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. 2017:1510:329-337.
doi: 10.1007/978-1-4939-6527-4_24.

Assessing the Role of Paralog-Specific Sumoylation of HDAC1

Simona Citro  1 , Susanna Chiocca  2
Affiliations

Assessing the Role of Paralog-Specific Sumoylation of HDAC1

Simona Citro et al. Methods Mol Biol. 2017.

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.

Keywords: HDAC; HDAC1; PIASy; PTM; SUMO1; SUMO2/3.

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