Arginine methylation of hnRNP K enhances p53 transcriptional activity

• Published in: FEBS letters Vol. 582; no. 12; pp. 1761 - 1765
• Main Authors: Chen, Yibin, Zhou, Xinyuan, Liu, Na, Wang, Chaochen, Zhang, Liang, Mo, Wei, Hu, Gengxi
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 28.05.2008
• Subjects: Arginine - metabolism; Arginine methylation; C-terminus domain; Cell Line; CTD; Cyclin-Dependent Kinase Inhibitor p21 - genetics; DBD; DNA-binding domain; Heterogeneous-Nuclear Ribonucleoprotein K - metabolism; Heterogeneous-Nuclear Ribonucleoprotein K - radiation effects; hnRNP K; Humans; Methylation; p53; Protein Processing, Post-Translational; RNA interference; RNA, Messenger - metabolism; RNAi; TAD; transactivation domain; Transcription, Genetic; Transcriptional regulation; Tumor Suppressor Protein p53 - metabolism; Ultraviolet Rays; UV radiation; UV radiation; CTD; RNAi; TAD; DBD; hnRNP K; Transcriptional regulation; Arginine methylation; p53
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2008.04.051

Previous studies have illustrated that hnRNP K, which could be methylated at arginine residues, plays a key role in coordinating transcriptional responses to DNA damage as a cofactor for p53. In this study, we observed that hnRNP K was markedly arginine methylated in response to UV radiation. Furthermore, arginine methylation of hnRNP K enhanced its affinity with p53. Inhibition of methylation in hnRNP K attenuated the recruitment of p53 to p21 promoter, and reduced p53 transcriptional activity. These data suggested that arginine methylation of hnRNP K is a key element for p53 transcriptional activity.