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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor

Goedele N Maertens1, Selma El Messaoudi-Aubert, Sarah Elderkin

  • 1Cancer Research UK, London Research Institute, London, UK.

The EMBO Journal
|July 6, 2010
PubMed

Insights

Two ubiquitin-specific proteases, USP7 and USP11, interact with Polycomb repressive complex 1 (PRC1) and regulate its function. Their absence causes tumor suppressor de-repression and cell cycle arrest.

Area of Science:

  • Epigenetics and transcriptional regulation.
  • Cellular senescence and tumor suppression.

Background:

  • Polycomb repressive complex 1 (PRC1) is crucial for transcriptional repression.
  • PRC1 mediates histone H2A mono-ubiquitination via Posterior sex combs (Psc) and Sex combs extra (Sce) proteins.

Purpose of the Study:

  • To investigate the interaction of ubiquitin-specific proteases (USPs) with human PRC1 complexes.
  • To elucidate the role of USP7 and USP11 in PRC1 function and epigenetic regulation.

Main Methods:

  • Co-purification of USP7 and USP11 with human PRC1 components.
  • Gene ablation of USP7 or USP11 in primary human fibroblasts.
  • Analysis of INK4a tumor suppressor de-repression and PRC1 binding.
  • Investigation of Psc and Sce protein ubiquitination and turnover.

Main Results:

  • USP7 and USP11 directly interact with PRC1 components, including Psc orthologues MEL18 and BMI1.
  • Ablation of USP7 or USP11 leads to INK4a de-repression, loss of PRC1 binding, and senescence.
  • USP7 and USP11 control the ubiquitination status, turnover, and abundance of Psc and Sce proteins.

Conclusions:

  • USP7 and USP11 play a novel regulatory role in Polycomb complex function.
  • These USPs are critical for maintaining PRC1-mediated transcriptional repression and preventing cellular senescence.

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