Abstract
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial in neurons because of their polarization, morphological complexity and functional specialization. SUMOylation has emerged as a major mediator of intranuclear and nucleo-cytoplasmic translocations of proteins involved in critical pathways such as circadian rhythm, apoptosis and protein degradation. In addition, SUMO-regulated re-localization of extranuclear proteins is required to sustain neuronal excitability and synaptic transmission. Thus, SUMOylation is a key arbiter of neuronal viability and function. Here, we provide an overview of recent advances in our understanding of regulation of neuronal protein localization and translocation by SUMO and highlight exciting areas of ongoing research.
Highlights
SUMOylation is the covalent attachment of a member of the SUMO family of proteins to one or more lysine residues on target proteins
This is supported by the finding that in acute inflammatory demyelinating polyneuropathy (AIDP) neurons, the glucocorticoid receptor (GR), itself a SUMO substrate, is localized to promyelocytic leukemia (PML) bodies, whereas in healthy cells GR does not localize to any nuclear foci [42,43]
SUMO2/3, which is involved in the localization of BMAL1 to PML bodies where it functions as a transcription factor [11]
Summary
SUMOylation is the covalent attachment of a member of the SUMO family of proteins to one or more lysine residues on target proteins. SUMOylation is best characterized for 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. The signaling pathways that orchestrate protein trafficking are necessarily sophisticated and multilayered and it has become evident that for many neuronal proteins SUMOylation is an important factor in regulating their localization and function under both physiological and pathophysiological conditions [7,8]. Outcome of SUMOylation formation of PML bodies, possible transcriptional regulation upon axonal damage [9,10]. Possible effects on synaptic transmission in the hippocampus, internalization and/or degradation of receptors [20,21]. Agonist-induced deSUMOylation potentially regulates internalization of receptor [22]
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