Poly(A) Tail Length-dependent Stabilization of GAP-43 mRNA by the RNA-binding Protein HuD
Open accessAbstract
The neuronal ELAV-like RNA-binding protein HuD binds to a regulatory element in the 3'-untranslated region of the growth-associated protein-43 (GAP-43) mRNA. Here we report that overexpression of HuD protein in PC12 cells stabilizes the GAP-43 mRNA by delaying the onset of mRNA degradation and that this process depends on the size of the poly(A) tail. Using a polysome-based in vitro mRNA decay assay, we found that addition of recombinant HuD protein to the system increased the half-life of full-length, capped, and polyadenylated GAP-43 mRNA and that this effect was caused in part by a decrease in the rate of deadenylation of the mRNA. This stabilization was specific for GAP-43 mRNA containing the HuD binding element in the 3'-untranslated region and a poly(A) tail of at least 150 A nucleotides. In correlation with the effect of HuD on GAP-43 mRNA stability, we found that HuD binds GAP-43 mRNAs with long tails (A150) with 10-fold higher affinity than to those with short tails (A30). We conclude that HuD stabilizes the GAP-43 mRNA through a mechanism that is dependent on the length of the poly(A) tail and involves changes in its affinity for the mRNA.
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Binding of Hu protein to the poly(A) tail depends on tail length; the longer the poly(A) tail, the higher the affinity of Hu protein binding to its target mRNA.
“Binding to the poly(A) tail seems to depend on the tail length, since results from in vitro binding assays demonstrated that the longer the poly(A) tail, the higher the affinity of Hu protein binding to its target mRNA (Beckel-Mitchener et al. 2002).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Beckel-Mitchener et al. 2002
The section “HuD Binds with Higher Affinity to GAP-43 Molecules with Long Poly(A) Tails” reports an eightfold higher affinity for GAP-43 mRNA with an A150 tail than with an A30 tail in an in vitro binding assay. The Discussion clarifies that the assay measured HuD binding to a site in the 3′-UTR as a function of tail length, not direct binding to the poly(A) tail; direct tail binding is presented as consistent with the data, not demonstrated by that assay. Page numbers were not supplied in the passages. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHuD is more effective at stabilizing GAP-43 mRNAs that contain a longer poly(A) tail, indicating that HuD binds to both the ARE and poly(A) tail to increase GAP-43 mRNA half-life.
“Interestingly, HuD is more effective at stabilizing GAP-43 mRNAs that contain a longer poly(A) tail, indicating that HuD binds to both the ARE and poly(A) tail to increase GAP-43 mRNA half-life (Beckel-Mitchener et al. 2002).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Beckel-Mitchener et al. 2002
The Results report that HuD preferentially stabilizes GAP-43 mRNA with long poly(A) tails and increases its half-life. The Discussion says HuD binding to the ARE was measured, but binding to the poly(A) tail was only a possible explanation consistent with the data—not a demonstrated mechanism. Page numbers are not provided in our copy. (LLM, conf=0.88)
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References 52 · Cited by 113
Research works printed but not linked: 1
- Namgung, U., Matsuyama, S., and Routtenburg, A. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 11675-11680
- Authors
- Beckel-Mitchener, A. C., Miera, A., Keller, R., & Perrone-Bizzozero, N. I.
- Affiliations
- University of New Mexico (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 277
- Issue
- 31
- Pages
- 27996-28002
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2052632013
- Cited by
- 113
- References
- 52
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 12 · 2023: 4 · 2022: 6 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 6 · 2014: 3 · 2013: 7 · 2012: 3
- FWCI
- 1.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5s06gm052576-04)
- School of Medicine, University of New Mexico
- National Institute of General Medical Sciences (GM 52576)
- National Institute of Neurological Disorders and Stroke (NS 30255)
- 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
- HUD, GAP-43, mRNA stability, poly(A) tail length, deadenylation, 3' untranslated region, mRNA degradation, PC12 cells
- MeSH terms
- Animals, Gene Expression Regulation, Kinetics, Nerve Tissue Proteins, Poly A, RNA, Messenger, RNA-Binding Proteins, PC12 Cells, GAP-43 Protein, Rats, ELAV Proteins
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