AI Article Synopsis
- Butyrate response factor 1 (BRF1) is a CCCH zinc-finger protein that binds to AU-rich elements (ARE) in mRNAs, facilitating their degradation.
- Protein kinase B (PKB/Akt) stabilizes these ARE-containing transcripts by phosphorylating BRF1 at a specific site (serine 92), which reduces its ability to promote mRNA decay.
- The phosphorylation of BRF1 leads to its interaction with the scaffold protein 14-3-3, which ultimately aids in stabilizing ARE-mRNA by preventing the action of BRF1.
Article Abstract
Butyrate response factor (BRF1) belongs to the Tis11 family of CCCH zinc-finger proteins, which bind to mRNAs containing an AU-rich element (ARE) in their 3' untranslated region and promote their deadenylation and rapid degradation. Independent signal transduction pathways have been reported to stabilize ARE-containing transcripts by a process thought to involve phosphorylation of ARE-binding proteins. Here we report that protein kinase B (PKB/Akt) stabilizes ARE transcripts by phosphorylating BRF1 at serine 92 (S92). Recombinant BRF1 promoted in vitro decay of ARE-containing mRNA (ARE-mRNA), yet phosphorylation by PKB impaired this activity. S92 phosphorylation of BRF1 did not impair ARE binding, but induced complex formation with the scaffold protein 14-3-3. In vivo and in vitro data support a model where PKB causes ARE-mRNA stabilization by inactivating BRF1 through binding to 14-3-3.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC535089 | PMC |
| http://dx.doi.org/10.1038/sj.emboj.7600477 | DOI Listing |
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