Journal
MOLECULAR CELL
Volume 43, Issue 3, Pages 327-339Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2011.06.007
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Funding
- National Science Foundation [0842621, 0822033]
- National Institutes of Health [DA030086]
- Howard Hughes Medical Institute
- Starr Foundation
- Charles H. Revson, Sr., Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0822033] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0842621] Funding Source: National Science Foundation
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RNA-binding proteins coordinate the fates of multiple RNAs, but the principles underlying these global interactions remain poorly understood. We elucidated regulatory mechanisms of the RNA-binding protein HuR, by integrating data from diverse high-throughput targeting technologies, specifically PAR-CLIP, RIP-chip, and whole-transcript expression profiling. The number of binding sites per transcript, degree of HuR association, and degree of HuR-dependent RNA stabilization were positively correlated. Pre-mRNA and mature mRNA containing both intronic and 3' UTR binding sites were more highly stabilized than transcripts with only 3' UTR or only intronic binding sites, suggesting that HuR couples pre-mRNA processing with mature mRNA stability. We also observed HuR-dependent splicing changes and substantial binding of HuR in polypyrimidine tracts of pre-mRNAs. Comparison of the spatial patterns surrounding HuR and miRNA binding sites provided functional evidence for HuR-dependent antagonism of proximal miRNA-mediated repression. We conclude that HuR coordinates gene expression outcomes at multiple interconnected steps of RNA processing.
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