Ubiquitin-dependent regulation of the synapse

Aaron DiAntonio, Linda Hicke

Research output: Contribution to journalReview article

140 Scopus citations


Posttranslational modification of cellular proteins by the covalent attachment of ubiquitin regulates protein stability, activity, and localization. Ubiquitination is rapid and reversible and is a potent mechanism for the spatial and temporal control of protein activity. By sculpting the molecular composition of the synapse, this versatile posttranslational modification shapes the pattern, activity, and plasticity of synaptic connections. Synaptic processes regulated by ubiquitination, as well as ubiquitination enzymes and their targets at the synapse, are being identified by genetic, biochemical, and electrophysiological analyses. This work provides tantalizing hints that neuronal activity collaborates with ubiquitination pathways to regulate the structure and function of synapses.

Original languageEnglish
Pages (from-to)223-246
Number of pages24
JournalAnnual Review of Neuroscience
StatePublished - Aug 20 2004


  • Axon guidance
  • Proteasome
  • Protein degradation
  • Synaptic plasticity
  • Synaptic transmission

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