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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]
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A compendium of RNA-binding motifs for decoding gene regulation
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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].”
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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).”
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To localize or not to localize: mRNA fate is in 3′UTR ends
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“as well as influencing other post-transcriptional steps in gene expressio”
BackgroundIRES-mediated cap-independent translation, a path leading to hidden proteome
Yang, Y., & Wang, Z. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz091 · Cited by 260
Caruso, P. L., Dunmore, B. J., Schlosser, K., Schoors, S., dos Santos, C. C., Perez‐Iratxeta, C., Lavoie, J. R., Zhang, H., Long, L., Flockton, A. R., et al. (2017) · Circulation · doi:10.1161/circulationaha.117.028034 · Cited by 258
Post-transcriptional control of circadian rhythms
Kojima, S., Shingle, D. L., & Green, C. B. (2011) · Journal of Cell Science · doi:10.1242/jcs.065771 · Cited by 247
“Interestingly, hnRNP I shuttles between the cytoplasm and nucleus (Sawicka et al., 2008), and the protein level of hnRNP I in the cytoplasm is rhythmic, even though its overall level is not (Kim et al., 2010). hnRNP I interacts with the 3 -UTR of Per2 mRNA and promotes its degradation (Woo et al.,…”
BackgroundChen, M., Zhang, J., & Manley, J. L. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2513 · Cited by 242
“PTB is also involved in multiple processes, including polyadenylation, mRNA stability and translation initiation in addition to splicing (19).”
Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2
Keppetipola, N., Sharma, S., Li, Q., & Black, D. L. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.691456 · Cited by 201
“…by several stimuli including viral infection, cellular adhesion, apoptosis, and stress conditions such as hypoxia and toxic agents (Hellen et al., 1993; de Hoog et al., 2004; Ma et al., 2007; Galban et al., 2008; Sawicka et al., 2008; Babic et al., 2009; Cobbold et al., 2010; Gorospe et al., 2011).”
BackgroundLicatalosi, D. D., Yano, M., Fak, J. J., Mele, A., Grabinski, S. E., Zhang, C., & Darnell, R. B. (2012) · Genes & Development · doi:10.1101/gad.191338.112 · Cited by 193
Translational control in cellular and developmental processes
Kong, J., & Lasko, P. F. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3184 · Cited by 193
Zhang, L., Yang, Z., Trottier, J., Barbier, O., & Wang, L. (2016) · Hepatology · doi:10.1002/hep.28882 · Cited by 185
“translation initiation and mRNA stability (28).”
Li, Q., Zheng, S., Han, A., Lin, C.-H., Stoilov, P., Fu, X.-D., & Black, D. L. (2014) · eLife · doi:10.7554/elife.01201 · Cited by 174
“PTBP1 is known to also affect miRNA function and cytoplasmic translation (Sawicka et al., 2008; Fred and Welsh, 2009; Gorospe et al., 2011; Kafasla et al., 2012; Xue et al., 2013).”
New Insights into Vinculin Function and Regulation
Peng, X. L., Nelson, E. S., Maiers, J. L., & DeMali, K. A. (2011) · International review of cytology · doi:10.1016/b978-0-12-386043-9.00005-0 · Cited by 179
“Specifically, the 3′ untranslated region of vinculin binds polypyrimidine tract-binding protein (PTB), a widely expressed RNA-binding protein with roles in splicing, polyadenylation, mRNA stability, and translation initiation (Auweter and Allain, 2008; Sawicka et al., 2008).”
