT1. Twenty essential residues mapping to C2A (blue) or C2B (magenta) were identified in an intragenic suppressor screen that blocked the dominant-negative effects. c. Structure of the primary and tripartite interface of the SYT1/SNARE/CPX complex. d Location of mutations disrupting the primary SNARE interface on the SYT1 C2B domain. The polybasic stretch is shown in grey and localizes to the opposite C2B surface. SNARE-binding mutations fail to rescue release defects in Syt1 null mutants (right panel). e Location of the R250H mutation at the SYT1 dimer interface that disrupts oligomerization. This mutation reduces SV release (right panel), though not as severely as SNARE-binding mutants. a Modified from [49], b, d, and e modified from [62], and c modified from [38]