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Article

Arginine Methylation of hnRNPK Inhibits the DDX3-hnRNPK Interaction to Play an Anti-Apoptosis Role in Osteosarcoma Cells

by
Chiao-Che Chen
1,†,
Jen-Hao Yang
1,†,
Shu-Ling Fu
2,
Wey-Jinq Lin
3 and
Chao-Hsiung Lin
1,3,4,*
1
Department of Life Sciences and Institute of Genome Sciences, National Yang Ming Chiao Tung University, Taipei 112, Taiwan
2
Institute of Traditional Medicine, National Yang-Ming Chiao Tung University, Taipei 112, Taiwan
3
Institute of Biopharmaceutical Sciences, National Yang Ming Chiao Tung University, Taipei 112, Taiwan
4
Proteomics Research Center, National Yang Ming Chiao Tung University, Taipei 112, Taiwan
*
Author to whom correspondence should be addressed.
†
These authors contributed equally.
Int. J. Mol. Sci. 2021, 22(18), 9764; https://doi.org/10.3390/ijms22189764
Submission received: 4 August 2021 / Revised: 3 September 2021 / Accepted: 6 September 2021 / Published: 9 September 2021
(This article belongs to the Special Issue Cell Apoptosis)
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Abstract

Heterogeneous nuclear ribonucleoprotein K (hnRNPK) is an RNA/DNA binding protein involved in diverse cell processes; it is also a p53 coregulator that initiates apoptosis under DNA damage conditions. However, the upregulation of hnRNPK is correlated with cancer transformation, progression, and migration, whereas the regulatory role of hnRNPK in cancer malignancy remains unclear. We previously showed that arginine methylation of hnRNPK attenuated the apoptosis of U2OS osteosarcoma cells under DNA damage conditions, whereas the replacement of endogenous hnRNPK with a methylation-defective mutant inversely enhanced apoptosis. The present study further revealed that an RNA helicase, DDX3, whose C-terminus preferentially binds to the unmethylated hnRNPK and could promote such apoptotic enhancement. Moreover, C-terminus-truncated DDX3 induced significantly less apoptosis than full-length DDX3. Notably, we also identified a small molecule that docks at the ATP-binding site of DDX3, promotes the DDX3-hnRNPK interaction, and induces further apoptosis. Overall, we have shown that the arginine methylation of hnRNPK suppresses the apoptosis of U2OS cells via interfering with DDX3–hnRNPK interaction. On the other hand, DDX3–hnRNPK interaction with a proapoptotic role may serve as a target for promoting apoptosis in osteosarcoma cells.
Keywords: apoptosis; hnRNPK; DDX3; DNA damage; protein–protein interaction apoptosis; hnRNPK; DDX3; DNA damage; protein–protein interaction

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MDPI and ACS Style

Chen, C.-C.; Yang, J.-H.; Fu, S.-L.; Lin, W.-J.; Lin, C.-H. Arginine Methylation of hnRNPK Inhibits the DDX3-hnRNPK Interaction to Play an Anti-Apoptosis Role in Osteosarcoma Cells. Int. J. Mol. Sci. 2021, 22, 9764. https://doi.org/10.3390/ijms22189764

AMA Style

Chen C-C, Yang J-H, Fu S-L, Lin W-J, Lin C-H. Arginine Methylation of hnRNPK Inhibits the DDX3-hnRNPK Interaction to Play an Anti-Apoptosis Role in Osteosarcoma Cells. International Journal of Molecular Sciences. 2021; 22(18):9764. https://doi.org/10.3390/ijms22189764

Chicago/Turabian Style

Chen, Chiao-Che, Jen-Hao Yang, Shu-Ling Fu, Wey-Jinq Lin, and Chao-Hsiung Lin. 2021. "Arginine Methylation of hnRNPK Inhibits the DDX3-hnRNPK Interaction to Play an Anti-Apoptosis Role in Osteosarcoma Cells" International Journal of Molecular Sciences 22, no. 18: 9764. https://doi.org/10.3390/ijms22189764

APA Style

Chen, C.-C., Yang, J.-H., Fu, S.-L., Lin, W.-J., & Lin, C.-H. (2021). Arginine Methylation of hnRNPK Inhibits the DDX3-hnRNPK Interaction to Play an Anti-Apoptosis Role in Osteosarcoma Cells. International Journal of Molecular Sciences, 22(18), 9764. https://doi.org/10.3390/ijms22189764

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