BackgroundCold shock proteins: from cellular mechanisms to pathophysiology and disease
Lindquist, J. A., & Mertens, P. R. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0274-6 · Cited by 177
Cleavage and polyadenylation: Ending the message expands gene regulation
Neve, J., Patel, R. J., Wang, Z., Louey, A., & Furger, A. (2017) · RNA Biology · doi:10.1080/15476286.2017.1306171 · Cited by 185
Coelho, M. B., Attig, J., Bellora, N., König, J., Hallegger, M., Kayikci, M., Eyras, E., Ule, J., & Smith, C. W. J. (2015) · The EMBO Journal · doi:10.15252/embj.201489852 · Cited by 161
“Polypyrimidine tract binding (PTB / PTBP1 / hnRNPI) protein is an intensively investigated RNA-binding protein, which regulates splicing and other post-transcriptional steps of gene expression (reviewed in Kafasla et al , 2012; Keppetipola et al , 2012; Sawicka et al , 2008).”
Gerstberger, S. C., Hafner, M., Ascano, M., & Tuschl, T. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-1221-6_1 · Cited by 154
“Sixty RBPs occur with several repeated RRMs; among them are the PTBP and the ELAVL families, regulators of mRNA splicing, stability, and localization (Sawicka et al. 2008; Simone and Keene 2013).”
BackgroundStreamlined platform for short hairpin RNA interference and transgenesis in cultured mammalian cells
Khandelia, P., Yap, K., & Makeyev, E. V. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103532108 · Cited by 148
“Satisfyingly, all four computationally designed shRNAs reduced PTBP1 expression at both the mRNA and the protein levels compared with the shFLuc control (Fig.”
MethodRNA binding protein/RNA element interactions and the control of translation
Pichon, X., A. Wilson, L., Stoneley, M., Bastide, A., A King, H., Somers, J., & E Willis, A. (2012) · Current Protein & Peptide Science · doi:10.2174/138920312801619475 · Cited by 144
Self-citationShu, B., Zhou, Y., Li, H., Zhang, R., He, C., & Yang, X. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00756-x · Cited by 144
“As an RNA-binding protein and a splicing factor, PTBP1 may activate or repress the transcription of a target gene, by regulating pre-mRNA splicing, polyadenylation, mRNA stability, and/or translation initiation [31].”
BackgroundAbdelmohsen, K., Tominaga, K., Lee, E. K., Srikantan, S., Kang, M. J., Kim, M. M., Selimyan, R., Martindale, J. L., Yang, X., Carrier, F., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr488 · Cited by 137
“However, most RBPs influence the fate of target transcripts in multiple ways; for example, the embryonic lethal abnormal vision (elav)/Hu protein HuR stabilizes some target mRNAs, but modulates the translation of other targets (9), AUF1 (AU-binding factor 1)/ hnRNP D (heterogeneous nuclear ribonucleoprotein D) modulat…”
BackgroundThe role of IRES trans-acting factors in regulating translation initiation
King, H. A., Cobbold, L. C., & Willis, A. E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381581 · Cited by 148
Self-citationNew Insights into Functional Roles of the Polypyrimidine Tract-Binding Protein
Romanelli, M. G., Diani, E., & Lievens, P. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141122906 · Cited by 141
“The cell type and the position of the specific RNA binding sites are determinant factors for the variety of PTB effects on RNA destiny [19].”
BackgroundThe human RBPome: From genes and proteins to human disease
Neelamraju, Y., Hashemikhabir, S., & Janga, S. C. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.04.031 · Cited by 119
“4 UTP14A HELZ RBM34 MRPS11 ALKBH5 GPATCH4 CKAP4 SUGP1 ADARB1 RBM4 CXorf57 MRPL42 ZNF593 TLR2 MRPS15 TDRKH TSNAX LLPH TRA2B DUSP14 SCAF8 DDX3X UBE2D1 MAPRE1 CELF1 CPSF7 RALY TRA2A ZNF638 TIPARP FAM103A1 RDM1 KNOP1 HOXB6 RBM41 ENOX2 MRPS26 C1orf52 NOL7 FRG1 MAGOH RBM4B C2orf15 RPP25 ZC3H7B ESRP2 ZC3H18 YTHDF1 UBTF LRP1…”
BackgroundInfluentialNowak, U. M., Matthews, A. J., Zheng, S., & Chaudhuri, J. (2010) · Nature Immunology · doi:10.1038/ni.1977 · Cited by 131
“PTBP1 and PTBP2 are generally considered repressive regulators of splicing that bind RNA with polypyrimidine tracts, block spliceosome assembly at the site and mediate exon exclusion during alternative splicin”
BackgroundMasuda, K., & Kuwano, Y. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1520 · Cited by 116
“In contrast, HuR, PTB, hnRNP A1, and the cytoplasmic polyadenylation-element-binding protein have been shown to promote translation (Abdelmohsen et al., 2008; Hagele, Kuhn, Boning, & Katschinski, 2009; Masuda et al., 2012; Sawicka et al., 2008; R. Yang, Weber, & Carrier, 2006).”
