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Fox-1 family of RNA-binding proteins
Open accessAbstract
The Fox-1 family of RNA-binding proteins are evolutionarily conserved regulators of tissue-specific alternative splicing in metazoans. The Fox-1 family specifically recognizes the (U)GCAUG stretch in regulated exons or in flanking introns, and either promotes or represses target exons. Recent unbiased bioinformatics analyses of alternatively spliced exons and comparison of various vertebrate genomes identified the (U)GCAUG stretch as a highly conserved and widely distributed element enriched in intronic regions surrounding exons with altered inclusion in muscle, heart, and brain, consistent with specific expression of Fox-1 and Fox-2 in these tissues. Global identification of Fox-2 target RNAs in living cells revealed that many of the Fox-2 target genes themselves encode splicing regulators. Further systematic elucidation of target genes of the Fox-1 family and other splicing regulators in various tissues will lead to a comprehensive understanding of splicing regulatory networks.
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![Fig. 1 The Fox-1 family RNA-binding proteins are phylogenetically conserved. a Amino acid sequence alignment of the RRM domain of the Fox-1 family proteins in human and mouse (Fox-1, Fox-2, and Fox-3), zebrafish (a2bp1, LOC797814, zFox-1/2bp1l, and zgc85694), fruitfly (Drosophila CG32062), and nematode (C. elegans FOX-1, ASD-1, and SPN-4). Identical amino acid residues are shaded in orange and residues with similar properties are in yellow. The secondary structure of the human Fox-1 RRM domain is indicated above the alignment [23]. b Schematic illustration of the domain structure of mouse Fox-1 and Fox-2, zebrafish Fox-1/A2bp1l, and C. elegans FOX-1. RRM domain is in orange. Identities of amino acid sequences of each domain compared to that of mouse Fox-1 are indicated. Amino acid positions are indicated. c Amino acid sequence alignment of putative hPY-NLS of the Fox-1 family proteins. The C-terminal-most regions of mouse Fox-1, Fox-2, zebrafish a2bp1, zFox-1/2bp1l, Drosophila CG32062, and C. elegans FOX-1 and ASD-1 are aligned with confirmed hPY-NLS of human hnRNP A1, hnRNP D, hnRNP F, and TAP [18]. Residues that match the consensus of hPY-NLS [18] are shaded in orange and yellow. ϕ, hydrophobic side chain. Positions of the N-terminal-most residues are indicated. d Solution structure of the RRM domain of Fox-1/Fox-2 in complex with 5′-UGCAUGU-3′ in ribbon (protein backbone) and stick (RNA) representation. Right panel Image of left panel rotated by 90° as indicated. Important protein side chains and peptide bonds involved in hydrophobic or static interactions with the RNA are represented as sticks. Oxygen, nitrogen, hydrogen, and phosphorus atoms are in red, blue, light yellow, and magenta, respectively. Carbon atoms in the protein, the RNA backbone, and bases are in green, yellow, and gray, respectively. Hydrogen bonds are indicated as cyan dotted sticks. Hydrogen atoms in the RNA backbone are omitted except for one involved in a hydrogen bond. Illustrations were generated from a dataset deposited as ‘2err’ in PDBj database with MOLMOL [78]](/paper-figures/46f92f2d09934e6dbbf815a26b4e0f2b/fox-1-family-of-rna-binding-proteins-figure-1.jpg)
