Ontology highlight
ABSTRACT:
SUBMITTER: Winter S
PROVIDER: S-EPMC2206135 | biostudies-literature | 2008 Jan
REPOSITORIES: biostudies-literature
Winter Stefan S Simboeck Elisabeth E Fischle Wolfgang W Zupkovitz Gordin G Dohnal Ilse I Mechtler Karl K Ammerer Gustav G Seiser Christian C
The EMBO journal 20071206 1
Interphase phosphorylation of S10 at histone H3 is linked to transcriptional activation of a specific subset of mammalian genes like HDAC1. Recently, 14-3-3 proteins have been described as detectors for this phosphorylated histone H3 form. Here, we report that 14-3-3 binding is modulated by combinatorial modifications of histone H3. S10 phosphorylation is necessary for an interaction, but additional H3K9 or H3K14 acetylation increases the affinity of 14-3-3 for histone H3. Histone H3 phosphoacet ...[more]