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BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair

Ismail, Ismail Hassan, Andrin, Christi, McDonald, Darin, Hendzel, Michael J.·2010·Journal of Cell Biology
DOI 10.1083/jcb.201003034PMC PMC2953429
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Abstract

Polycomb group (PcG) proteins are major determinants of cell identity, stem cell pluripotency, and epigenetic gene silencing during development. The polycomb repressive complex 1, which contains BMI1, RING1, and RING2, functions as an E3-ubuiquitin ligase. We found that BMI1 and RING2 are recruited to sites of DNA double-strand breaks (DSBs) where they contribute to the ubiquitylation of γ-H2AX. In the absence of BMI1, several proteins dependent on ubiquitin signaling, including 53BP1, BRCA1, and RAP80, are impaired in recruitment to DSBs. Loss of BMI1 sensitizes cells to ionizing radiation to the same extent as loss of RNF8. The simultaneous depletion of both proteins revealed an additive increase in radiation sensitivity. These data uncover an unexpected link between the polycomb and the DNA damage response pathways, and suggest a novel function for BMI1 in maintaining genomic stability.

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  • PRCs are essential players in DNA damage repair via activation of damage response machinery proteins.

    “What is more, PRCs are essential players in DNA damage repair via the activation of damage response machinery proteins.134,135,136”

    From MiR-128-3p – a gray eminence of the human central nervous system (2024) · cites this paper as [135]

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Metadata

Authors
Ismail, I. H., Andrin, C., McDonald, D., & Hendzel, M. J.
Affiliations
Department of Oncology, University of Alberta, Edmonton, T6G 1Z2 Alberta, Canada 1
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2010-10-04
Volume
191
Issue
1
Pages
45-60
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201003034
PMC
PMC2953429
Cited by
255
References
6
Language
en

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