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Ribosomal protein S2 interplays with MDM2 to induce p53

Title
Ribosomal protein S2 interplays with MDM2 to induce p53
Authors
Cho J.Park J.Shin S.C.Kim J.-H.Kim E.E.Song E.J.
Ewha Authors
송은주
Issue Date
2020
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
Biochemical and Biophysical Research Communications
Keywords
MDM2p53Ribosomal protein S2Ubiquitination
Publisher
Elsevier B.V.
Indexed
SCI; SCIE; SCOPUS scopus
Document Type
Article
Abstract
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. © 2020 Elsevier Inc.
DOI
10.1016/j.bbrc.2020.01.038
Appears in Collections:
약학대학 > 약학과 > Journal papers
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