Ontology highlight
ABSTRACT:
SUBMITTER: Huang H
PROVIDER: S-EPMC6029451 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Huang He H Tang Shuang S Ji Ming M Tang Zhanyun Z Shimada Miho M Liu Xiaojing X Qi Shankang S Locasale Jason W JW Roeder Robert G RG Zhao Yingming Y Li Xiaoling X
Molecular cell 20180501 4
Lysine 2-hydroxyisobutyrylation (Khib) is an evolutionarily conserved and widespread histone mark like lysine acetylation (Kac). Here we report that p300 functions as a lysine 2-hyroxyisobutyryltransferase to regulate glycolysis in response to nutritional cues. We discovered that p300 differentially regulates Khib and Kac on distinct lysine sites, with only 6 of the 149 p300-targeted Khib sites overlapping with the 693 p300-targeted Kac sites. We demonstrate that diverse cellular proteins, parti ...[more]