Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion.

ABSTRACT: Intrinsically disordered proteins (IDPs) and their conformational transitions play an important role in neurotransmitter release at the neuronal synapse. Here, the SNARE proteins are essential by forming the SNARE complex that drives vesicular membrane fusion. While it is widely accepted that the SNARE proteins are intrinsically disordered in their monomeric prefusion form, important mechanistic aspects of this prefusion conformation and its lipid interactions, before forming the SNARE complex, are not fully understood at the molecular level and remain controversial. Here, by a combination of NMR and fluorescence spectroscopy methods, we find that vesicular synaptobrevin-2 (syb-2) in its monomeric prefusion conformation shows high flexibility, characteristic for an IDP, but also a high dyn

SUBMITTER: Lakomek NA 

PROVIDER: S-EPMC6500178 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature