Ubiquitin-dependent regulation of the synapse

Annu Rev Neurosci. 2004;27:223-46. doi: 10.1146/annurev.neuro.27.070203.144317.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Central Nervous System / cytology
  • Central Nervous System / enzymology
  • Central Nervous System / physiology*
  • Cysteine Endopeptidases / metabolism
  • Growth Cones / metabolism
  • Growth Cones / ultrastructure
  • Humans
  • Multienzyme Complexes / metabolism
  • Nerve Tissue Proteins / metabolism
  • Neural Pathways / cytology
  • Neural Pathways / enzymology
  • Neural Pathways / growth & development
  • Neuronal Plasticity / physiology*
  • Proteasome Endopeptidase Complex
  • Protein Processing, Post-Translational / physiology*
  • Synapses / enzymology
  • Synapses / physiology*
  • Synapses / ultrastructure
  • Synaptic Transmission / physiology
  • Ubiquitin / metabolism*

Substances

  • Multienzyme Complexes
  • Nerve Tissue Proteins
  • Ubiquitin
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex