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 Citationer (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.

Originalsprog	Engelsk
Artikelnummer	190147
Tidsskrift	Open Biology
Vol/bind	9
Udgave nummer	9
Antal sider	16
ISSN	2046-2441
DOI	https://doi.org/10.1098/rsob.190147
Status	Udgivet - 2019

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10.1098/rsob.190147Licens: CC BY

rsob.190147Forlagets udgivne version, 885 KBLicens: CC BY

Citationsformater

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AU - McClellan, Amie J.

AU - Laugesen, Sophie Heiden

AU - Ellgaard, Lars

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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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