The Elav-like Proteins Bind to a Conserved Regulatory Element in the 3′-Untranslated Region of GAP-43 mRNA
Open accessAbstract
Previous studies have identified three brain proteins (40, 65 and 95 kDa, respectively) that specifically bind to the 3'-untranslated region of GAP-43 mRNA. In this study, using a specific monoclonal antibody, we now show that the 40-kDa proteins are members of the Elav-like protein family. This family of specific RNA-binding proteins comprise three neural specific members called HuD, HuC, and Hel-N1. We have shown that purified recombinant HuD can bind with high affinity to GAP-43 mRNA. In addition, we have mapped the binding site to a highly conserved 26-nucleotide sequence within the regulatory element. The binding of HuD to this site is readily displaced by RNA oligonucleotides encoding other HuD binding sites. We also show that only the first and second RNA binding domains of HuD are required for selective binding to GAP-43 mRNA.
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GAP-43 mRNA houses a class III ARE in its 3′ UTR.
“Among all of the HuD-regulated mRNAs, the most prominent is the GAP-43 mRNA, which houses a class III ARE in its 3′ UTR (Chung et al. 1997; Tsai et al. 1997).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Chung et al. 1997
The paper describes a conserved U-rich element in the GAP-43 mRNA 3′ UTR and maps a 26-nucleotide HuD-binding site there (Abstract; HuD binding-site section, page unavailable). Our copy does not identify that element as a class III ARE, so the specific classification is not established by this source. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThis function of HuD requires its shuttling to the cytoplasm and involves stabilization of various target mRNAs whose protein products promote microtubule assembly and growth cone development including GAP-43, Tau, and AChE.
“This function of HuD requires its shuttling to the cytoplasm and involves stabilization of various target mRNAs whose protein products promote microtubule assembly and growth cone development including GAP-43, Tau, and AChE (Chung et al. 1997; Aranda-Abreu et al. 1999; Kasashima et al. 1999; Deschenes-Furry et al. 2003).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Chung et al. 1997
The GAP-43 binding-site results show that HuD binds a conserved element in GAP-43 mRNA. The Discussion proposes a possible role for Elav-like proteins in GAP-43 regulation, but treats their involvement in mRNA stabilization as a hypothesis requiring further investigation. This paper does not establish that HuD must shuttle to the cytoplasm or that it stabilizes the listed target mRNAs. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
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- Authors
- Chung, S., Eckrich, M., Perrone-Bizzozero, N., Kohn, D. T., & Furneaux, H.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- University of New Mexico (US)
- Corresponding author
- Furneaux, Henry
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-03
- Volume
- 272
- Issue
- 10
- Pages
- 6593-6598
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2082551528
- Cited by
- 142
- References
- 2
- Citations by year
- 2025: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 10 · 2012: 5
- FWCI
- 4.87
- 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 (5r01ns029682-04, CA08748)
- National Cancer Institute (P30-CA-08748, CA08748, P30CA008748)
- National Institute of Neurological Disorders and Stroke (NS 30255, NS29682)
- 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
- ELAV-like proteins, HUD, 3' untranslated region, RNA-binding proteins, RNA-binding domain, brain-specific proteins, monoclonal antibodies
- MeSH terms
- ELAV-Like Protein 2, Animals, Base Sequence, Binding, Competitive, Gene Expression Regulation, Membrane Glycoproteins, Molecular Sequence Data, Nerve Tissue Proteins, Recombinant Proteins, Regulatory Sequences, Nucleic Acid, RNA, Messenger, RNA-Binding Proteins, GAP-43 Protein, Rats, ELAV Proteins
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