Assessing the role of paralog-specific sumoylation of HDAC1

Research output: Chapter in Book/Report/Conference proceedingChapter

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.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages329-337
Number of pages9
Volume1510
DOIs
Publication statusPublished - 2017

Publication series

NameMethods in Molecular Biology
Volume1510
ISSN (Print)10643745

Keywords

  • HDAC
  • HDAC1
  • PIASy
  • PTM
  • SUMO1
  • SUMO2/3

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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