A Mechanism for Translationally Coupled mRNA Turnover
Open accessAbstract
mRNA turnover mediated by the major protein-coding-region determinant of instability (mCRD) of the c-fos proto-oncogene transcript illustrates a functional interplay between mRNA turnover and translation. We show that the function of mCRD depends on its distance from the poly(A) tail. Five mCRD-associated proteins were identified: Unr, a purine-rich RNA binding protein; PABP, a poly(A) binding protein; PAIP-1, a poly(A) binding protein interacting protein; hnRNP D, an AU-rich element binding protein; and NSAP1, an hnRNP R-like protein. These proteins form a multiprotein complex. Overexpression of these proteins stabilized mCRD-containing mRNA by impeding deadenylation. We propose that a bridging complex forms between the poly(A) tail and the mCRD and ribosome transit disrupts or reorganizes the complex, leading to rapid RNA deadenylation and decay.
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The poly(A) tail regulates the fate of mRNA by synergy with the 5' cap, the internal ribosomal entry site, and various RNA stability determinants.
“The poly(A) tail regulates the fate of mRNA by synergy with the 5Ј cap, with the internal ribosomal entry site, and with various RNA stability determinants.31,[38][39][40][41]”
From Modification of antigen-encoding RNA increases stability, translational efficacy, and T-cell stimulatory capacity of dendritic cells (2006) · cites this paper as [38]
The passages labeled Abstract (page unavailable) describe an interaction between the poly(A) tail and 5′ cap that influences translation, and experiments linking the tail to an mRNA decay determinant, the mCRD. They also mention cap-independent initiation, but do not establish that the poly(A) tail acts synergistically with an internal ribosomal entry site. (LLM, conf=0.84)
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Cites
AU-rich elements: characterization and importance in mRNA degradation
Chen, C.-Y. A., & Shyu, A.-B. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89102-1 · Cited by 1,948 · see citing works
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- [1]1. Caruccio, N ∙ Ross, J Purification of a human polyribosome-associated 3′ to 5′ exoribonuclease J. Biol. Chem. 1994; 269:31814-31821
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Regulation of mRNA Translation and Stability by microRNAs
Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214 · see citing works
Self-citationCodon optimality, bias and usage in translation and mRNA decay
Hanson, G., & Coller, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.91 · Cited by 825 · see citing works
Holtkamp, S., Kreiter, S., Selmi, A., Simon, P., Koslowski, M., Huber, C., Türeci, O., & Sahin, U. (2006) · Blood · doi:10.1182/blood-2006-04-015024 · Cited by 625 · see citing works
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Chapter 17 Messenger RNA Half‐Life Measurements in Mammalian Cells
Chen, C. A., Ezzeddine, N., & Shyu, A. (2008) · Methods in Enzymology · doi:10.1016/s0076-6879(08)02617-7 · Cited by 256 · see citing works
Self-citationHighly Selective Actions of HuR in Antagonizing AU-Rich Element-Mediated mRNA Destabilization
Chen, C.-Y. A., Xu, N., & Shyu, A.-B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7268-7278.2002 · Cited by 176 · see citing works
Self-citationHeterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages
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- Authors
- Grosset, C., Chen, C.-Y. A., Xu, N., Sonenberg, N., Jacquemin-Sablon, H., & Shyu, A.-B.
- Affiliations
- McGill University (CA)
- Corresponding author
- Shyu, Ann-Bin
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 103
- Issue
- 1
- Pages
- 29-40
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1986461283
- Cited by
- 295
- References
- 1
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 11 · 2023: 6 · 2022: 8 · 2021: 11 · 2020: 8 · 2019: 5 · 2018: 8 · 2017: 9 · 2016: 8 · 2015: 9 · 2014: 3 · 2013: 7 · 2012: 9
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- National Institutes of Health (GM 46454, GM 59211)
- 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
- mRNA turnover, c-fos, poly(A) tail, mRNA degradation, translation (biology), poly(A)-binding protein, HNRNPD, Ukrainian People's Republic, AU-rich elements, protein complexes, mRNA stability
- MeSH terms
- Proto-Oncogene Mas, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cells, Cultured, Chromosome Mapping, Cytoplasm, DNA-Binding Proteins, Gene Expression Regulation, Molecular Sequence Data, Peptide Initiation Factors, Peptides, Poly A, Ribonucleoproteins, RNA, Messenger, Protein Biosynthesis, RNA-Binding Proteins, Proto-Oncogene Proteins c-fos, Heterogeneous-Nuclear Ribonucleoproteins, Mice
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