Journal
MOLECULAR CELL
Volume 10, Issue 6, Pages 1331-1344Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(02)00730-X
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Funding
- NCRR NIH HHS [RR11823-04] Funding Source: Medline
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In response to T cell activation signals, the half-life of interleukin-2 (IL-2) mRNA is greatly extended. The cis elements mediating IL-2 mRNA stabilization are located in its 5' and 3' untranslated regions (UTR). The 3'UTR also contains AU-rich elements (AREs) that mediate rapid IL-2 mRNA degradation in the cytoplasm of nonstimulated T cells. NF90, a previously described RNA binding protein, binds to a subregion of the 3'UTR that contains several AREs and slows down the degradation of IL-2 mRNA. In nonstimulated cells, NF90 is mostly nuclear, but T cell activation results in its accumulation in the cytoplasm. The nuclear export of NF90 is required for IL-2 mRNA stabilization.
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