Ca²⁺-Triggered (de)ubiquitination Events in Synapses.

ABSTRACT: Neuronal communication relies on neurotransmitter release from synaptic vesicles (SVs), whose dynamics are controlled by Ca²⁺-dependent pathways, as many thoroughly studied phosphorylation cascades. However, little is known about other post-translational modifications, such as ubiquitination. To address this, we analyzed resting and stimulated synaptosomes (isolated synapses) by quantitative mass spectrometry. We identified more than 5000 ubiquitination sites on ∼2000 proteins, the majority of which participate in SV recycling processes. Several proteins showed significant changes in ubiquitination in response to Ca²⁺ influx, with the most pronounced changes in CaMKIIα and the clathrin adaptor protein AP180. To validate this finding, we generated a CaMKIIα mutant lack

SUBMITTER: Ainatzi S 

PROVIDER: S-EPMC12008530 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature