Phosphoproteomic analysis reveals that PP4 dephosphorylates KAP-1 impacting the DNA damage response

• Published in: The EMBO journal Vol. 31; no. 10; pp. 2403 - 2415
• Main Authors: Lee, Dong-Hyun, Goodarzi, Aaron A, Adelmant, Guillaume O, Pan, Yunfeng, Jeggo, Penelope A, Marto, Jarrod A, Chowdhury, Dipanjan
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 16.05.2012; Blackwell Publishing Ltd; Nature Publishing Group
• Subjects: Cell Division; checkpoint; Deoxyribonucleic acid; DNA; DNA - radiation effects; DNA Damage; DNA damage signalling; double-strand DNA break; Enzymes; G2 Phase; HeLa Cells; Humans; Ionizing radiation; Lesions; Models, Biological; Molecular biology; Mutants; phosphatase; Phosphoprotein Phosphatases - metabolism; Phosphorylation; Protein Processing, Post-Translational; Radiation, Ionizing; Repressor Proteins - metabolism; Signal transduction; Substrates; Tripartite Motif-Containing Protein 28

Protein phosphatase PP4C has been implicated in the DNA damage response (DDR), but its substrates in DDR remain largely unknown. We devised a novel proteomic strategy for systematic identification of proteins dephosphorylated by PP4C and identified KRAB‐domain‐associated protein 1 (KAP‐1) as a subst...