4.3 Article

Histone H2A.X Tyr142 phosphorylation: A novel sWItCH for apoptosis?

Journal

DNA REPAIR
Volume 8, Issue 7, Pages 873-876

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2009.04.003

Keywords

DNA repair; Chromatin; H2A.X; Kinase; WICH complex; Apoptosis; DNA damage response

Funding

  1. Swiss National Foundation
  2. UBS AG 'im Auftrag eines Kunden
  3. Canton of Zijrich

Ask authors/readers for more resources

Histone H2A.X phosphorylation on Set 139 in response to DNA damage is the major signal for the assembly of the so-called gamma H2A.X chromatin domain, a region surrounding an unrepaired DNA double-strand break that is characterized by the accumulation of a large number of DNA damage response proteins. However, it is not yet clear how this event is regulated in space and time. The recent discovery of H2A.X Tyr142 phosphorylation by the WICH complex and its dephosphorylation by the EYA1/3 phosphatases may provide substantial novel insight into this process. WSTF, a subunit of the WICH complex bears a novel kinase domain at its N-terminus that constitutively targets WAY on Tyr142. This novel histone modification appears to determine the relative recruitment of either DNA repair or pro-apoptotic factors to sites of DNA damage. Thus, the balance of WAY Tyr142 phosphorylation/dephosphorylation may constitute a novel switch mechanism to determine cell fate after DNA damage. (C) 2009 Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.3
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
Article Genetics & Heredity

The impact of chromatin on double-strand break repair: Imaging tools and discoveries

Marit A. E. van Bueren, Aniek Janssen

Summary: Eukaryotic nuclei rely on multiple repair pathways to accurately repair DNA damage, particularly in chromatin domains enriched for repetitive DNA sequences. Tailored repair mechanisms are necessary to maintain genome stability in these domains.

DNA REPAIR (2024)