Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Dec 24;13:13225–13236. doi: 10.2147/OTT.S278755

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2020 She et al.

This work is published and licensed by Dove Medical Press Limited. The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php).

PMC Copyright notice

The regulatory mechanism of RBM38. (A) Through its RRM domain, RBM38 specifically binds to the AREs in the 3′UTR of the target mRNAs, forms complexes with mRNAs, and then positively or negatively regulate the stability of the target mRNAs to affect the expression of the target genes. For example, RBM38 upregulates the expression of p73, p21 and MIC-1 by maintaining the stability of their mRNAs. (B) RBM38 downregulates the expression of mdm2, p63 and c-Myc by reducing the stability of their mRNAs. (C) Translation initiation of p53 mRNA requires the combination of eIF4E and the promoter start codon (AUG), while RBM38 competitively interacts with eIF4E and prevents it from binding to the AUG on p53 mRNAs, thus blocking the translation of p53.