![Fig. 3 Schematic structure and major splicing patterns of the mouse Fox-1/A2bp1 and Fox-2/Rbm9 genes. Boxes indicate exons and horizontal lines indicate introns. Use of these exons is supported by cDNA and/or EST sequences in GenBank/EMBL/DDBJ databases, and the exons are designated after [19] for Fox-2/Rbm9 and human orthologs in [14]. Coding regions are coloured; RRM domains in orange, brain-specific region in green, muscle-specific region in magenta, other isoform-specific regions in blue, and common regions in yellow. The size of the exons is not proportional to that of the introns](/paper-figures/759d5da591a1490184a9826f6878452b/fox-1-family-of-rna-binding-proteins-figure-3.jpg)
![Fig. 4 A model for repression of prespliceosome complex formation by the Fox-1 family. The repression of calcitonin-specific exon 4 of calcitonin/CGRP pre-mRNA in neuronal cells by the Fox-1 family involves two distinct regulatory events. First, the −34 element in the UIF region prevents E′ complex formation through repressing SF1 binding to the branch point (B). Second, the +45 exonic element blocks transition to E complex via inhibiting U2AF65 binding to polypyrimidine tract (PY). This figure is modified from [49]](/paper-figures/0e3f6814588b4d23adf9e09bd7ec6a93/fox-1-family-of-rna-binding-proteins-figure-4.jpg)
![Fig. 5 Fox-1 family proteins ASD-1 and FOX-1 regulate tissue-specific mutually exclusive alternative splicing of the FGFR gene, egl-15, in C. elegans. a Tissue-specific mutually exclusive selection exons of the egl-15 gene of C. elegans. Note that muscle-specific exon 5A resides downstream of exon 5B. b Schematic illustration of muscle-specific repression of exon 5B. Nucleotide sequence of the UIF region is presented. The cis-elements for tissue-specific regulation are in orange. Fox, ASD-1 or FOX-1; SUP, SUP-12. (c,d) Left lateral view of adult hermaphrodite worms expressing egl-15 alternative splicing reporter in body wall muscles and vulval muscles in the wild-type (wt) background (c) and the asd-1; fox-1 double mutant background (d). Merged images of DIC and confocal images of GFP (green) and RFP (magenta). The egl-15 alternative splicing reporter worms express either RFP, representing exon 5A selection, or GFP, representing exon 5B selection, in body wall muscles and vulval muscles (see [16] for detail). Note that in the asd-1; fox-1 double mutant, vulval muscles (arrowheads) express GFP and are mislocalized off the vulva (Vul, arrows), and late embryos with reporter expression in body wall muscles retained in the uterus. Anterior is to the left. Scale bar in (c) 50 μm. (c,d) are modified from [16]](/paper-figures/d1b3fec2258a4678a16d014c4dce0748/fox-1-family-of-rna-binding-proteins-figure-5.jpg)
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“RBFOX binding upstream of, or within, an alternative exon typically inhibits exon inclusion, whereas downstream binding usually promotes splicing48.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [48]
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Cites
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,156
Alternative isoform regulation in human tissue transcriptomes
Wang, E. T., Sandberg, R., Luo, S., Khrebtukova, I., Zhang, L., Mayr, C., Kingsmore, S. F., Schroth, G. P., & Burge, C. B. (2008) · Nature · doi:10.1038/nature07509 · Cited by 5,181
Pan, Q., Shai, O., Lee, L. J., Frey, B. J., & Blencowe, B. J. (2008) · Nature Genetics · doi:10.1038/ng.259 · Cited by 3,951
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
HITS-CLIP yields genome-wide insights into brain alternative RNA processing
Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352 · cited 2×
“These stories are reminiscent of the CLIP-seq analysis of NOVA that led to the discovery that NOVA interacts with 30 UTRs of target mRNAs and regulates alternative polyadenylation in the brain [43].”