BackgroundPost-Transcriptional Control of the Hypoxic Response by RNA-Binding Proteins and MicroRNAs
Gorospe, M., Tominaga, K., Wu, X., Fähling, M., & Ivan, M. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00007 · Cited by 115
“RBPs and miRNAs can recruit mRNAs to these degradation machineries (reviewed by Butler, 2002; Kedersha and Anderson, 2007; Fabian et al., 2010), but their specific involvement in the hypoxia-triggered changes in mRNA turnover in mammalian systems awaits further study.”
InfluentialCompetitive Regulation of Nucleolin Expression by HuR and miR-494
Tominaga, K., Srikantan, S., Lee, E. K., Subaran, S. S., Martindale, J. L., Abdelmohsen, K., & Gorospe, M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05955-11 · Cited by 108
“Numerous RBPs that affect the stability and translation of mRNAs encoding proliferative proteins have been described, including elav/Hu proteins (the ubiquitous HuR and the primarily neuronal HuB, HuC, and HuD), AU-binding factor 1 (AUF1), tristetraprolin (TTP), KH domain-containing RBP (KSRP), the T-cell intracellula…”
MethodNF90 selectively represses the translation of target mRNAs bearing an AU-rich signature motif
Kuwano, Y., Pullmann, R., Marasa, B. S., Abdelmohsen, K., Lee, E. K., Yang, X., Martindale, J. L., Zhan, M., & Gorospe, M. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp861 · Cited by 105
“For example, HuR (human antigen R) stabilizes some target mRNAs but modulates the translation of other target mRNAs (6), AUF1 (AUbinding factor 1) promotes the decay of some mRNAs but can also stabilize and promote the translation of other target transcripts (7–11), the T-cell intracellular antigen1 (TIA-1) and the TI…”
BackgroundTrans‐acting translational regulatory RNA binding proteins
Harvey, R. F., Smith, T. S., Mulroney, T. E., Queiroz, R. M. L., Pizzinga, M., Dezi, V., Villanueva, E., Ramakrishna, M., Lilley, K. S., & Willis, A. E. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1465 · Cited by 106
“, 2005) and binding of each RRM to different regions of a single RNA enables extensive restructuring of the 50 UTR is essential for this process (Kafasla et al., 2011; Sawicka et al., 2008).”
BackgroundInfluentialSelf-citationRühl, C., Stauffer, E., Kahles, A., Wagner, G., Drechsel, G., Rätsch, G., & Wachter, A. (2012) · The Plant Cell · doi:10.1105/tpc.112.103622 · Cited by 94
“One example for positiondependent splicing is constituted by the hnRNP protein PTB (Xue et al., 2009; Llorian et al., 2010), an in animals, wellcharacterized regulator of AS that binds to pyrimidine-rich motifs within pre-mRNAs (Sawicka et al., 2008; Wachter et al., 2012).”
BackgroundKafasla, P., Morgner, N., Pöyry, T. A. A., Curry, S., Robinson, C. V., & Jackson, R. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.015 · Cited by 94
“…anticipate that they will prove extremely useful for investigating PTB interactions with other picornavirus IRESs, with the numerous cellular mRNA IRESs that have been reported to be PTB-dependent (Sawicka et al., 2008), and with pre-mRNAs that are subject to alternative splicing regulated by PTB.”
