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JMJD8 Functions as a Novel AKT1 Lysine Demethylase
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 demethylas...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9820096/ https://www.ncbi.nlm.nih.gov/pubmed/36613903 http://dx.doi.org/10.3390/ijms24010460 |
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author | Wang, Yujuan Zhang, Yaoyao Li, Zehua Wang, Junfeng |
author_facet | Wang, Yujuan Zhang, Yaoyao Li, Zehua Wang, Junfeng |
author_sort | Wang, Yujuan |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9820096 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98200962023-01-07 JMJD8 Functions as a Novel AKT1 Lysine Demethylase Wang, Yujuan Zhang, Yaoyao Li, Zehua Wang, Junfeng Int J Mol Sci Article 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. MDPI 2022-12-27 /pmc/articles/PMC9820096/ /pubmed/36613903 http://dx.doi.org/10.3390/ijms24010460 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Yujuan Zhang, Yaoyao Li, Zehua Wang, Junfeng JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title | JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title_full | JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title_fullStr | JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title_full_unstemmed | JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title_short | JMJD8 Functions as a Novel AKT1 Lysine Demethylase |
title_sort | jmjd8 functions as a novel akt1 lysine demethylase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9820096/ https://www.ncbi.nlm.nih.gov/pubmed/36613903 http://dx.doi.org/10.3390/ijms24010460 |
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