JMJD8 Functions as a Novel AKT1 Lysine Demethylase

被引:5
|
作者
Wang, Yujuan [1 ]
Zhang, Yaoyao [1 ,2 ]
Li, Zehua [1 ,2 ]
Wang, Junfeng [1 ,3 ]
机构
[1] Chinese Acad Sci, Hefei Inst Phys Sci, High Magnet Field Lab, CAS Key Lab High Magnet Field & Ion Beam Phys Biol, Hefei 230031, Peoples R China
[2] Univ Sci & Technol China, Grad Sch, Sci Isl Branch, Hefei 230026, Peoples R China
[3] Anhui Univ, Inst Phys Sci & Informat Technol, Hefei 230601, Peoples R China
基金
中国国家自然科学基金;
关键词
JMJD8; demethylase; AKT1; tri-methylated lysine; JmjC domain; HISTONE; FAMILY;
D O I
10.3390/ijms24010460
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
JMJD8 is a protein from the JMJD family that only has the JmjC domain. Studies on the function of JMJD8 indicate that JMJD8 is involved in signaling pathways, including AKT/NF-kappa B, and thus affects cell proliferation and development. Here, we reported the activity of JMJD8 as a non-histone demethylase. We investigated the demethylation of JMJD8 on trimethylated lysine of AKT1 in vivo and in vitro using trimethylated AKT1 short peptide and AKT1 protein, and we tracked the regulation of JMJD8 on AKT1 activity at the cellular level. The results showed that JMJD8, a mini lysine demethylase, altered AKT1 protein function via changing its degree of methylation.
引用
收藏
页数:11
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