BackgroundInfluentialLong non-coding RNA-dependent mechanism to regulate heme biosynthesis and erythrocyte development
Liu, J., Li, Y., Tong, J., Gao, J., Guo, Q., Zhang, L., Wang, B., Zhao, H., Wang, H., Jiang, E., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06883-x · Cited by 93
Flather, D. P., & Semler, B. L. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00594 · Cited by 92
“Frontiers in Microbiology | www.frontiersin.org 2 June 2015 | Volume 6 | Article 594 of complexes through the NPC is energy-independent as GTP hydrolysis is required only as a final step in the transport process (Schwoebel et al., 1998).”
BackgroundDefining the roles and interactions of PTB
Kafasla, P., Mickleburgh, I., Llorian, M., Coelho, M. B., Gooding, C., Cherny, D., Joshi, A., Kotik-Kogan, O., Curry, S., Eperon, I. C., et al. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120044 · Cited by 97
Polypyrimidine tract‐binding protein stimulates the poliovirus IRES by modulating eIF4G binding
Kafasla, P., Morgner, N., Robinson, C. V., & Jackson, R. J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.231 · Cited by 97
“It will be interesting to see that those cellular mRNA IRESs that are strongly stimulated by PTB (Sawicka et al, 2008) follow the poliovirus or the EMCV model.”
BackgroundRNA–protein interactions in vivo: global gets specific
Änkö, M., & Neugebauer, K. M. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.02.005 · Cited by 92
Quantitative Map of Proteome Dynamics during Neuronal Differentiation
Frese, C. K., Mikhaylova, M., Stucchi, R., Gautier, V., Liu, Q., Mohammed, S., Heck, A. J. R., Altelaar, M. A. F., & Hoogenraad, C. C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.025 · Cited by 88
“Ptbp2 is predominantly expressed in brain tissue during the early stages of neurogenesis, and its main function is the precisely timed negative regulation of alternative splicing events of a distinct set of target genes that play key roles in neuronal differentiation (Sawicka et al., 2008).”
BackgroundIzaguirre, D. I., Zhu, W., Hai, T., Beird, H. C., Krahe, R., & Cote, G. J. (2011) · Molecular Carcinogenesis · doi:10.1002/mc.20859 · Cited by 92
“The protein contains four RNArecognitions motifs, an N-terminal nuclear localization signal, and a nuclear export signal [30,31].”
The RNA-binding protein PTBP1 is necessary for B cell selection in germinal centers
Monzón‐Casanova, E., Screen, M., Díaz‐Muñoz, M. D., Coulson, R., Bell, S. E., Lamers, G., Solimena, M., Smith, C. W. J., & Turner, M. (2018) · Nature Immunology · doi:10.1038/s41590-017-0035-5 · Cited by 87
Cho, S. K., Sharma, P., Butler, N., Kang, I., Shah, S. N., Rao, A. G., & Hannapel, D. J. (2015) · Journal of Experimental Botany · doi:10.1093/jxb/erv389 · Cited by 86
RBM4 down-regulates PTB and antagonizes its activity in muscle cell–specific alternative splicing
Lin, J.-C., & Tarn, W. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007131 · Cited by 85
“The polypyrimidine tract-binding (PTB) protein is a master regulator of alternative splicing in mammalian cells and also functions at several other steps of mRNA metabolism (Sawicka et al., 2008).”
Differential protein occupancy profiling of the mRNA transcriptome
Schueler, M., Munschauer, M., Gregersen, L. H., Finzel, A., Loewer, A., Chen, W., Landthaler, M., & Dieterich, C. (2014) · Genome biology · doi:10.1186/gb-2014-15-1-r15 · Cited by 84
“Yet, recent analyses suggest that they may also contribute to mRNA stability and influence translation [39-41].”
