4.6 Review

Histone Ubiquitination: An Integrative Signaling Platform in Genome Stability

Journal

TRENDS IN GENETICS
Volume 37, Issue 6, Pages 566-581

Publisher

CELL PRESS
DOI: 10.1016/j.tig.2020.12.005

Keywords

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Funding

  1. Swiss National Science Foundation [310030_184966]
  2. European Research Council [EU/ERC-851564]
  3. Swiss National Science Foundation (SNF) [310030_184966] Funding Source: Swiss National Science Foundation (SNF)

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This passage discusses the mechanisms in place to maintain genome stability, focusing on the central role of chromatin ubiquitination. It reviews specific histone ubiquitination events within the cellular DNA damage response, with emphasis on the recent discovery of Ub phosphorylation as a novel regulator. Exciting open questions for future research on the implications of histone (phospho)ubiquitination on chromatin structure are highlighted.
Complex mechanisms are in place to maintain genome stability. Ubiquitination of chromatin plays a central role in these mechanisms. The ever-growing complexity of the ubiquitin (Ub) code and of chromatin modifications and dynamics challenges our ability to fully understand how histone ubiquitination regulates genome stability. Here we review the current knowledge on specific, low-abundant histone ubiquitination events that are highly regulated within the cellular DNA damage response (DDR), with particular emphasis on the latest discovery of Ub phosphorylation as a novel regulator of the DDR signaling pathway. We discuss players involved and potential implications of histone (phospho)ubiquitination on chromatin structure, and we highlight exciting open questions for future research.

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