MethodUnderstanding alternative splicing: towards a cellular code
Matlin, A. J., Clark, F., & Smith, C. W. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1645 · Cited by 1,299
Alternative splicing: increasing diversity in the proteomic world
Graveley, B. R. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(00)02176-4 · Cited by 1,228
Maris, C., Dominguez, C., & Allain, F. H. ‐. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04653.x · Cited by 1,135
Lim, J., Hao, T., Shaw, C., Patel, A. J., Szabó, G., Rual, J.-F., Fisk, C. J., Li, N., Smolyar, A., Hill, D. E., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.032 · Cited by 789
ESRP1 and ESRP2 Are Epithelial Cell-Type-Specific Regulators of FGFR2 Splicing
Warzecha, C. C., Sato, T. K., Nabet, B., Hogenesch, J. B., & Carstens, R. P. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.025 · Cited by 580
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Mechanisms and Consequences of Alternative Polyadenylation
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Busch, A., & Hertel, K. J. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.100 · Cited by 418
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Zhang, X., Chen, M. H., Wu, X., Kodani, A., Fan, J., Doan, R. N., Ozawa, M., Ma, J., Yoshida, N., Reiter, J. F., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.025 · Cited by 363
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Anczuków, O., & Krainer, A. R. (2016) · RNA · doi:10.1261/rna.057919.116 · Cited by 304
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Duan, W., Zhang, Y., Hou, Z., Huang, C. L., Zhu, H., Zhang, C., & Yin, Q. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9122-5 · Cited by 312
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Lee, J.-A., Damianov, A., Lin, C.-H., Fontes, M., Parikshak, N. N., Anderson, E. S., Geschwind, D. H., Black, D. L., & Martin, K. C. (2016) · Neuron · doi:10.1016/j.neuron.2015.11.025 · Cited by 232
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Fogel, B. L., Wexler, E., Wahnich, A., Friedrich, T., Vijayendran, C., Gao, F., Parikshak, N., Konopka, G., & Geschwind, D. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds240 · Cited by 216
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Chronic cocaine-regulated epigenomic changes in mouse nucleus accumbens
Feng, J., Wilkinson, M., Liu, X., Purushothaman, I., Ferguson, D., Vialou, V., Maze, I., Shao, N., Kennedy, P., Koo, J., et al. (2014) · Genome Biology · doi:10.1186/gb-2014-15-4-r65 · Cited by 198
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Ahmetov, I. I., Egorova, E. S., Gabdrakhmanova, L. J., & Fedotovskaya, O. N. (2016) · Medicine and sport science/Medicine and sport · doi:10.1159/000445240 · Cited by 183
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Darnell, R. B. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062912-114322 · Cited by 181
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Fisher, S. A. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00111.2010 · Cited by 180
Bräutigam, C., Rago, L., Rolke, A., Waldmeier, L., Christofori, G., & Winter, J. (2013) · Oncogene · doi:10.1038/onc.2013.50 · Cited by 175
Developmental regulation of RNA processing by Rbfox proteins
Conboy, J. G. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1398 · Cited by 133
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Jangi, M., Boutz, P. L., Paul, P., & Sharp, P. A. (2014) · Genes & Development · doi:10.1101/gad.235770.113 · Cited by 136
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Jacko, M., Weyn‐Vanhentenryck, S. M., Smerdon, J. W., Yan, R., Feng, H., Williams, D. J., Pai, J. A., Xu, K., Wichterle, H., & Zhang, C. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.020 · Cited by 131
Dysregulation of mRNA Localization and Translation in Genetic Disease
