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
Cites
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Translational control of gene expression
Hannig, E. M. (2001) · BioEssays · doi:10.1002/bies.1108 · Cited by 1,194
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Structure of PTB Bound to RNA: Specific Binding and Implications for Splicing Regulation
Oberstrass, F. C., Auweter, S., Erat, M. C., Hargous, Y., Henning, A., Wenter, P., Reymond, L., Amir-Ahmady, B., Pitsch, S., Black, D. L., et al. (2005) · Science · doi:10.1126/science.1114066 · Cited by 464
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Regulation of Fas Alternative Splicing by Antagonistic Effects of TIA-1 and PTB on Exon Definition
Izquierdo, J. M., Oró, N. M., Bonnal, S., Martínez, C., Castelo, R., Guigó, R., Bilbao, D., & Valcárcel, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.015 · Cited by 364
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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
- Knoch, 2004, Regulation of PTB nucleocytoplasmic translocation and expression of secretory granule proteins in INS-1 cells, Diabetologia, 47, A153
- Knoch, 2006, PTB1 binds to the 5´-UTR of mRNAs encoding proteins of the insulin secretory granules, Diabetologia, 49, 156
- Belsham, 2000, Translation initiation on picornavirus RNA, 869
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A compendium of RNA-binding motifs for decoding gene regulation
Ray, D., Kazan, H., Cook, K. B., Weirauch, M. T., Najafabadi, H. S., Li, X., Gueroussov, S., Albu, M., Zheng, H., Yang, A., et al. (2013) · Nature · doi:10.1038/nature12311 · Cited by 1,480
Circular RNA-protein interactions: functions, mechanisms, and identification
Huang, A., Zheng, H., Wu, Z., Chen, M., & Huang, Y. (2020) · Theranostics · doi:10.7150/thno.42174 · Cited by 914
“RBPs contain various structural motifs, such as the RNA-recognition motif (RRM), dsRNA-binding domain, zinc finger domain, and others [85], and several of these may be involved in circRNA binding.”
BackgroundMechanisms and Functions of Long Non-Coding RNAs at Multiple Regulatory Levels
Zhang, X., Wang, W., Zhu, W., Dong, J., Cheng, Y., Yin, Z., & Shen, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225573 · Cited by 906
“Recently, RNA pull-down and LC-MS assays have revealed that lncRNA MEG3 binds polypyrimidine tract-binding protein 1 (PTBP1), which belongs to the hnRNPs subfamily and controls almost all aspects of mRNA metabolism [96].”
BackgroundAlternative pre-mRNA splicing regulation in cancer: pathways and programs unhingedPreprint
David, C. J., & Manley, J. L. (2010) · Genes & Development · doi:10.1101/gad.1973010 · Cited by 848
“The translational activity of PTBwas shown to be important for the up-regulation of translation of a subset of apoptotic mRNAs upon the induction of TRAIL-induced apoptosis (Sawicka et al. 2008).”
BackgroundMatoulkova, E., Michalova, E., Vojtesek, B., & Hrstka, R. (2012) · RNA Biology · doi:10.4161/rna.20231 · Cited by 357
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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