Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
AbstractIn response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs, and affect gene expression during cellular activation, proliferation, and stress responses. In this review, we summarize the effect of phosphorylation on the function of ARE-binding proteins ZFP36 and ELAVL1 and the GRE-binding protein CELF1. The networks of target mRNAs that these proteins bind and regulate include transcripts encoding kinases and kinase signaling pathways (KSP) components. Thus, kinase signaling pathways are involved in feedback regulation, whereby kinases regulate RNA-binding proteins that subsequently regulate mRNA stability of ARE- or GRE-containing transcripts that encode components of KSP. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Vlasova-St. Louis, I.; Bohjanen, P.R. Feedback Regulation of Kinase Signaling Pathways by AREs and GREs. Cells 2016, 5, 4.
Vlasova-St. Louis I, Bohjanen PR. Feedback Regulation of Kinase Signaling Pathways by AREs and GREs. Cells. 2016; 5(1):4.Chicago/Turabian Style
Vlasova-St. Louis, Irina; Bohjanen, Paul R. 2016. "Feedback Regulation of Kinase Signaling Pathways by AREs and GREs." Cells 5, no. 1: 4.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.