Cellular functions and molecular mechanisms of non-lysine ubiquitination
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 ha...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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The Royal Society
2019-09-01
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| Series: | Open Biology |
| Subjects: | |
| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.190147 |
| _version_ | 1811313461024522240 |
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| author | Amie J. McClellan Sophie Heiden Laugesen Lars Ellgaard |
| author_facet | Amie J. McClellan Sophie Heiden Laugesen Lars Ellgaard |
| author_sort | Amie J. McClellan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T10:54:07Z |
| format | Article |
| id | doaj.art-273d19b13ccc4dd0b0531c1892977369 |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-04-13T10:54:07Z |
| publishDate | 2019-09-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-273d19b13ccc4dd0b0531c18929773692022-12-22T02:49:34ZengThe Royal SocietyOpen Biology2046-24412019-09-019910.1098/rsob.190147190147Cellular functions and molecular mechanisms of non-lysine ubiquitinationAmie J. McClellanSophie Heiden LaugesenLars EllgaardProtein 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.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.190147endoplasmic reticulum-associated degradationmarch e3 ligasesprotein degradationserine/threonine ubiquitinationubiquitin–proteasome system |
| spellingShingle | Amie J. McClellan Sophie Heiden Laugesen Lars Ellgaard Cellular functions and molecular mechanisms of non-lysine ubiquitination Open Biology endoplasmic reticulum-associated degradation march e3 ligases protein degradation serine/threonine ubiquitination ubiquitin–proteasome system |
| title | Cellular functions and molecular mechanisms of non-lysine ubiquitination |
| title_full | Cellular functions and molecular mechanisms of non-lysine ubiquitination |
| title_fullStr | Cellular functions and molecular mechanisms of non-lysine ubiquitination |
| title_full_unstemmed | Cellular functions and molecular mechanisms of non-lysine ubiquitination |
| title_short | Cellular functions and molecular mechanisms of non-lysine ubiquitination |
| title_sort | cellular functions and molecular mechanisms of non lysine ubiquitination |
| topic | endoplasmic reticulum-associated degradation march e3 ligases protein degradation serine/threonine ubiquitination ubiquitin–proteasome system |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.190147 |
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