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 language | English |
|---|---|
| Pages (from-to) | 22-28 |
| Number of pages | 7 |
| Journal | Animal Cells and Systems |
| Volume | 22 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2018 Jan 2 |
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All Science Journal Classification (ASJC) codes
- Animal Science and Zoology
- Biochemistry, Genetics and Molecular Biology(all)
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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 journal › Article
TY - JOUR
T1 - Sumoylation of the histone demethylase KDM4A is required for binding to tumor suppressor p53 in HCT116 colon cancer cell lines
AU - Yu, Seung Eun
AU - Park, Su Hyung
AU - Jang, Yeun Kyu
PY - 2018/1/2
Y1 - 2018/1/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85041002945&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85041002945&partnerID=8YFLogxK
U2 - 10.1080/19768354.2018.1426628
DO - 10.1080/19768354.2018.1426628
M3 - Article
AN - SCOPUS:85041002945
VL - 22
SP - 22
EP - 28
JO - Animal Cells and Systems
JF - Animal Cells and Systems
SN - 1976-8354
IS - 1
ER -