Abstract
Protein SUMOylation regulates multiple processes involved in the differentiation and maturation of cells and tissues during development. Despite this, relatively little is known about the spatial and temporal regulation of proteins that mediate SUMOylation and deSUMOylation in the CNS. Here we monitor the expression of key SUMO pathway proteins and levels of substrate protein SUMOylation in the forebrain and cerebellum of Wistar rats during development. Overall, the SUMOylation machinery is more highly-expressed at E18 and decreases thereafter, as previously described. All of the proteins investigated are less abundant in adult than in embryonic brain. Furthermore, we show for first time that the profiles differ between cerebellum and cerebrum, indicating differential regional regulation of some of the proteins analysed. These data provide further basic observation that may open a new perspective of research about the role of SUMOylation in the development of different brain regions.
Highlights
SUMOylation is the covalent attachment of a 97-residue protein, SUMO (Small Ubiquitinrelated MOdifier), to lysine residues on target proteins
In order to address how profiles of protein SUMOylation and SUMO pathway proteins are altered in cerebellum and cerebrum during development, we homogenised rat brains at SUMOylation during rat brain development various stages of development
Due to their small size, the embryonic day 18 (E18) brains were not dissected into cerebrum and cerebellum, and instead we prepared whole homogenate from these brains
Summary
SUMOylation is the covalent attachment of a 97-residue protein, SUMO (Small Ubiquitinrelated MOdifier), to lysine residues on target proteins. SUMOylation is best characterised for modifying nuclear proteins involved in genome integrity, nuclear structure and transcription [1, 2] but it is clear that SUMOylation is important for extranuclear signal transduction, trafficking and modification of cytosolic and integral membrane proteins. Several hundred SUMOylation substrates have been validated and many more candidate substrates have been identified by proteomic studies [3,4,5]
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