Posttranslational modifications critically support nervous system development and maintenance. Protein ubiquitination is one type of posttranslational modification that serves a dominant role in marking proteins for degradation. This is accomplished via the attachment of the 76-amino acid protein ubiquitin on lysine residues, oftentimes as a single ubiquitin attachment or as an assembly of polymeric homogenous chains. While protein ubiquitination and degradation pathways have been demonstrated to be critical for the regulation of neural processes, their disruption has been associated with numerous neurological disorders. It is known that ubiquitination can occur on non-lysine residues, and recent findings have demonstrated that ubiquitin chains can be assembled via heterogeneous linkages. New literature has also unveiled new ways to degrade proteins, which can be initiated by ubiquitin-dependent or ubiquitin-independent mechanisms.

The goal of this Research Topic is to bring together ubiquitin and protein degradation experts from all fields of science to provide new insights into non-canonical roles of protein ubiquitination and degradation. The unveiling of these new mechanisms will assist in elucidating their neurobiological significance.

Topics pertaining to this call will focus on aspects of ubiquitin signaling that go against the classic signaling “dogma”. Topics can include but are not limited to:

• substrate ubiquitination on non-lysine residues
• newly defined functions of ubiquitin chains
• heterogenous ubiquitin chain assembly and disassembly
• identification of new proteins that regulate protein ubiquitination or degradation
• structural and functional studies related to non-canonical proteasome function
• lipid-based modes of protein degradation
• spatially restricted regulation of protein ubiquitination and degradation

Research studies can include in vitro and in vivo approaches but must, to some degree, provide insight into nervous system regulation.

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Frontiers in Cellular Neuroscience

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