TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD
Abstract
Hu proteins are RNA-binding proteins that are implicated in the control of stabilization, nuclear export, and/or translation of specific mRNAs with AU-rich elements (AREs) in the 3'-untranslated region. Three neuron-specific Hu proteins (HuD, HuB, and HuC), but not a ubiquitously expressed Hu protein HuR, have an activity to induce neurite outgrowth when they are overexpressed in a rat neuronal cell line PC12. Here we show that TAP/NXF1, the primary export receptor for the bulk mRNA, is a specific binding partner for HuD. In vitro binding experiments using recombinant proteins revealed that the interaction between TAP and HuD is direct and that HuD can form a ternary complex together with both TAP and RNA. Interestingly, HuR does not interact with TAP. These results suggest that HuD acts as a novel adaptor protein to recruit TAP for efficient export of ARE-containing mRNAs in neuronal cells.
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The first two RRMs of HuD associate with the primary general mRNA export adaptor complex TAP-p15 in an RNA-independent manner, and this interaction may be necessary for shuttling of HuD.
“Moreover, in vitro binding assays showed that the first two RRMs of HuD associate with the primary general mRNA export adaptor complex (TAP-p15; also known as NXF1/NXT1) in a RNA-independent manner and that this interaction may be necessary for shuttling of HuD (Saito et al. 2004).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Saito et al. 2004
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- Authors
- Saito, K., Fujiwara, T., Katahira, J., Inoue, K., & Sakamoto, H.
- Affiliations
- Kobe University (JP)
- The University of Osaka (JP)
- Corresponding author
- Sakamoto, Hiroshi
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2004-08
- Volume
- 321
- Issue
- 2
- Pages
- 291-297
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1992240096
- Cited by
- 31
- References
- 0
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2022: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 3 · 2014: 1 · 2013: 2 · 2012: 2
- FWCI
- 0.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- HUD, HU protein, mRNA export, AU-rich elements, RNA-binding proteins, HuR, ternary complex, adaptor proteins, neurite outgrowth, neurons, PC12 cells, mRNA stabilization
- MeSH terms
- ELAV-Like Protein 4, Animals, Binding Sites, HeLa Cells, Humans, Nerve Tissue Proteins, Neurons, Protein Binding, RNA, Messenger, Neurites, RNA-Binding Proteins, PC12 Cells, Sequence Deletion, Protein Structure, Tertiary, Nucleocytoplasmic Transport Proteins, RNA Transport, Rats, ELAV Proteins
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