Wang, E. T., Taliaferro, J. M., Lee, J.-A., Sudhakaran, I. P., Rossoll, W., Groß, C., Moss, K. R., & Bassell, G. J. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2352-16.2016 · Cited by 114
Rbfox1 Regulates Synaptic Transmission through the Inhibitory Neuron-Specific vSNARE Vamp1
Vuong, C. K., Wei, W., Lee, J.-A., Lin, C.-H., Damianov, A., de la Torre-Ubieta, L., Halabi, R., Otis, K. O., Martin, K. C., O’Dell, T. J., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.03.008 · Cited by 102
Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2
Sun, S., Zhang, Z., Fregoso, O. I., & Krainer, A. R. (2011) · RNA · doi:10.1261/rna.030486.111 · Cited by 105
Alternative splicing of the cell fate determinant Numb in hepatocellular carcinoma
Lu, Y., Xu, W., Ji, J., Feng, D., Sourbier, C., Yang, Y., Qu, J., Zeng, Z., Wang, C., Chang, X., et al. (2015) · Hepatology · doi:10.1002/hep.27923 · Cited by 101
Dredge, B. K., & Jensen, K. B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021585 · Cited by 101
Microexons: discovery, regulation, and function
Ustianenko, D., Weyn‐Vanhentenryck, S. M., & Zhang, C. (2017) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1418 · Cited by 104
Inference of transcriptional regulation in cancers
Jiang, P., Freedman, M. L., Liu, J. S., & Liu, X. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424272112 · Cited by 93
Orchestration of Neurodevelopmental Programs by RBFOX1
Bill, B. R., Lowe, J. K., DyBuncio, C. T., & Fogel, B. L. (2013) · International Review of Neurobiology · doi:10.1016/b978-0-12-418700-9.00008-3 · Cited by 94
Wei, C., Qiu, J., Zhou, Y., Xue, Y., Hu, J., Ouyang, K., Banerjee, I., Zhang, C., Chen, B., Li, H., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.013 · Cited by 95
Dou, X., Xiao, Y., Shen, C., Wang, K., Wu, T., Liu, C., Li, Y., Yu, X., Liu, J., Dai, Q., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01213-w · Cited by 100
Diversification of the muscle proteome through alternative splicing
Nakka, K. K., Ghigna, C., Gabellini, D., & Dilworth, F. J. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0152-3 · Cited by 97
RBFox2 Binds Nascent RNA to Globally Regulate Polycomb Complex 2 Targeting in Mammalian Genomes
Wei, C., Xiao, R., Chen, L., Cui, H., Zhou, Y., Xue, Y., Hu, J., Zhou, B., Tsutsui, T., Qiu, J., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.013 · Cited by 91
Repression of Pumilio Protein Expression by Rbfox1 Promotes Germ Cell Differentiation
Carreira-Rosario, A., Bhargava, V., Hillebrand, J., Kollipara, R. K., Ramaswami, M., & Buszczak, M. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.02.010 · Cited by 89
Satellite-like cells contribute to pax7-dependent skeletal muscle repair in adult zebrafish
Berberoglu, M. A., Gallagher, T. L., Morrow, Z. T., Talbot, J. C., Hromowyk, K. J., Tenente, I. M., Langenau, D. M., & Amacher, S. L. (2017) · Developmental Biology · doi:10.1016/j.ydbio.2017.03.004 · Cited by 85
Ahmetov, I. I., Kulemin, N. A., Викторович, П. Д., Naumov, V., Akimov, E. B., Bravyy, Y. R., Egorova, E. S., Galeeva, A. R., Generozov, E. V., Kostryukova, E., et al. (2014) · Biology of Sport · doi:10.5604/20831862.1124568 · Cited by 82
RNA ‐binding proteins, neural development and the addictions
Bryant, C. D., & Yazdani, N. (2015) · Genes Brain & Behavior · doi:10.1111/gbb.12273 · Cited by 82
RBFox2 Binds Nascent RNA to Globally Regulate Polycomb Complex 2 Targeting in Mammalian Genomes
Wei, C., Xiao, R., Chen, L., Cui, H., Zhou, Y., Xue, Y., Hu, J., Zhou, B., Tsutsui, T., Qiu, J., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.003 · Cited by 81
Park, J. Y., Li, W., Zheng, D., Zhai, P., Zhao, Y., Matsuda, T., Vatner, S. F., Sadoshima, J., & Tian, B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022391 · Cited by 79
Shumay, E., Fowler, J. S., & Volkow, N. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011067 · Cited by 80
Janakiraman, H., House, R. P., Gangaraju, V. K., Diehl, J. A., Howe, P. H., & Palanisamy, V. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0547 · Cited by 74
