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Biochim Biophys Acta. 2008 Aug;1779(8):495-506. doi: 10.1016/j.bbagrm.2007.12.010. Epub 2008 Jan 5.

Roles of ubiquitination at the synapse.

Author information

1
Department of Neurology, Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University, Nashville, TN 37235-1634, USA.

Abstract

The ubiquitin proteasome system (UPS) was first described as a mechanism for protein degradation more than three decades ago, but the critical roles of the UPS in regulating neuronal synapses have only recently begun to be revealed. Targeted ubiquitination of synaptic proteins affects multiple facets of the synapse throughout its life cycle; from synaptogenesis and synapse elimination to activity-dependent synaptic plasticity and remodeling. The recent identification of specific UPS molecular pathways that act locally at the synapse illustrates the exquisite specificity of ubiquitination in regulating synaptic protein trafficking and degradation events. Synaptic activity has also been shown to determine the subcellular distribution and composition of the proteasome, providing additional mechanisms for locally regulating synaptic protein degradation. Together these advances reveal that tight control of protein turnover plays a conserved, central role in establishing and modulating synapses in neural circuits.

PMID:
18222124
PMCID:
PMC2668815
DOI:
10.1016/j.bbagrm.2007.12.010
[Indexed for MEDLINE]
Free PMC Article

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