Abstract
BackgroundSmall Ubiquitin-like MOdifier protein (SUMO) is a key regulator of nuclear functions but little is known regarding the role of the post-translational modification sumoylation outside of the nucleus, particularly in the Central Nervous System (CNS).Methodology/Principal FindingsHere, we report that the expression levels of SUMO-modified substrates as well as the components of the sumoylation machinery are temporally and spatially regulated in the developing rat brain. Interestingly, while the overall sumoylation is decreasing during brain development, there are progressively more SUMO substrates localized at synapses. This increase is correlated with a differential redistribution of the sumoylation machinery into dendritic spines during neuronal maturation.Conclusions/SignificanceOverall, our data clearly demonstrate that the sumoylation process is developmentally regulated in the brain with high levels of nuclear sumoylation early in the development suggesting a role for this post-translational modification during the synaptogenesis period and a redistribution of the SUMO system towards dendritic spines at a later developmental stage to modulate synaptic protein function.
Highlights
Neurons are highly specialized cells whose connectivity at synapses enables rapid information transfer in the brain
Sumoylation is seen as an important protein modification for the regulation of many proteins in the Central Nervous System (CNS)
We focused on two aspects of the sumoylation process in the CNS: the developmental regulation of Small Ubiquitin-like MOdifier protein (SUMO)-modified protein and sumoylation enzyme expression and the dendritic reorganization of sumoylation and desumoylation enzymes during neuronal maturation
Summary
Neurons are highly specialized cells whose connectivity at synapses enables rapid information transfer in the brain. Synapse formation and elimination as well as synaptic transmission and plasticity largely depend on the correct targeting and arrangement of complex protein networks on both sides of the synapse. These networks are organized in an array of scaffolding and adaptors molecules, presenting multiple protein-protein interaction domains to anchor and position effectors such as neurotransmitter receptors or components of signaling pathways and their associated regulators. The spatiotemporal and functional regulation of these protein complexes is still largely unknown These dynamic processes are often regulated by post-translational modifications (PTM) such as phosphorylation or ubiquitination [1]. Small Ubiquitin-like MOdifier protein (SUMO) is a key regulator of nuclear functions but little is known regarding the role of the post-translational modification sumoylation outside of the nucleus, in the Central Nervous System (CNS)
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