Kuroyanagi, H., Ohno, G., Sakane, H., Maruoka, H., & Hagiwara, M. (2010) · Nature Protocols · doi:10.1038/nprot.2010.107 · Cited by 75
Self-citationRNA binding proteins in the regulation of heart development
Blech-Hermoni, Y. N., & Ladd, A. N. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.08.008 · Cited by 72
Chen, Y., Zubović, L., Yang, F., Godin, K. S., Pavelitz, T., Castellanos, J., Macchi, P., & Varani, G. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw177 · Cited by 66
RNA‐binding proteins in neurodegenerative disease: TDP‐43 and beyond
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Elorza, A., Márquez, Y., Cabrera, J. R., Sanchez‐Trincado, J. L., Santos‐Galindo, M., Hernández, I. H., Picó, S., Díaz‐Hernandéz, J. I., García‐Escudero, R., Irimia, M., et al. (2021) · Brain · doi:10.1093/brain/awab087 · Cited by 64
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Llorian, M., & Smith, C. W. J. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.03.006 · Cited by 59
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Begg, B. E., Jens, M., Wang, P. Y., Minor, C. M., & Burge, C. B. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0475-8 · Cited by 60
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Runfola, V., Sebastian, S., Dilworth, F. J., & Gabellini, D. (2015) · Journal of Cell Science · doi:10.1242/jcs.161059 · Cited by 54
Maurin, M. M., Ranjouri, M., Megino‐Luque, C., Newberg, J. Y., Du, D., Martin, K., Miner, R. E., Prater, M. S., Wee, D. K. B., Centeno, B. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-44126-w · Cited by 53
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Hu, J., Gao, C., Wei, C., Xue, Y., Shao, C., Hao, Y., Gou, L., Zhou, Y., Zhang, J., Ren, S. V., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1822176116 · Cited by 50
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O'Brien, J. E., Drews, V. L., Jones, J. M., Dugas, J. C., Barres, B. A., & Meisler, M. H. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.10.005 · Cited by 49
Stress Granules Contain Rbfox2 with Cell Cycle-related mRNAs
Park, C., Choi, S., Kim, Y.-E., Lee, S., Park, S.-H., Adelstein, R. S., Kawamoto, S., & Kim, K. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-11651-w · Cited by 49
Kuroyanagi, H., Watanabe, Y., & Hagiwara, M. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003337 · Cited by 46
Self-citationOhno, G., Ono, K., Togo, M., Watanabe, Y., Ono, S., Hagiwara, M., & Kuroyanagi, H. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002991 · Cited by 45
Self-citationThe transcription factor ERG recruits CCR4–NOT to control mRNA decay and mitotic progression
Rambout, X., Detiffe, C., Bruyr, J., Mariavelle, E., Cherkaoui, M., Brohée, S., Demoitié, P., Lebrun, M., Soin, R., Lesage, B., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3243 · Cited by 48
The function of spliceosome components in open mitosis
Hofmann, J. C., Husedzinovic, A., & Gruß, O. J. (2010) · Nucleus · doi:10.4161/nucl.1.6.13328 · Cited by 44
Maxeiner, S., Glassmann, A., Kao, H., & Schilling, K. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1159-9 · Cited by 45
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Zaharieva, E. E., Chipman, J. K., & Soller, M. (2012) · Toxicology · doi:10.1016/j.tox.2012.01.014 · Cited by 46
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Fisher, E., & Feng, J. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1728 · Cited by 45
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Chen, Y., Yang, F., Zubović, L., Pavelitz, T., Yang, W. J., Godin, K. S., Walker, M. J. P., Zheng, S., Macchi, P., & Varani, G. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2128 · Cited by 42
Zhou, Y., Fan, J., Zhu, H., Li, J., Fan, W., Kapoor, I., Wang, Y., Wang, Y., Zhu, G., & Wang, J. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.09301 · Cited by 41
