1. JMJD8 Functions as a Novel AKT1 Lysine Demethylase
- Author
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Yujuan Wang, Yaoyao Zhang, Zehua Li, and Junfeng Wang
- Subjects
Inorganic Chemistry ,Organic Chemistry ,JMJD8 ,demethylase ,AKT1 ,tri-methylated lysine ,JmjC domain ,General Medicine ,Physical and Theoretical Chemistry ,Molecular Biology ,Spectroscopy ,Catalysis ,Computer Science Applications - Abstract
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-κB, 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.
- Published
- 2022