Elucidation of chromatin dynamics by an energy sensor histone demethylase

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K13042
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Applied health science
• Research Institution: The University of Tokyo
• Principal Investigator: SAKAI Juro 東京大学, 先端科学技術研究センター, 教授 (80323020)
• Co-Investigator(Renkei-kenkyūsha): KAWAMURA Takeshi 東京大学, アイソトープ総合センター, 准教授 (70306835) ; KIMURA Hiroshi 東京工業大学, 生命理工学研究科, 教授 (30241392) ; ABURATANI Hiroyuki 東京大学, 先端科学技術研究センター, 教授 (10202657) ; INAGAKI Takeshi 群馬大学, 生体調節研究所, 教授 (10507825) ; MATSUMURA Yoshihiro 東京大学, 先端科学技術研究センター, 准教授 (20375257) ; ABE Yohei 東京大学, 先端科学技術研究センター, 学振特別研究員 (80771063)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: ヒストン脱メチル化酵素 / 栄養 / AMPキナーゼ / 飢餓時のエピゲノム変化

Outline of Final Research Achievements

AMP Activated Protein Kinase (AMPK) is a serine / threonine phosphorylating enzyme and plays an extremely important role in metabolism, cell proliferation and reprogramming as an intracellular energy sensor. Since histone demethylase JMJD1A has multiple motifs of AMPK from “ScanSite”, we analyzed whether AMPK phosphorylated JMJD1A and was functioning. The JMJD1A recombinant protein was found to be phosphorylated AMP dependent in vitro by Phos-tag gel separation and immunoblotting (IB) with JMJD1A antibody and IB analysis using AMPK substrate antibody. Furthermore, phospho-proteomic analysis demonstrated that there are more than ten serine and/or threonine residues phosphorylated by AMPK. Identification of phosphorylated amino acid residues of endogenous JMJD1A by AMPK is still on the way.

Free Research Field

代謝医学・分子生理学