Cibi, D. M., Mia, M. M., Shekeran, S. G., Yun, L. S., Sandireddy, R., Gupta, P. S., Hota, M., Sun, L., Ghosh, S., & Singh, M. K. (2019) · eLife · doi:10.7554/elife.45418 · Cited by 46
Pistoni, M., Shiue, L., Cline, M., Bortolanza, S., Neguembor, M. V., Xynos, A., Ares, M., & Gabellini, D. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003186 · Cited by 40
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Rajaram, M., Zhang, J., Wang, T., Li, J., Kuscu, C., Qi, H., Kato, M., Grubor, V. D., Weil, R. J., Helland, Å., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066264 · Cited by 45
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Ma, L., Hanson, R. L., Traurig, M. T., Muller, Y. L., Kaur, B. P., Perez, J. M., Meyre, D., Fu, M., Körner, A., Franks, P. W., et al. (2010) · Diabetes · doi:10.2337/db09-1604 · Cited by 41
Parallels between neuron and lens fiber cell structure and molecular regulatory networks
Frederikse, P. H., Kasinathan, C., & Kleiman, N. J. (2012) · Developmental Biology · doi:10.1016/j.ydbio.2012.05.022 · Cited by 38
Jiang, P., Singh, M., & Coller, H. A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003075 · Cited by 38
Li, P., Yu, Z., He, L., Zhou, D., Xie, S., Hou, H., & Geng, X. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.05.087 · Cited by 36
Alternative mRNA Splicing in the Pathogenesis of Obesity
Wong, C., Xu, L., & Yau, M. Y. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020632 · Cited by 34
RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing
Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., et al. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2870 · Cited by 33
Self-citationLucas, C. G., Calvez, M., Babu, R., & Brown, A. M. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.10.037 · Cited by 38
Shen, F., Xu, X. M., Yu, Z., Li, H., Shen, H., Li, X., Shen, M., & Chen, G. (2020) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20916860 · Cited by 33
Zubović, L., Baralle, M., & Baralle, F. E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks249 · Cited by 30
RetractedNlend, R. N., Meyer, K., & Schümperli, D. (2010) · RNA Biology · doi:10.4161/rna.7.4.12206 · Cited by 30
A widespread length-dependent splicing dysregulation in cancer
Zhang, S., Mao, M., Lv, Y., Yang, Y., He, W., Song, Y., Wang, Y., Yang, Y., Abo, M. A., Freedman, J. A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn9232 · Cited by 26
RNA splicing regulated by RBFOX1 is essential for cardiac function in zebrafish
Frese, K., Meder, B., Keller, A., Just, S., Haas, J., Vogel, B., Fischer, S., Backes, C., Matzas, M., Köhler, D., et al. (2015) · Journal of Cell Science · doi:10.1242/jcs.166850 · Cited by 27
RNA and neuronal function: the importance of post-transcriptional regulation
Bhat, V. D., Jayaraj, J., & Babu, K. (2022) · Oxford Open Neuroscience · doi:10.1093/oons/kvac011 · Cited by 26
RBFOX2 protein domains and cellular activities
Arya, A. D., Wilson, D. I., Baralle, D., & Raponi, M. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140050 · Cited by 26
Conserved functions of RNA-binding proteins in muscle
Nikonova, E. V., Kao, S.-Y., Ravichandran, K., Wittner, A., & Spletter, M. L. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.02.008 · Cited by 24
Parra, M., Gee, S. L., Mohandas, N., & Conboy, J. G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158154 · Cited by 25
Protein kinase WNK3 regulates the neuronal splicing factor Fox-1
Lee, A.-Y., Chen, W., Stippec, S., Self, J., Yang, F., Ding, X., Chen, S., Juang, Y.-C. A., & Cobb, M. H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215406109 · Cited by 28
Analysis of PI3K pathway components in human cancers
DARAGMEH, J., Barriah, W., Saad, B., & Zaid, H. (2016) · Oncology Letters · doi:10.3892/ol.2016.4309 · Cited by 25
Tissue-Specific Alternative Splicing of Tak1 Is Conserved in Deuterostomes
Venables, J. P., Vignal, E., Baghdiguian, S., Fort, P., & Tazi, J. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr193 · Cited by 25