BackgroundHigh-throughput characterization of protein-RNA interactions
Cook, K. B., Hughes, T., & Morris, Q. (2014) · Briefings in Functional Genomics · doi:10.1093/bfgp/elu047 · Cited by 86
Stauffer, E., Westermann, A. J., Wagner, G., & Wachter, A. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04321.x · Cited by 80
Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses
Lloyd, R. E. (2015) · Virology · doi:10.1016/j.virol.2015.03.001 · Cited by 81
“PTB is a shuttling, but mostly nuclear resident protein that associates with pre-mRNAs and plays roles in pre-mRNA processing, alternative splicing, mRNA metabolism and transport (Kafasla et al., 2010; Sawicka et al., 2008).”
BackgroundMajumder, M., Yaman, İ., Gaccioli, F., Zeenko, V. V., Wang, C., Caprara, M. G., Venema, R. C., Komar, A. A., Snider, M. D., & Hatzoglou, M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01774-08 · Cited by 81
“Alternative splicing gives rise to several isoforms of PTB (72).”
BackgroundInfluentialRNA ‐binding proteins, neural development and the addictions
Bryant, C. D., & Yazdani, N. (2015) · Genes Brain & Behavior · doi:10.1111/gbb.12273 · Cited by 82
“In addition to splicing, PTBP1 can bind directly to 3′ UTRs to regulate cleavage in polyadenylation, 3′ UTR exon inclusion and mRNA stability (Sawicka et al. 2008).”
BackgroundRNA‐binding proteins implicated in the hypoxic response
Masuda, K., Abdelmohsen, K., & Gorospe, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00842.x · Cited by 80
“Other effects of PTB, such as its ability to promote polyadenylation [33], may also contribute to the increased stability of the insulin mRNA.”
BackgroundInfluentialLncRNA MACC1-AS1 sponges multiple miRNAs and RNA-binding protein PTBP1
Zhang, X., Zhou, Y., Chen, S., Li, W., Chen, W., & Gu, W. (2019) · Oncogenesis · doi:10.1038/s41389-019-0182-7 · Cited by 79
TIA1 Prevents Skipping of a Critical Exon Associated with Spinal Muscular Atrophy
Singh, N. N., Seo, J., Ottesen, E. W., Shishimorova, M., Bhattacharya, D., & Singh, R. N. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00945-10 · Cited by 78
“This could be due to an indirect effect owing to alternation of other cellular processes (46).”
BackgroundHannigan, M. M., Zagore, L. L., & Licatalosi, D. D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.089 · Cited by 79
“Loss of Ptbp2 may also expose sites that can be recognized by other RBPs and/or alter RNA structure, leading to widespread redistribution of RBP-RNA interactions.”
InfluentialSola, I., Galán, C., Mateos‐Gómez, P. A., Palacio, L., Zúñiga, S., Cruz, J. L. G., Almazán, F., & Enjuanes, L. (2011) · Journal of Virology · doi:10.1128/jvi.00195-11 · Cited by 76
Proteomics of methyl jasmonate induced defense response in maize leaves against Asian corn borer
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“RNA-binding proteins (RBPs) play key roles in posttranscriptional control of RNAs, which along with transcriptional regulation, are an important way to regulate patterns of gene expression during development [45].”
BackgroundFeng, Z., Zhang, X., Zhou, J., Li, Q., Chu, L., Di, G., Xu, Z., Chen, Q., Wang, M., Jiang, X., et al. (2023) · Nature Cancer · doi:10.1038/s43018-023-00650-8 · Cited by 70
“…in different solid tumor cell lines, and the clinical samples analyzed in the database also support this evidence that EIF4G2/PTBP1 is associated with the proliferation and progression of tumor cells with vigorous metabolism 55,56 , extensively driving mRNA splicing, stability and transport 57 .”
