Related Experiment Video
Updated: May 23, 2025

Quantification of γH2AX Foci in Response to Ionising Radiation
Published on: April 6, 2010
Global γH2AX phosphorylation in Drosophila is reversed by the phosphatase Mts
Zivkos Apostolou1, Silke Krause1, Peter B Becker1
1Biomedical Center, Molecular Biology Division, Ludwig-Maximilians-Universität München, Munich, Germany.
Abstract:
The phosphorylation of the histone variant H2AX to form γH2AX is an early and critical histone modification during the DNA damage response. This phosphorylation has proven to be a highly specific molecular marker for tracking the initiation and resolution of DNA damage. In this study, we investigate the roles of three phosphatases in removing the 'γ' phospho-epitope from H2AX in Drosophila Kc167 cells. We found that the bulk of the X-ray-induced γH2AX signal is erased by the PP2A-type phosphatase MTS (microtubule star).
Related Concept Videos
Activation and Inactivation of G Proteins
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Amplifying Signals via Enzymatic Cascade

