Takashi Ito

TL;DR: It is shown that ionizing irradiation induces TIP60 acetylation of histone H2AX, a variant form of H2A known to be phosphorylated following DNA damage, and ubiquitination via the ubiquitin-conjugating enzyme UBC13, which is induced by DNA damage.

TL;DR: The identification of a human multiprotein complex (WINAC) that directly interacts with the vitamin D receptor (VDR) through the Williams syndrome transcription factor (WSTF) suggests that WINAC dysfunction contributes to Williams syndrome, which could therefore be considered, at least in part, a chromatin-remodeling factor disease.

TL;DR: It is demonstrated that multiple effector mechanisms including H2A ubiquitination and chromatin compaction combine to mediate PRC1-dependent repression of genes that are crucial for the maintenance of ESC identity.

TL;DR: A novel mode of trans-histone cross-talk is revealed, in which H2A ubiquitylation controls the di- and trimethylation of H3K4, resulting in regulation of transcriptional initiation.

TL;DR: The results strongly suggest that Ser-386 is the target of the IRF-3 kinase and critical determinant for the activation of IRf-3.