Ontology highlight
ABSTRACT:
SUBMITTER: Geng H
PROVIDER: S-EPMC3471753 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Geng Hao H Liu Qiong Q Xue Changhui C David Larry L LL Beer Tomasz M TM Thomas George V GV Dai Mu-Shui MS Qian David Z DZ
The Journal of biological chemistry 20120820 42
Lysine acetylation regulates protein stability and function. p300 is a component of the HIF-1 transcriptional complex and positively regulates the transactivation of HIF-1. Here, we show a novel molecular mechanism by which p300 facilitates HIF-1 activity. p300 increases HIF-1α (HIF1α) protein acetylation and stability. The regulation can be opposed by HDAC1, but not by HDAC3, and is abrogated by disrupting HIF1α-p300 interaction. Mechanistically, p300 specifically acetylates HIF1α at Lys-709, w ...[more]