Ubiquitin-dependent protein degradation is necessary for long-term plasticity and memory

Abstract

Synaptic plasticity is considered as a basis of learning and memory and, in its turn, is associated with the reconstruction of molecular complexes in the preand postsynaptic parts. One of the means of this reconstruction is ubiquitin-dependent degradation of proteins in proteasomes, which leads to local elimination of preliminarily defined proteins–targets strictly within a certain time period in order to subsequently modify molecular complexes, such as postsynaptic density, the presynaptic apparatus of neuromediator release, and the receptor apparatus of preand postsynaptic membranes. Here, we review the bases of the organization of ubiquitin-dependent protein degradation of proteins in proteasomes and its role in synaptic plasticity and consolidation, reconsolidation, and the extinction of memory. In addition, one section is focused on the analysis of novel data on the mechanisms of the regulation of ubiquitin-dependent protein degradation, because knowledge on the mechanisms of regulation helps one to better understand how the process of protein degradation interacts with other intracellular processes in the cell.