Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes

Marieke Meijer, Miriam Öttl, Jie Yang, Aygul Subkhangulova, Avinash Kumar, Zicheng Feng, Torben W. van Voorst, Alexander J. Groffen, Jan R.T. van Weering, Yongli Zhang, Matthijs Verhage

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Tomosyns are widely thought to attenuate membrane fusion by competing with synaptobrevin-2/VAMP2 for SNARE-complex assembly. Here, we present evidence against this scenario. In a novel mouse model, tomosyn-1/2 deficiency lowered the fusion barrier and enhanced the probability that synaptic vesicles fuse, resulting in stronger synapses with faster depression and slower recovery. While wild-type tomosyn-1m rescued these phenotypes, substitution of its SNARE motif with that of synaptobrevin-2/VAMP2 did not. Single-molecule force measurements indeed revealed that tomosyn’s SNARE motif cannot substitute synaptobrevin-2/VAMP2 to form template complexes with Munc18-1 and syntaxin-1, an essential intermediate for SNARE assembly. Instead, tomosyns extensively bind synaptobrevin-2/VAMP2-containing template complexes and prevent SNAP-25 association. Structure-function analyses indicate that the C-terminal polybasic region contributes to tomosyn’s inhibitory function. These results reveal that tomosyns regulate synaptic transmission by cooperating with synaptobrevin-2/VAMP2 to prevent SNAP-25 binding during SNARE assembly, thereby limiting initial synaptic strength and equalizing it during repetitive stimulation.

Original languageEnglish
Article number2652
Pages (from-to)1-20
Number of pages20
JournalNature communications
Volume15
Issue number1
Early online date26 Mar 2024
DOIs
Publication statusE-pub ahead of print - 26 Mar 2024

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