Amrane, S., Rébora, K., Zniber, I., Dupuy, D., & Mackereth, C. D. (2014) · Nature Communications · doi:10.1038/ncomms5595 · Cited by 23
Su, W., Lv, M., Wang, D., He, Y., Han, H., Zhang, Y., Zhang, X., Lv, S., & Yao, L. (2024) · Mediators of Inflammation · doi:10.1155/2024/7459054 · Cited by 22
RNA-Binding Proteins in Heart Development
Giudice, J., & Cooper, T. A. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-1221-6_11 · Cited by 23
RNA-binding proteins regulating the CD44 alternative splicing
Maltseva, D. V., & Tonevitsky, A. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1326148 · Cited by 23
Hagen, E. M., Sicko, R. J., Kay, D. M., Rigler, S. L., Dimopoulos, A., Ahmad, S., Doleman, M. H., Fan, R., Romitti, P. A., Browne, M. L., et al. (2016) · Human Genetics · doi:10.1007/s00439-016-1727-x · Cited by 21
Chen, P.-F., Hsiao, J. S., Sirois, C. L., & Chamberlain, S. J. (2016) · Scientific Reports · doi:10.1038/srep25368 · Cited by 21
The Role of Genetic Polymorphisms in Diabetic Retinopathy: Narrative Review
Sienkiewicz‐Szłapka, E., Fiedorowicz, E., Król-Grzymała, A., Kordulewska, N. K., Rozmus, D., Cieślińska, A., & Grzybowski, A. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115865 · Cited by 20
Improved discovery of RNA-binding protein binding sites in eCLIP data using DEWSeq
Schwarzl, T., Sahadevan, S., Lang, B., Miladi, M., Backofen, R., Huber, W. K., Hentze, M. W., & Tartaglia, G. G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad998 · Cited by 21
MEF2C exon α: Role in gene activation and differentiation
Infantino, V., Convertini, P., Menga, A., & Iacobazzi, V. (2013) · Gene · doi:10.1016/j.gene.2013.08.044 · Cited by 19
Wen, J., Chiba, A., & Cai, X. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq679 · Cited by 19
Kim, Y., Kim, J. O., Park, K.-S., Won, M., Kim, K. E., & Kim, K. K. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0150 · Cited by 20
Wang, J., Li, G., Yu, D., Wong, Y. P., Yong, T. F., Liang, M. C., Liao, P. H., Foo, R., Hoppe, U. C., & Soong, T. W. (2017) · Channels · doi:10.1080/19336950.2017.1381805 · Cited by 19
The combinatorial control of alternative splicing in C. elegans
Tan, J. H., & Fraser, A. G. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1007033 · Cited by 18
Bitel, C. L., Nathan, R. S., Wong, P., Kuppasani, S., Matsushita, M., Kanazawa, H., & Frederikse, P. H. (2010) · Current Eye Research · doi:10.3109/02713683.2010.500114 · Cited by 18
Hakim, N. H. A., Majlis, B. Y., Suzuki, H., & Tsukahara, T. (2016) · BioScience Trends · doi:10.5582/bst.2016.01169 · Cited by 18
Metadata
- Authors
- Kuroyanagi, H.
- Affiliations
- Tokyo Medical and Dental University (JP)
- Corresponding author
- Kuroyanagi, Hidehito
- ORCID
- Kuroyanagi, Hidehito
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2009-08-18
- Volume
- 66
- Issue
- 24
- Pages
- 3895-3907
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC2777236
- OpenAlex
- W2057774013
- Cited by
- 187
- References
- 78
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 10 · 2022: 13 · 2021: 7 · 2020: 9 · 2019: 9 · 2018: 12 · 2017: 11 · 2016: 23 · 2015: 10 · 2014: 10 · 2013: 17 · 2012: 11
- FWCI
- 0.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Cellular and Molecular Life Sciences (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Tokyo Medical and Dental University
- Japan Society for the Promotion of Science
- 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
- RNA-binding proteins, alternative splicing, intronic splicing enhancer, muscle, heart, brain, splicing regulators, splicing regulatory network, vertebrate genomes
- MeSH terms
- RNA Splicing Factors, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Humans, Molecular Sequence Data, RNA-Binding Proteins, Spliceosomes, Sequence Homology, Amino Acid, Alternative Splicing
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