The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.
Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein
Abstract
PTB (polypyrimidine-tract-binding protein) is a ubiquitous RNA-binding protein. It was originally identified as a protein with a role in splicing but it is now known to function in a large number of diverse cellular processes including polyadenylation, mRNA stability and translation initiation. Specificity of PTB function is achieved by a combination of changes in the cellular localization of this protein (its ability to shuttle from the nucleus to the cytoplasm is tightly controlled) and its interaction with additional proteins. These differences in location and trans-acting factor requirements account for the fact that PTB acts both as a suppressor of splicing and an activator of translation. In the latter case, the role of PTB in translation has been studied extensively and it appears that this protein is required for an alternative form of translation initiation that is mediated by a large RNA structural element termed an IRES (internal ribosome entry site) that allows the synthesis of picornaviral proteins and cellular proteins that function to control cell growth and cell death. In the present review, we discuss how PTB regulates these disparate processes.
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“dual roles for RBPs in the control of splicing and stability are emerging28–30.”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [28]
Citations
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Flagged first, then by citations
Research works printed but not linked: 4
- Lou, 1999, Polypyrimidine tract-binding protein positively regulates inclusion of an alternative 3′-terminal exon, Mol. Cell. Biol., 19, 78, 10.1128/MCB.19.1.78 · DOI
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Murugan, A., Nanjegowda, N. B., & Jothi, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.21.578728
Deciphering the Role of ARK5 and hnRNP A1 in Regulating the Osmotic Stress.
Bhattarai, K. R. (2024) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2024-16079
Pol II degradation activates cell death independently from the loss of transcriptionPreprint
Harper, N. W., Birdsall, G. A., Honeywell, M. E., Pai, A. A., & Lee, M. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.09.627542
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“In uninfected cells, PTB plays a crucial role in alternative pre-mRNA splicing [ 38 ].”
López‐Ulloa, B., Mendonça, D., Guzmán‐Correa, D., Martínez‐Torres, J., Guzmán, D., Blanlot, C., Patricio Astudillo, P., Rojas-Araya, B., & López‐Lastra, M. (2025) · FEBS Journal · doi:10.1111/febs.70361
“Knockdown of endogenous PTB or the overexpression of His-PTB does not impact HTLV-1 IRES or sHBZ IRES activity PTB, a well-known ITAF for several viral IRESs [25,29], binds to the 5 0 UTR of the HTLV-1 mRNA [30], the region that harbors the HTLV-1 IRES [14,15].”
Regulation Of Fatty Acid Desaturase Expression And Alternative Splicing
Reardon, H. T. (2012) · eCommons (Cornell University)
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Baril, T., & Hayward, A. (2022) · Figshare · doi:10.6084/m9.figshare.19185946
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Baril, T., & Hayward, A. (2022) · Figshare · doi:10.6084/m9.figshare.19185943
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Baril, T., & Hayward, A. (2022) · Figshare · doi:10.6084/m9.figshare.19185940
Baril, T., & Hayward, A. (2022) · Figshare · doi:10.6084/m9.figshare.19185952
Réseau de contrôle de la traduction par l'Hormone Folliculo-Stimulante
Huamán, K. B. L. (2013) · theses.fr (ABES) · doi:10.70675/d4a25518z7516z44aez84b3zf8a0eb211064
Rôle de la protéine HBc du virus de l'hépatite B sur la biologie des ARN viraux
Quioc-Salomon, B. (2019) · theses.fr (ABES) · doi:10.70675/b6ed09afzdf34z40e4z9737z206181f96139
Age-dependent remodelling of RNP condensates in Drosophila neurons
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“It binds to the polypyrimidine tract of mRNA (Sawicka et al. 2008; Zhang et al. 2017), controlling its target mRNA maturation, stability, location, and translation (Sawicka et al. 2008).”
The heat shock protein 70 (Hsp70) family of chaperones is essential for rhinovirus replicationPreprint
James, M. T., Dane, C., Moore, A. O., & Mousnier, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.13.742791
Kajal, Pandey, A., Yadav, R., Shukla, R., & Mishra, S. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12713-x
The RNA Recognition Motif and Messenger RNA
Hall, K. B. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4954-6_6
Metadata
- Authors
- Sawicka, K., Bushell, M., Spriggs, K. A., & Willis, A. E.
- Affiliations
- University of Nottingham (GB)
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2008-07-22
- Volume
- 36
- Issue
- 4
- Pages
- 641-647
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W1995239307
- Cited by
- 332
- References
- 85
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 21 · 2023: 18 · 2022: 29 · 2021: 11 · 2020: 15 · 2019: 20 · 2018: 17 · 2017: 10 · 2016: 14 · 2015: 16 · 2014: 24 · 2013: 19 · 2012: 31
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council
- 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
- polypyrimidine tract-binding protein, PTB, RNA-binding proteins, splicing regulation, polyadenylation, mRNA stability, translation initiation, internal ribosome entry site, nucleocytoplasmic shuttling, protein-protein interaction
- MeSH terms
- Animals, Virus Replication, RNA-Binding Proteins, Alternative Splicing, RNA Stability, RNA Transport, Polypyrimidine Tract-Binding Protein
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