Identification of a target RNA motif for RNA-binding protein HuR
Open accessAbstract
HuR, a protein that binds to specific mRNA subsets, is increasingly recognized as a pivotal posttranscriptional regulator of gene expression. Here, HuR was immunoprecipitated under conditions that preserved HuR-RNA interactions, and HuR-bound target mRNAs were identified by cDNA array hybridization. Analysis of primary sequences and secondary structures shared among HuR targets led to the identification of a 17- to 20-base-long RNA motif rich in uracils. This HuR motif was found in almost all mRNAs previously reported to be HuR targets, was located preferentially within 3′ untranslated regions of all unigene transcripts examined, and was conserved in >50% of human and mouse homologous genes. Importantly, the HuR motif allowed the successful prediction and subsequent validation of novel HuR targets from gene databases. This study describes an HuR target RNA motif and presents a general strategy for identifying target motifs for RNA-binding proteins.
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ELAVL proteins recognize U- and AU-rich elements.
“that recognize U- and AU-rich elements112–118”
From The neurogenetics of alternative splicing (2016) · cites this paper as [117]
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HuR Uses AUF1 as a Cofactor To Promote p16<sup>INK4</sup> mRNA Decay
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Self-citationMolecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM
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Systematic analysis of posttranscriptional gene expression
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Polyamines Regulate c-Myc Translation through Chk2-dependent HuR Phosphorylation
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HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs
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Prognostic Role of HuR in Hereditary Breast Cancer
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- Authors
- de Silanes, I. L., Zhan, M., Lal, A., Yang, X., & Gorospe, M.
- Affiliations
- Laboratory of Cellular and Molecular Biology and Research Resources Branch, National Institute on Aging-Intramural Research Program, National Institutes of Health, Baltimore, MD 21224
- Houston Methodist (US)
- National Institutes of Health (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-02-23
- Volume
- 101
- Issue
- 9
- Pages
- 2987-2992
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC365732
- OpenAlex
- W2135070076
- Cited by
- 502
- References
- 48
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 11 · 2023: 21 · 2022: 21 · 2021: 16 · 2020: 16 · 2019: 16 · 2018: 21 · 2017: 19 · 2016: 21 · 2015: 30 · 2014: 30 · 2013: 23 · 2012: 39
- FWCI
- 7.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- HuR, RNA-binding proteins, post-transcriptional regulation, mRNA targets, 3' untranslated region, target prediction, sequence conservation
- MeSH terms
- ELAV-Like Protein 1, Animals, Antigens, Surface, Base Sequence, Binding Sites, Carcinoma, Humans, Nucleic Acid Conformation, RNA, Messenger, Colorectal Neoplasms, RNA-Binding Proteins, 5' Untranslated Regions, Oligonucleotide Array Sequence Analysis, 3' Untranslated Regions, Cell Line, Tumor, Mice, ELAV Proteins
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