Ca²⁺ binding to synapsin I regulates resting Ca²⁺ and recovery from synaptic depression in nerve terminals.

ABSTRACT: Synapsin I (SynI) is a synaptic vesicle (SV)-associated phosphoprotein that modulates neurotransmission by controlling SV trafficking. The SynI C-domain contains a highly conserved ATP binding site mediating SynI oligomerization and SV clustering and an adjacent main Ca²⁺ binding site, whose physiological role is unexplored. Molecular dynamics simulations revealed that the E373K point mutation irreversibly deletes Ca²⁺ binding to SynI, still allowing ATP binding, but inducing a destabilization of the SynI oligomerization interface. Here, we analyzed the effects of this mutation on neurotransmitter release and short-term plasticity in excitatory and inhibitory synapses from primary hippocampal neurons. Patch-clamp recordings showed an increase in the frequency of minia

SUBMITTER: Moschetta M 

PROVIDER: S-EPMC9678998 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature