Cho, Jinhong Park, Jinyoung Shin, Sang Chul Kim, Jae-Hong Kim, Eunice EunKyeong Song, Eun Joo 2024-01-19T18:01:49Z 2024-01-19T18:01:49Z 2021-09-04 2020-03-05 0006-291X https://pubs.kist.re.kr/handle/201004/118862 The MDM2-p53 pathway is crucial for maintenance of p53 homeostasis. Some ribosomal proteins (RPs) play critical roles in regulating p53 by interacting with MDM2. However, the role and functional mechanism of each RP in MDM2-p53 pathway still remain unknown. In this study, we found that Ribosomal Protein S2 (RPS2) is a new regulator of MDM2-P53 signaling pathway to regulate p53 protein level. Here, we characterized that RPS2 interacts with MDM2 through the RING finger domain of MDM2. RPS2 is ubiquitinated by MDM2 and the ubiquitinated status of RPS2 regulates the stability of p53, which is activated in response to cellular stresses such as DNA damage, oxidative stress, and especially ribosomal stress. In addition, p53 is not induced in RPS2 knockdown even in the ribosomal stressed condition, indicating that RPS2 is essential for the stabilization of p53. Collectively, our data suggest that RPS2 plays a critical role in the regulation of p53 signaling including the ribosomal stress response. (C) 2020 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE UBIQUITINATION ACTIVATION PATHWAY L11 Ribosomal protein S2 interplays with MDM2 to induce p53 Article 10.1016/j.bbrc.2020.01.038 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.523, no.2, pp.542 - 547 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 523 2 542 547 scie scopus 000524737600040 2-s2.0-85077714996 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article UBIQUITINATION ACTIVATION PATHWAY L11 Ribosomal protein S2 MDM2 p53 Ubiquitination