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Related Experiment Video

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

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Published on: January 29, 2018

The polycomb repressive complex 2 is a potential target of SUMO modifications.

Eva Madi Riising1, Roberto Boggio, Susanna Chiocca

  • 1Biotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.

Plos One
|July 17, 2008
PubMed
Summary

Researchers discovered that sumoylation, a protein modification, affects Polycomb Repressive Complex 2 (PRC2) components like SUZ12 and EZH2. This finding suggests a new way to regulate PRC2

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Biochemistry

Background:

  • Polycomb Repressive Complex 2 (PRC2) is crucial for transcriptional repression via histone methylation.
  • PRC2 regulates cell proliferation, development, and tumor suppressor genes.
  • Dysregulation of PRC2 components is implicated in human cancers.

Purpose of the Study:

  • To investigate novel post-translational modifications of PRC2 components.
  • To explore the role of sumoylation in PRC2 function and regulation.

Main Methods:

  • In vitro and in vivo sumoylation assays for SUZ12 and EZH2.
  • Mapping of SUZ12 sumoylation sites.
  • Interaction studies with UBC9 and PIASXbeta.

Main Results:

  • SUZ12 and EZH2 were found to be sumoylated both in vitro and in vivo.
  • The major sumoylation site on SUZ12 was identified.
  • SUZ12 interacts with UBC9 and PIASXbeta, with PIASXbeta enhancing SUZ12 sumoylation.

Conclusions:

  • Sumoylation represents a novel post-translational modification of PRC2 components.
  • This modification offers a potential mechanism for modulating PRC2 activity.
  • Further research is needed to elucidate the physiological relevance of SUZ12 and EZH2 sumoylation in epigenetic regulation.