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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Acknowledgments
This work was supported by grants from Associazione Italiana per la Ricerca sul Cancro to Susanna Chiocca (AIRC IG5732, AIRC IG12075). SCi was supported by a fellowship from Fondazione Umberto Veronesi (FUV).
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Citro, S., Chiocca, S. (2017). Assessing the Role of Paralog-Specific Sumoylation of HDAC1. In: Krämer, O. (eds) HDAC/HAT Function Assessment and Inhibitor Development. Methods in Molecular Biology, vol 1510. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6527-4_24
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DOI: https://doi.org/10.1007/978-1-4939-6527-4_24
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