Protein homeostasis and synaptic plasticity

Abstract

It is clear that de novo protein synthesis has an important function in synaptic transmission and plasticity. A substantial amount of work has shown that mRNA translation in the hippocampus is spatially controlled and that dendritic protein synthesis is required for different forms of long-term synaptic plasticity. More recently, several studies have highlighted a function for protein degradation by the ubiquitin proteasome system in synaptic plasticity. These observations suggest that changes in synaptic transmission involve extensive regulation of the synaptic proteome. Here, we review experimental data supporting the idea that protein homeostasis is a regulatory motif for synaptic plasticity.

Figure 1

Local protein synthesis and degradation in a hippocampal neurons. Protein concentration is given by the rate of synthesis and degradation in the different cellular compartments. (A) Cell body and (B, C) distal dendrites. Under steady state (B), the ribosomes and the proteasomes are mainly localized to the dendritic shaft. Activation of synapses leads to the recruitment of ribosomes and proteasomes to dendritic spines (C), where they cooperate to modulate the local proteome.