Minireview: Posttranscriptional Regulation of the Insulin and Insulin-Like Growth Factor Systems
Lee, E. K., & Gorospe, M. (2009) · Endocrinology · doi:10.1210/en.2009-1123 · Cited by 66
SINEUP long non-coding RNA acts via PTBP1 and HNRNPK to promote translational initiation assemblies
Toki, N., Takahashi, H., Sharma, H., Valentine, M. N. Z., Rahman, M. F., Zucchelli, S., Gustincich, S., & Carninci, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa814 · Cited by 68
Internal translation initiation of picornaviruses and hepatitis C virus
Niepmann, M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.05.002 · Cited by 68
Insights into the Biology of IRES Elements through Riboproteomic Approaches
Pacheco, A., & Martı́nez-Salas, E. (2010) · BioMed Research International · doi:10.1155/2010/458927 · Cited by 67
“ITAFs, as it is the case of PTB, do not act alone but in combination with various factors presumably contributing to explain the opposite effects on IRES activity [34].”
BackgroundPBRM1, SETD2 and BAP1 — the trinity of 3p in clear cell renal cell carcinoma
Walton, J., Lawson, K. A., Prinos, P., Finelli, A., Arrowsmith, C. H., & Ailles, L. (2022) · Nature Reviews Urology · doi:10.1038/s41585-022-00659-1 · Cited by 74
Viral Subversion of Host Functions for Picornavirus Translation and RNA Replication
Chase, A. J., & Semler, B. L. (2012) · Future Virology · doi:10.2217/fvl.12.2 · Cited by 64
Fingerhut, J. M., Moran, J. V., & Yamashita, Y. M. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008028 · Cited by 62
Taniguchi, K., Uchiyama, K., & Akao, Y. (2020) · Cancer Science · doi:10.1111/cas.14694 · Cited by 59
Wang, Y., Li, Z., Xu, S., Li, W., Chen, M., Jiang, M., & Fan, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04509-1 · Cited by 60
“FIRRE enhances BECN1 mRNA stability in PTBP1-mediated manner Based on the function of PTBP1 in cytoplasm on mRNA stability [25], we hypothesized that FIRRE and PTBP1 could modulate BECN1 mRNA stability.”
BackgroundThe Sequence and Structure Determine the Function of Mature Human miRNAs
Rolle, K., Piwecka, M., Belter, A., Wawrzyniak, D., Jeleniewicz, J., Barciszewska, M. Z., & Barciszewski, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151246 · Cited by 60
Bailey, D., Karakasiliοtis, I., Vashist, S., Chung, L. M. W., Reese, J., McFadden, N., Benson, A., Yarovinsky, F., Peter Simmonds, K., & Goodfellow, I. (2010) · Journal of Virology · doi:10.1128/jvi.02053-09 · Cited by 59
RNA-Binding Protein PTB and MicroRNA-221 Coregulate AdipoR1 Translation and Adiponectin Signaling
Lustig, Y., Barhod, E., Ashwal-Fluss, R., Gordin, R., Shomron, N., Umansky, K. B., Hemi, R., Karasik, A., & Kanety, H. (2013) · Diabetes · doi:10.2337/db13-1032 · Cited by 56
“PTB plays critical roles in mRNA metabolism and regulates mRNA splicing, polyadenylation, and mRNA stability (38,39).”
BackgroundWachter, A., Rühl, C., & Stauffer, E. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00081 · Cited by 54
“Splicing-independent functions of PTBs have also been described in other species, including repression of translation in Drosophila (Besse et al., 2009) and human (Boutz et al., 2007), as well as the widespread positive role in translation from IRES (Auweter and Allain, 2008; Sawicka et al., 2008).”
BackgroundInfluentialBoros, Á., Nemes, C., Pankovics, P., Kapusinszky, B., Delwart, E., & Reuter, G. (2012) · Journal of General Virology · doi:10.1099/vir.0.043224-0 · Cited by 54
“The presence of a nearly identical p(Y) tract located at the same position (upper loop region of the 39 UTR) in murine noroviruses (MNVs) and in turkey/M176/2011/ HUN indicates that it could serve as a core binding site for the cellular poly(C)-binding proteins (PCBP1 and 2) and/ or PTB (Makeyev & Liebhaber, 2002; Saw…”
BackgroundInfluentialChase, A. J., Daijogo, S., & Semler, B. L. (2013) · Journal of Virology · doi:10.1128/jvi.02503-13 · Cited by 54
Agis-Juárez, R. A., Galván, I. J., Medina, F., Daikoku, T., Padmanabhan, R., Ludert, J. E., & del Angel, R. M. (2009) · Journal of General Virology · doi:10.1099/vir.0.013433-0 · Cited by 54
“Moreover, a phosphorylated form of PTB was found associated with the membrane-bound HCV replication complex (Chang & Luo, 2006).”
