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Neurotransmission

Playing tag!

Nature Reviews Neuroscience volume 11, page 297 (2010)Cite this article

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The tagging of proteins with ubiquitin in mammalian cells involves hundreds of enzymes that confer specificity. This led the authors to hypothesize that protein ubiquitylation — in addition to having a role in degradation — may modulate synaptic activity.

First, the authors tested the effect of proteasome inhibitors (MG132 and clasto-lactacystin β-lactone) on synaptic transmission in cultured rodent hippocampal neurons. They measured the changes in frequency (reflecting a presynaptic effect) and amplitude (reflecting a postsynaptic effect) of miniature postsynaptic currents (mPSCs) before and after application of the proteasome inhibitors. They observed changes in the frequency but not in the amplitude of inhibitory and excitatory mPSCs within 10 minutes of inhibitor application, which indicates that the UPS regulates presynaptic release.

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References

ORIGINAL RESEARCH PAPER

  1. Rinetti, G. V. & Schweizer, F. E. Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons. J. Neurosci. 30, 3157–3166 (2010)

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FURTHER READING

  1. Tai, H.-C. & Schuman, E. M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nature Rev. Neurosci. 9, 826–838 (2008)

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Authors
  1. Claudia Wiedemann
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Wiedemann, C. Playing tag!. Nat Rev Neurosci 11, 297 (2010). https://doi.org/10.1038/nrn2842

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