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Context-dependent control of alternative splicing by RNA-binding proteins
Open accessAbstract
Sequence-specific RNA-binding proteins (RBPs) bind to pre-mRNA to control alternative splicing, but it is not yet possible to read the 'splicing code' that dictates splicing regulation on the basis of genome sequence. Each alternative splicing event is controlled by multiple RBPs, the combined action of which creates a distribution of alternatively spliced products in a given cell type. As each cell type expresses a distinct array of RBPs, the interpretation of regulatory information on a given RNA target is exceedingly dependent on the cell type. RBPs also control each other's functions at many levels, including by mutual modulation of their binding activities on specific regulatory RNA elements. In this Review, we describe some of the emerging rules that govern the highly context-dependent and combinatorial nature of alternative splicing regulation.
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“Alternative splicing patterns (BOX 1) are regulated by specialized pre-mRNA binding proteins that alter spliceosome assembly at specific splice sites5–8”
From The neurogenetics of alternative splicing (2016) · cites this paper as [7]
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Development and Applications of CRISPR-Cas9 for Genome Engineering
Hsu, P. D., Lander, E. S., & Zhang, F. (2014) · Cell · doi:10.1016/j.cell.2014.05.010 · Cited by 5,762
Transcriptome-wide Identification of RNA-Binding Protein and MicroRNA Target Sites by PAR-CLIP
Hafner, M., Landthaler, M., Burger, L., Khorshid, M., Hausser, J., Berninger, P., Rothballer, A., Ascano, M., Jungkamp, A.-C., Munschauer, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.009 · Cited by 2,873
Mechanisms of Alternative Pre-Messenger RNA Splicing
Black, D. L. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161720 · Cited by 2,704
The Spliceosome: Design Principles of a Dynamic RNP Machine
Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665
Expansion of the eukaryotic proteome by alternative splicing
Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,270
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
Frequent pathway mutations of splicing machinery in myelodysplasia
Yoshida, K., Sanada, M., Shiraishi, Y., Nowak, D., Nagata, Y., Yamamoto, R., Sato, Y., Sato-Otsubo, A., Kon, A., Nagasaki, M., et al. (2011) · Nature · doi:10.1038/nature10496 · Cited by 2,029
Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012
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
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Kim, H. J., Kim, N. C., Wang, Y., Scarborough, E. A., Moore, J., Diaz, Z., MacLea, K. S., Freibaum, B. D., Li, S., Molliex, A., et al. (2013) · Nature · doi:10.1038/nature11922 · Cited by 1,478
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Dvinge, H., Kim, E. H., Abdel-Wahab, O. I., & Bradley, R. K. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.51 · Cited by 706
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Park, E., Pan, Z., Zhang, Z., Lin, L., & Xing, Y. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.11.002 · Cited by 385
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de Klerk, E., & ‘t Hoen, P. A. C. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.01.001 · Cited by 350
Alternative splicing and related RNA binding proteins in human health and disease
Tao, Y., Zhang, Q., Wang, H., Yang, X., & Mu, H. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01734-2 · Cited by 351
The neurogenetics of alternative splicing
Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340
Pradella, D., Naro, C., Sette, C., & Ghigna, C. (2017) · Molecular Cancer · doi:10.1186/s12943-016-0579-2 · Cited by 334
Intron retention as a component of regulated gene expression programs
Jacob, A. G., & Smith, C. W. J. (2017) · Human Genetics · doi:10.1007/s00439-017-1791-x · Cited by 339
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Sibley, C. R., Blázquez, L., & Ule, J. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.46 · Cited by 327
Aberrant RNA Splicing in Cancer
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Calixto, C. P. G., Guo, W., James, A. B., Τzioutziou, N. A., Entizne, J. C., Panter, P. E., Knight, H., Nimmo, H. G., Zhang, R., & Brown, J. W. S. (2018) · The Plant Cell · doi:10.1105/tpc.18.00177 · Cited by 304
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Han, Y., Gao, S., Muegge, K., Zhang, W., & Zhou, B. (2015) · Bioinformatics and Biology Insights · doi:10.4137/bbi.s28991 · Cited by 303
Wang, Y., Xie, Z., Kutschera, E., Adams, J. I., Kadash-Edmondson, K. E., & Xing, Y. (2024) · Nature Protocols · doi:10.1038/s41596-023-00944-2 · Cited by 296
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Frankiw, L., Baltimore, D., & Li, G. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0195-7 · Cited by 253
Wang, E., & Aifantis, I. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.04.011 · Cited by 246
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Mazin, P., Khaitovich, P., Cardoso-Moreira, M., & Kaessmann, H. (2021) · Nature Genetics · doi:10.1038/s41588-021-00851-w · Cited by 219
Feng, M., Xie, X., Han, G., Zhang, T., Li, Y., Li, Y., Yin, R., Wang, Q., Zhang, T., Wang, P., et al. (2021) · Blood · doi:10.1182/blood.2020009676 · Cited by 213
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Wang, Z., Li, B., Luo, Y.-X., Lin, Q., Liu, S., Zhang, X., Zhou, H., Yang, J., & Qu, L. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.035 · Cited by 209
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Damianov, A., Yi, Y., Lin, C.-H., Lee, J.-A., Tran, D., Vashisht, A. A., Bahrami‐Samani, E., Xing, Y., Martin, K. C., Wohlschlegel, J. A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.040 · Cited by 210
Emerging Functions of Circular RNAs.