InfluentialHsu, J. C.-C., Reid, D. W., Hoffman, A. M., Sarkar, D., & Nicchitta, C. V. (2018) · RNA · doi:10.1261/rna.063313.117 · Cited by 54
“…evidence that many previously identified RNA-binding proteins are multifunctional, a role for nonconventional modes of RNA localization and anchoring to the ER membrane can now be reasonably considered (Mangus et al. 2003; Sawicka et al. 2008; Markus and Morris 2009; Turner and Hodson 2012).”
Bocobza, S. E., & Aharoni, A. (2014) · The Plant Journal · doi:10.1111/tpj.12540 · Cited by 52
“Polypyrimidine tract-binding proteins were reported to be involved in the regulation of premRNA splicing in plants (Stauffer et al., 2010; R€uhl et al., 2012), RNA poly-adenylation, and in mRNA stability (Sawicka et al., 2008).”
BackgroundThe human insulin receptor mRNA contains a functional internal ribosome entry segment
Spriggs, K. A., Cobbold, L. C., Ridley, S. H., Coldwell, M. J., Bottley, A., Bushell, M., Willis, A. E., & Siddle, K. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp623 · Cited by 51
“The proteins required for this process have yet to be fully identified although it has been found that many cellular and viral IRESs require polypryimidine tract binding protein (PTB) for activity (4, 5 ).”
BackgroundSelf-citationInsights into Dengue Virus Genome Replication
Alcaráz‐Estrada, S. L., Yocupicio‐Monroy, M., & del Angel, R. M. (2010) · Future Virology · doi:10.2217/fvl.10.49 · Cited by 50
“Since most of the functions of PTB are carried out in the nucleus, the major location of this protein is in the nuclear compartment; however, it also shuttles between the nucleus and the cytoplasm [120].”
Cui, J., & Placzek, W. J. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.60 · Cited by 50
“PTBP1 is a RNA binding protein that regulates RNA splicing, IRES (internal ribosome entry segment)-mediated translation initiation, 3′-end processing, mRNA turnover, localization, and transportation.(28) PTBP1 has been shown to be involved in distinct cellular processes including T-cell activation,(29) HCV replication…”
BackgroundZhang, L., Yang, Z., Huang, W., & Wu, J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1423-6 · Cited by 50
Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus
Jiang, L., Yao, H., Duan, X., Lü, X., & Liu, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.05.036 · Cited by 47
“Though PTB is present predominantly in the nucleus at static state, a significant cytoplasmic localization was also reported and it can shuttle between the nucleus and cytoplasm [38,39].”
Reid, D. C., Chang, B. L., Gunderson, S., Sugden, L. A., Thompson, W. A., & Fairbrother, W. G. (2009) · RNA · doi:10.1261/rna.1821809 · Cited by 48
“…polypyrimidine tract binding protein (PTB), a well-studied member of the hnRNP family (Perez et al. 1997a; Liu et al. 2002; Shen et al. 2004; Wollerton et al. 2004; Amir-Ahmady et al. 2005; Sharma et al. 2005; Spellman and Smith 2006; Boutz et al. 2007; Matlin et al. 2007; Sawicka et al. 2008).”
