Sumoylation of the histone demethylase KDM4A is required for binding to tumor suppressor p53 in HCT116 colon cancer cell lines

Seung Eun Yu, Su Hyung Park, Yeun Kyu Jang

Research output: Contribution to journalArticle

Abstract

The histone demethylase lysine-specific demethylase 4A (KDM4A/Jmjd2A) has diverse functions, including involvement in gene regulation and cell cycle, and plays an oncogenic role in cancer cells. The modulation of KDM4A through post-translational modifications remains unclear. Here, we show that small ubiquitin-like modifier (SUMO) 1-mediated modification of KDM4A was required for interaction with tumor suppressor p53. Our data revealed that KDM4A is mainly sumoylated at lysine residue 471. However, the SUMO modification resulted in little change in subcellular localization, demethylase activity, or protein stability of KMD4A. Intriguingly, co-immunoprecipitation data revealed that sumoylation-defective mutants of KDM4A had a lower binding ability with p53 compared to that of wild-type KDM4A, suggesting a positive role for sumoylation in the interaction between KDM4A and p53. Together, these data suggest that KDM4A is post-translationally modified by SUMO, and this sumoylation may be a novel regulatory switch for controlling the interplay between KDM4A and p53.

Original languageEnglish
Pages (from-to)22-28
Number of pages7
JournalAnimal Cells and Systems
Volume22
Issue number1
DOIs
Publication statusPublished - 2018 Jan 2

Fingerprint

Histone Demethylases
Sumoylation
modifiers (genes)
ubiquitin
Ubiquitin
colorectal neoplasms
histones
Colonic Neoplasms
Tumors
Cells
cell lines
Cell Line
neoplasms
lysine
cdc Genes
Neoplasms
Protein Stability
post-translational modification
binding capacity
Post Translational Protein Processing

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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abstract = "The histone demethylase lysine-specific demethylase 4A (KDM4A/Jmjd2A) has diverse functions, including involvement in gene regulation and cell cycle, and plays an oncogenic role in cancer cells. The modulation of KDM4A through post-translational modifications remains unclear. Here, we show that small ubiquitin-like modifier (SUMO) 1-mediated modification of KDM4A was required for interaction with tumor suppressor p53. Our data revealed that KDM4A is mainly sumoylated at lysine residue 471. However, the SUMO modification resulted in little change in subcellular localization, demethylase activity, or protein stability of KMD4A. Intriguingly, co-immunoprecipitation data revealed that sumoylation-defective mutants of KDM4A had a lower binding ability with p53 compared to that of wild-type KDM4A, suggesting a positive role for sumoylation in the interaction between KDM4A and p53. Together, these data suggest that KDM4A is post-translationally modified by SUMO, and this sumoylation may be a novel regulatory switch for controlling the interplay between KDM4A and p53.",
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Sumoylation of the histone demethylase KDM4A is required for binding to tumor suppressor p53 in HCT116 colon cancer cell lines. / Yu, Seung Eun; Park, Su Hyung; Jang, Yeun Kyu.

In: Animal Cells and Systems, Vol. 22, No. 1, 02.01.2018, p. 22-28.

Research output: Contribution to journalArticle

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