HuR and mRNA stability
Open accessAbstract
An important mechanism of posttranscriptional gene regulation in mammalian cells is the rapid degradation of messenger RNAs (mRNAs) signaled by AU-rich elements (AREs) in their 3' untranslated regions. HuR, a ubiquitously expressed member of the Hu family of RNA-binding proteins related to Drosophila ELAV, selectively binds AREs and stabilizes ARE-containing mRNAs when overexpressed in cultured cells. This review discusses mRNA decay as a general form of gene regulation, decay signaled by AREs, and the role of HuR and its Hu-family relatives in antagonizing this mRNA degradation pathway. The influence of newly identified protein ligands to HuR on HuR function in both normal and stressed cells may explain how ARE-mediated mRNA decay is regulated in response to environmental change.
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There are a few known AUBPs that enhance mRNA stability, with Hu proteins being the most notable.
“Nevertheless, there are a few known AUBPs that enhance mRNA stability, with Hu proteins being the most notable (Brennan and Steitz 2001; Hinman and Lou 2008; Pascale et al. 2008).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Brennan and Steitz 2001
The ELAVL family consists of four highly homologous members.
“The ELAVL (also known as Hu) family of proteins consists of four highly homologous members109–111”
From The neurogenetics of alternative splicing (2016) · cites this paper as [110]
ELAVLs regulate mRNA stability and translation efficiency through binding to 3′ UTRs.
“The ELAVLs have primarily been studied as regulators of mRNA stability and translation efficiency through their binding to 3′ UTRs110,111,123”
From The neurogenetics of alternative splicing (2016) · cites this paper as [110]
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- Authors
- Brennan, C. M., & Steitz*, J. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- ORCID
- Brennan, C. M.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2001-02
- Volume
- 58
- Issue
- 2
- Pages
- 266-277
- ISSN
- 1420-682X (ISSN-L)
- PMC
- PMC11146503
- OpenAlex
- W2005558505
- Cited by
- 1,095
- References
- 119
- Citations by year
- 2026: 25 · 2025: 49 · 2024: 31 · 2023: 26 · 2022: 40 · 2021: 28 · 2020: 38 · 2019: 32 · 2018: 48 · 2017: 33 · 2016: 34 · 2015: 43 · 2014: 54 · 2013: 55 · 2012: 55
- FWCI
- 15.94
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA-16038, P01CA016038)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- HuR, AU-rich elements, mRNA stability, mRNA degradation, post-transcriptional regulation, RNA-binding proteins, 3' untranslated region, ELAV, protein ligands, cellular stress response
- MeSH terms
- ELAV-Like Protein 1, Amino Acid Sequence, Animals, Antigens, Surface, Base Sequence, Biological Transport, Active, Carrier Proteins, Cell Differentiation, Cytoplasm, Humans, Models, Biological, Molecular Sequence Data, RNA, Messenger, RNA-Binding Proteins, Sequence Homology, Amino Acid, RNA Stability, ELAV Proteins
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