BackgroundA miR‐194/PTBP1/CCND3 axis regulates tumor growth in human hepatocellular carcinoma
Kang, H., Heo, S., Shin, J. J., Ji, E., Tak, H., Ahn, S., Lee, K. J., Lee, E. K., & Kim, W. (2019) · The Journal of Pathology · doi:10.1002/path.5325 · Cited by 47
The Long Non-coding RNAs: Paramount Regulators of the NLRP3 Inflammasome
Menon, M. P., & Hua, K. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.569524 · Cited by 47
“This resulted in the decay of SHP mRNA (149, 150).”
BackgroundAID targeting is dependent on RNA polymerase II pausing
Kenter, A. L. (2012) · Seminars in Immunology · doi:10.1016/j.smim.2012.06.001 · Cited by 50
miR-124-3p is a chronic regulator of gene expression after brain injury
Vuokila, N., Łukasiuk, K., Bot, A. M., van Vliet, E. A., Aronica, E., Pitkänen, A., & Puhakka, N. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2911-z · Cited by 46
Zhu, L., Wei, Q., Qi, Y., Ruan, X., Wu, F., Li, L., Zhou, J., Liu, W., Jiang, T., Zhang, J., et al. (2019) · Molecular Therapy · doi:10.1016/j.ymthe.2019.05.023 · Cited by 45
DeBoer, E., Kraushar, M. L., Hart, R. P., & Rašin, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.05.042 · Cited by 47
Licatalosi, D. D. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-29073-7_6 · Cited by 46
Multiple Mobile mRNA Signals Regulate Tuber Development in Potato
Hannapel, D. J., & Banerjee, A. K. (2017) · Plants · doi:10.3390/plants6010008 · Cited by 45
“These proteins contain four RNA recognition motifs that bind at four cytosine/uracil (CU) motifs located within 100–200-nt regions inside the UTRs of the target RNAs [61].”
BackgroundJames, C. C., & Smyth, J. W. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.09.054 · Cited by 46
Joshi, A., Coelho, M. B., Kotik-Kogan, O., Simpson, P. J., Matthews, S., Smith, C. W. J., & Curry, S. (2011) · Structure · doi:10.1016/j.str.2011.09.020 · Cited by 45
The Domains of Polypyrimidine Tract Binding Protein Have Distinct RNA Structural Preferences
Clerté, C., & Hall, K. B. (2009) · Biochemistry · doi:10.1021/bi8016872 · Cited by 44
Fochi, S., Lorenzi, P., Galasso, M., Stefani, C., Trabetti, E., Zipeto, D., & Romanelli, M. G. (2020) · Genes · doi:10.3390/genes11040402 · Cited by 42
“Beside its role in splicing processes, PTBP1 participates in several steps of RNA metabolism, including stability, polyadenylation, transport and cap-independent translation driven by internal ribosomal entry sites (IRESs) [41,47,48].”
BackgroundMarkus, M. A., Marques, F. Z., & Morris, B. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028926 · Cited by 42
Ma, J., Weng, L., Jia, Y., Liu, B., Wu, S., Xue, L., Yin, X., Mao, A., Wang, Z., & Shang, M. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14896 · Cited by 41
LncRNAs and their RBPs: How to influence the fate of stem cells?
Zhao, C., Xie, W. J., Zhu, H., Zhao, M., Liu, W., Wu, Z., Wang, L., Zhu, B., Li, S., Zhou, Y., et al. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02851-x · Cited by 40
“In the cytoplasm, PTBP1 is involved in translation initiation and mRNA stability [89].”
BackgroundPTBP1 mRNA isoforms and regulation of their translation
de Tacca, L. A., Pulos-Holmes, M. C., Floor, S. N., & Cate, J. H. D. (2019) · RNA · doi:10.1261/rna.070193.118 · Cited by 39
“The alternatively spliced isoforms, PTBP1-2 and PTBP1-4, encode an additional 19 or 26 amino acids, respectively, between the RRM2 and RRM3 domains derived from exon 9 inclusion (Garcia-Blanco et al. 1989; Valcárcel and Gebauer 1997; Sawicka et al. 2008; Romanelli et al. 2013).”
Background
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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