Dynamic formation of the protein-lipid prefusion complex.

ABSTRACT: Synaptic vesicles (SVs) fuse with the presynaptic membrane (PM) to release neuronal transmitters. The SV protein synaptotagmin 1 (Syt1) serves as a Ca²⁺ sensor for evoked fusion. Syt1 is thought to trigger fusion by penetrating the PM upon Ca²⁺ binding; however, the mechanistic detail of this process is still debated. Syt1 interacts with the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) complex, a coiled-coil four-helical bundle that enables the SV-PM attachment. The SNARE-associated protein complexin (Cpx) promotes Ca²⁺-dependent fusion, possibly interacting with Syt1. We employed all-atom molecular dynamics to investigate the formation of the Syt1-SNARE-Cpx complex interacting with the lipid bilayers of the PM and SVs. Our

SUBMITTER: Bykhovskaia M 

PROVIDER: S-EPMC11495646 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature