Arginine methylation of hnRNP K enhances p53 transcriptional activity.
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.
Chen
Yibin
Y
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Zhou
Xinyuan
X
Liu
Na
N
Wang
Chaochen
C
Zhang
Liang
L
Mo
Wei
W
Hu
Gengxi
G
D001120:Arginine / Q000378:metabolism*; D002460:Cell Line; D050759:Cyclin-Dependent Kinase Inhibitor p21 / Q000235:genetics; D034641:Heterogeneous-Nuclear Ribonucleoprotein K / Q000378:metabolism* / Q000528:radiation effects; D006801:Humans; D008745:Methylation; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000378:metabolism; D014158:Transcription, Genetic; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*; D014466:Ultraviolet Rays
C493956:CDKN1A protein, human; D050759:Cyclin-Dependent Kinase Inhibitor p21; D034641:Heterogeneous-Nuclear Ribonucleoprotein K; D012333:RNA, Messenger; D016159:Tumor Suppressor Protein p53; D001120:Arginine