Cellular functions and molecular mechanisms of non-lysine ubiquitination

Amie J. McClellan; Sophie Heiden Laugesen; Lars Ellgaard

doi:10.1098/rsob.190147

Cellular functions and molecular mechanisms of non-lysine ubiquitination

Amie J. McClellan, Sophie Heiden Laugesen, Lars Ellgaard

Biomolecular Sciences

24 Citations (Scopus)

12 Downloads (Pure)

Abstract

Protein ubiquitination is of great cellular importance through its central role in processes such as degradation, DNA repair, endocytosis and inflammation. Canonical ubiquitination takes place on lysine residues, but in the past 15 years non-lysine ubiquitination on serine, threonine and cysteine has been firmly established. With the emerging importance of non-lysine ubiquitination, it is crucial to identify the responsible molecular machinery and understand the mechanistic basis for non-lysine ubiquitination. Here, we first provide an overview of the literature that has documented non-lysine ubiquitination. Informed by these examples, we then discuss the molecular mechanisms and cellular implications of non-lysine ubiquitination, and conclude by outlining open questions and future perspectives in the field.

Original language	English
Article number	190147
Journal	Open Biology
Volume	9
Issue number	9
Number of pages	16
ISSN	2046-2441
DOIs	https://doi.org/10.1098/rsob.190147
Publication status	Published - 2019

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rsob.190147Final published version, 885 KBLicence: CC BY

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AU - Laugesen, Sophie Heiden

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N2 - Protein ubiquitination is of great cellular importance through its central role in processes such as degradation, DNA repair, endocytosis and inflammation. Canonical ubiquitination takes place on lysine residues, but in the past 15 years non-lysine ubiquitination on serine, threonine and cysteine has been firmly established. With the emerging importance of non-lysine ubiquitination, it is crucial to identify the responsible molecular machinery and understand the mechanistic basis for non-lysine ubiquitination. Here, we first provide an overview of the literature that has documented non-lysine ubiquitination. Informed by these examples, we then discuss the molecular mechanisms and cellular implications of non-lysine ubiquitination, and conclude by outlining open questions and future perspectives in the field.

AB - Protein ubiquitination is of great cellular importance through its central role in processes such as degradation, DNA repair, endocytosis and inflammation. Canonical ubiquitination takes place on lysine residues, but in the past 15 years non-lysine ubiquitination on serine, threonine and cysteine has been firmly established. With the emerging importance of non-lysine ubiquitination, it is crucial to identify the responsible molecular machinery and understand the mechanistic basis for non-lysine ubiquitination. Here, we first provide an overview of the literature that has documented non-lysine ubiquitination. Informed by these examples, we then discuss the molecular mechanisms and cellular implications of non-lysine ubiquitination, and conclude by outlining open questions and future perspectives in the field.

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Cellular functions and molecular mechanisms of non-lysine ubiquitination

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