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Ca2+-Triggered (de)ubiquitination Events in Synapses
Sofia Ainatzi1, Svenja V Kaufmann1, Ivan Silbern1
1Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Goettingen, Germany; Bioanalytics, Institute of Clinical Chemistry, University Medical Center, Goettingen, Germany.
Molecular & Cellular Proteomics : MCP
|March 15, 2025
Summary
Ubiquitination, a protein modification, regulates synaptic vesicle recycling and neuronal communication. This study reveals how calcium influx affects protein ubiquitination, impacting synaptic function.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Neuronal communication depends on synaptic vesicle (SV) release, primarily regulated by calcium (Ca2+)-dependent phosphorylation.
- The role of other post-translational modifications, like ubiquitination, in SV dynamics remains largely unexplored.
Purpose of the Study:
- To investigate the role of ubiquitination in regulating synaptic vesicle recycling and neuronal function.
- To identify ubiquitination changes in response to calcium influx during synaptic activity.
Main Methods:
- Quantitative mass spectrometry was used to analyze ubiquitination sites in resting and stimulated synaptosomes.
- A CaMKIIα mutant lacking a specific ubiquitination site (K291) was generated and analyzed in neuronal and non-neuronal cells.
Main Results:
- Over 5000 ubiquitination sites were identified on approximately 2000 proteins, many involved in SV recycling.
- Ca2+ influx significantly altered ubiquitination patterns, notably for CaMKIIα and AP180.
- K291 ubiquitination of CaMKIIα was found to influence its synaptic function.
Conclusions:
- Ubiquitination is a significant post-translational modification involved in synaptic vesicle recycling.
- Calcium-dependent ubiquitination dynamically regulates synaptic function, particularly through kinases like CaMKIIα.
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