Ontology highlight
ABSTRACT:
SUBMITTER: Kuroda T
PROVIDER: S-EPMC3061030 | biostudies-literature | 2011 Mar
REPOSITORIES: biostudies-literature
The EMBO journal 20110204 6
A number of external and internal insults disrupt nucleolar structure, and the resulting nucleolar stress stabilizes and activates p53. We show here that nucleolar disruption induces acetylation and accumulation of p53 without phosphorylation. We identified three nucleolar proteins, MYBBP1A, RPL5, and RPL11, involved in p53 acetylation and accumulation. MYBBP1A was tethered to the nucleolus through nucleolar RNA. When rRNA transcription was suppressed by nucleolar stress, MYBBP1A translocated to ...[more]