Cortés-López, M., & Miura, P. (2016) · Europe PMC (PubMed Central) · Cited by 204
Pseudouridine synthases modify human pre-mRNA co-transcriptionally and affect pre-mRNA processing
Martínez, N. M., Su, A., Burns, M. C., Nussbacher, J. K., Schaening-Burgos, C., Sathe, S., Yeo, G. W.-M., & Gilbert, W. V. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.023 · Cited by 201
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Nikom, D., & Zheng, S. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00717-6 · Cited by 201
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Shao, C., Yang, B., Wu, T., Huang, J. S., Tang, P., Zhou, Y., Zhou, J. J., Qiu, J., Jiang, L., Li, H., et al. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2906 · Cited by 177
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Naro, C., Jolly, A., Persio, S. D., Bielli, P., Setterblad, N., Alberdi, A. J., Vicini, E., Geremia, R., de la Grange, P., & Sette, C. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.03.003 · Cited by 167
The emerging role of alternative splicing in senescence and aging
Deschênes, M., & Chabot, B. (2017) · Aging Cell · doi:10.1111/acel.12646 · Cited by 172
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Hsiao, Y.-H. E., Bahn, J. H., Yang, Y., Lin, X., Tran, S. S., Yang, E.-W., Quinones-Valdez, G., & Xiao, X. G. (2018) · Genome Research · doi:10.1101/gr.231209.117 · Cited by 166
Karimi, H. Z., Baldrich, P., Rutter, B. D., Borniego, L., Zajt, K. K., Meyers, B. C., & Innes, R. W. (2022) · The Plant Cell · doi:10.1093/plcell/koac043 · Cited by 163
Bebee, T. W., Park, J. W., Sheridan, K. I., Warzecha, C. C., Cieply, B. W., Rohacek, A. M., Xing, Y., & Carstens, R. P. (2015) · eLife · doi:10.7554/elife.08954 · Cited by 161
Papasaikas, P., Tejedor, J. R., Vigevani, L., & Valcárcel, J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.030 · Cited by 172
Wang, H., Zhang, Y., Wang, T., Yang, Q., Yang, Y., Li, Z., Li, B., Wen, X., Yin, W., Yin, W., et al. (2021) · The Plant Cell · doi:10.1093/plcell/koab046 · Cited by 163
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Daguenet, É., Dujardin, G., & Valcárcel, J. (2015) · EMBO Reports · doi:10.15252/embr.201541116 · Cited by 159
Wang, X., Li, J., Bian, X., Wu, C., Hua, J., Chang, S., Yu, T., Li, H., Li, Y., Hu, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012881118 · Cited by 156
Linares, A. J., Lin, C.-H., Damianov, A., Adams, K. L., Novitch, B. G., & Black, D. L. (2015) · eLife · doi:10.7554/elife.09268 · Cited by 159
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Wang, L., Yang, T., Wang, B., Lin, Q., Zhu, S., Li, C., Ma, Y.-C., Tang, J., Xing, J., Li, X., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz1622 · Cited by 149
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Dvinge, H., Guenthoer, J., Porter, P. L., & Bradley, R. K. (2019) · Genome Research · doi:10.1101/gr.246678.118 · Cited by 147
Garrido-Martín, D., Borsari, B., Calvo, M., Reverter, F., & Guigó, R. (2021) · Nature Communications · doi:10.1038/s41467-020-20578-2 · Cited by 147
Funnell, T., Tasaki, S., Oloumi, A., Araki, S., Kong, E., Yap, D., Nakayama, Y., Hughes, C. S., Cheng, S., Tozaki, H., et al. (2017) · Nature Communications · doi:10.1038/s41467-016-0008-7 · Cited by 139
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Mailer, R. K., Joly, A.-L., Liu, S., Éliás, S., Tegner, J. N., & Andersson, J. (2015) · Scientific Reports · doi:10.1038/srep14674 · Cited by 140
Emerging roles for RNA-binding proteins as effectors and regulators of cardiovascular disease
de Bruin, R. G., Rabelink, T. J., van Zonneveld, A. J., & van der Veer, E. P. (2016) · European Heart Journal · doi:10.1093/eurheartj/ehw567 · Cited by 133
Ye, J., Beetz, N., O’Keeffe, S., Tapia, J. C., Macpherson, L. J., Chen, W. V., Bassel‐Duby, R., Olson, E. N., & Maniatis, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1508461112 · Cited by 124
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Metadata
- Authors
- Fu, X.-D., & Ares, M.
- Affiliations
- University of California San Diego (US)
- University of California, Santa Cruz (US)
- Corresponding author
- Fu, Xiang-Dong
- Ares, Manuel
- Venue
- Nature Reviews Genetics
- Published
- 2014-08-12
- Volume
- 15
- Issue
- 10
- Pages
- 689-701
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- PMC
- PMC4440546
- OpenAlex
- W2029979788
- Cited by
- 1,044
- References
- 176
- Citations by year
- 2026: 67 · 2025: 95 · 2024: 89 · 2023: 93 · 2022: 92 · 2021: 99 · 2020: 93 · 2019: 94 · 2018: 93 · 2017: 94 · 2016: 68 · 2015: 61 · 2014: 5
- FWCI
- 7.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM052872, GM049369, GM040478, GM052872, R01GM049369, R01GM040478)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- alternative splicing, RNA-binding proteins, splicing regulation, pre-mRNA, combinatorial regulation, cell-type-specific splicing, splicing patterns
- MeSH terms
- Animals, Binding Sites, Humans, Organ Specificity, Protein Binding, RNA-Binding Proteins, Alternative Splicing, Regulatory Elements, Transcriptional, Cellular Microenvironment
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