Chapter title |
Assessing the Role of Paralog-Specific Sumoylation of HDAC1
|
---|---|
Chapter number | 24 |
Book title |
HDAC/HAT Function Assessment and Inhibitor Development
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6527-4_24 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6525-0, 978-1-4939-6527-4
|
Authors |
Simona Citro, Susanna Chiocca |
Abstract |
Attachment of ubiquitin or ubiquitin-like (Ubl) modifiers, such as the small ubiquitin-related modifier SUMO, is a posttranslational modification (PTM) that reversibly regulates the function and the stability of target proteins. The SUMO paralogs SUMO1 and SUMO2/3, although sharing a common conjugation pathway, seem to play different roles in the cell. Many regulatory mechanisms, which contribute to SUMO-paralog-specific modification, have emerged. We have recently found that cell environment affects SUMO-paralog-specific sumoylation of HDAC1, whose conjugation to SUMO1 and not to SUMO2 facilitates its protein turnover. Here, we describe how to identify SUMO-paralog-specific conjugation of HDAC1 and how the different expression of SUMO E3 ligases in the cell plays an important role in this mechanism. |
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Geographical breakdown
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Unknown | 1 | 100% |
Demographic breakdown
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Lecturer > Senior Lecturer | 1 | 100% |
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Biochemistry, Genetics and Molecular Biology | 1 | 100% |