Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA

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R-HSA-450385
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Homo sapiens
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Butyrate Response Factor 1 (BRF1, ZFP36L1, not to be confused with transcription factor IIIB) binds AU-rich elements in the 3' region of mRNAs. After binding, BRF1 recruits exonucleases (XRN1 and the exosome) and decapping enzymes (DCP1a and DCP2) to hydrolyze the RNA. The ability of BRF1 to direct RNA degradation is controlled by phosphorylation of BRF1. Protein kinase B/AKT1 phosphorylates BRF1 at serines 92 and 203. Phosphorylated BRF1 can still bind RNA but is sequestered by binding 14-3-3 protein, preventing BRF1 from destabilizing RNA. BRF1 is also phosphorylated by MK2 at serines 54, 92, 203, and at an unknown site in the C-terminus. It is unknown if this particular phosphorylated form of BRF1 binds 14-3-3.

Literature References
PubMed ID Title Journal Year
16391004 AU-rich elements and associated factors: are there unifying principles?

Barreau, C, Paillard, L, Osborne, HB

Nucleic Acids Res 2005
11719186 AU binding proteins recruit the exosome to degrade ARE-containing mRNAs

Chen, CY, Gherzi, R, Ong, SE, Chan, EL, Raijmakers, R, Pruijn, GJ, Stoecklin, G, Moroni, C, Mann, M, Karin, M

Cell 2001
15687258 Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1

Lykke-Andersen, J, Wagner, E

Genes Dev 2005
12704645 Post-transcriptional regulation of gene expression by degradation of messenger RNAs

Bevilacqua, A, Ceriani, MC, Capaccioli, S, Nicolin, A

J Cell Physiol 2003
12440953 AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors

Zhang, T, Kruys, V, Huez, G, Gueydan, C

Biochem Soc Trans 2002
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