Format

Send to

Choose Destination
Epigenetics. 2011 Feb;6(2):153-60. Epub 2011 Feb 1.

Histone tyrosine phosphorylation comes of age.

Author information

1
Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, FL, USA.

Erratum in

  • Epigenetics. 2011 Dec 1;6(12):1513.

Abstract

Histones were discovered over a century ago and have since been found to be the most extensively posttranslationally modified proteins, although tyrosine phosphorylation of histones had remained elusive until recently. The year 2009 proved to be a landmark year for histone tyrosine (Y) phosphorylation as five research groups independently discovered this modification. Three groups describe phosphorylation of Y142 in the variant histone H2A.X, where it may be involved in the cellular decision making process to either undergo DNA repair or apoptosis in response to DNA damage. Further, one group suggests that phosphorylation of histone H3 on Y99 is crucial for its regulated proteolysis in yeast, while another found that Y41 phosphorylation modulates chromatin architecture and oncogenesis in mammalian cells. These pioneering studies provide the initial conceptual framework for further analyses of the diverse roles of tyrosine phosphorylation on different histones, with far reaching implications for human health and disease.

PMID:
20935492
PMCID:
PMC3278784
DOI:
10.4161/epi.6.2.13589
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center