Independent regulation of synaptic size and activity by the anaphase-promoting complex

Cell. 2004 Nov 24;119(5):707-18. doi: 10.1016/j.cell.2004.11.028.

Abstract

Neuronal plasticity relies on tightly regulated control of protein levels at synapses. One mechanism to control protein abundance is the ubiquitin-proteasome degradation system. Recent studies have implicated ubiquitin-mediated protein degradation in synaptic development, function, and plasticity, but little is known about the regulatory mechanisms controlling ubiquitylation in neurons. In contrast, ubiquitylation has long been studied as a central regulator of the eukaryotic cell cycle. A critical mediator of cell-cycle transitions, the anaphase-promoting complex/cyclosome (APC/C), is an E3 ubiquitin ligase. Although the APC/C has been detected in several differentiated cell types, a functional role for the complex in postmitotic cells has been elusive. We describe a novel postmitotic role for the APC/C at Drosophila neuromuscular synapses: independent regulation of synaptic growth and synaptic transmission. In neurons, the APC/C controls synaptic size via a downstream effector Liprin-alpha; in muscles, the APC/C regulates synaptic transmission, controlling the concentration of a postsynaptic glutamate receptor.

Publication types

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

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / growth & development*
  • Drosophila melanogaster / metabolism
  • Drosophila melanogaster / ultrastructure
  • Intracellular Signaling Peptides and Proteins
  • Larva / growth & development
  • Larva / metabolism
  • Larva / ultrastructure
  • Microscopy, Electron, Transmission
  • Mutation / genetics
  • Nervous System / growth & development*
  • Nervous System / metabolism
  • Nervous System / ultrastructure
  • Neuromuscular Junction / growth & development*
  • Neuromuscular Junction / metabolism
  • Neuromuscular Junction / ultrastructure
  • Neuronal Plasticity / physiology*
  • Phosphoproteins / metabolism
  • Receptor Aggregation / physiology
  • Receptors, Glutamate / metabolism
  • Synaptic Membranes / metabolism
  • Synaptic Transmission / physiology
  • Ubiquitin / metabolism
  • Ubiquitin-Protein Ligase Complexes / genetics
  • Ubiquitin-Protein Ligase Complexes / metabolism*
  • Up-Regulation / genetics

Substances

  • Drosophila Proteins
  • Intracellular Signaling Peptides and Proteins
  • Liprin-alpha protein, Drosophila
  • Phosphoproteins
  • Receptors, Glutamate
  • Ubiquitin
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome