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Journal Article

An abundance of free regulatory (19 S) proteasome particles regulates neuronal synapses

MPS-Authors

Sun,  Chao
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Desch,  Kristina
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Nassim-Assir,  Belquis
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Giandomenico,  Stefano L
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Nemcova,  Paulina
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Langer,  Julian D
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;
Max Planck Institute for Biophysics, 60438 Frankfurt am Main, Germany.;

/persons/resource/persons208206

Schuman,  Erin M.       
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

External Resource

https://pubmed.ncbi.nlm.nih.gov/37228199/
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Citation

Sun, C., Desch, K., Nassim-Assir, B., Giandomenico, S. L., Nemcova, P., Langer, J. D., et al. (2023). An abundance of free regulatory (19 S) proteasome particles regulates neuronal synapses. Science, 380(6647). doi:10.1126/science.adf2018.


Cite as: https://hdl.handle.net/21.11116/0000-000D-3C7B-7
Abstract
The proteasome, the major protein-degradation machine in cells, regulates neuronal synapses and long-term information storage. Here, using super-resolution microscopy, we found that the two essential subcomplexes of the proteasome, the regulatory (19S) and catalytic (20S) particles, are differentially distributed within individual rat cortical neurons. We discovered an unexpected abundance of free 19S particles near synapses. The free neuronal 19S particles bind and deubiquitylate lysine 63-ubiquitin (Lys63-ub), a non-proteasome-targeting ubiquitin linkage. Pull-down assays revealed a significant overrepresentation of synaptic molecules as Lys63-ub interactors. Inhibition of the 19S deubiquitylase activity significantly altered excitatory synaptic transmission and reduced the synaptic availability of AMPA receptors at multiple trafficking points in a proteasome-independent manner. Together, these results reveal a moonlighting function of the regulatory proteasomal subcomplex near synapses.