Searchable abstracts of presentations at key conferences in endocrinology

ea0016s8.3 | Nuclear receptors | ECE2008

Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation

Metzger Eric , Yin Na , Wissmann Melanie , Kunowska Natalia , Friedrichs Nicolaus , Patnaik Debasis , Higgins Jonathan M G , Potier Noelle , Scheidtmann Karl-Heinz , Buettner Reinhard , Schule Roland

Post-translational modifications of histones such as methylation, acetylation, and phoshorylation regulate chromatin structure and gene expression. However, phosphorylation of histone H3 at threonine 11 (H3T11ph) has not been linked to transcriptional regulation. Here we show that protein kinase C-related kinase 1 (PRK1) phosphorylates H3T11 upon ligand-dependent recruitment to androgen receptor (AR) target genes. PRK1 is pivotal to AR function since PRK1 knockdown by RNAi or ...