Dynamic Formation of the Protein-Lipid Pre-fusion 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 into PM upon Ca²⁺ binding, however the mechanistic detail of this process is still debated. Syt1 interacts with the SNARE complex, a coiled-coil four-helical bundle that enables the SV-PM attachment. The SNARE-associated protein Complexin (Cpx) promotes the Ca²⁺-dependent fusion, possibly interacting with Syt1. We employed all-atom molecular dynamics (MD) to investigate the formation of the Syt1-SNARE-Cpx complex interacting with the lipid bilayers of PM and SV. Our simulations demonstrated that the PM-Syt1-SNARE-Cpx complex can tran

SUBMITTER: Bykhovskaia M 

PROVIDER: S-EPMC11042276 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature