The splicing factor SRSF3 is functionally connected to the nuclear RNA exosome for intronless mRNA decay
Open accessAbstract
The RNA exosome fulfills important functions in the processing and degradation of numerous RNAs species. However, the mechanisms of recruitment to its various nuclear substrates are poorly understood. Using Epstein-Barr virus mRNAs as a model, we have discovered a novel function for the splicing factor SRSF3 in the quality control of nuclear mRNAs. We have found that viral mRNAs generated from intronless genes are particularly unstable due to their degradation by the nuclear RNA exosome. This effect is counteracted by the viral RNA-binding protein EB2 which stabilizes these mRNAs in the nucleus and stimulates both their export to the cytoplasm and their translation. In the absence of EB2, SRSF3 participates in the destabilization of these viral RNAs by interacting with both the RNA exosome and its adaptor complex NEXT. Taken together, our results provide direct evidence for a connection between the splicing machinery and mRNA decay mediated by the RNA exosome. Our results suggest that SRSF3 aids the nuclear RNA exosome and the NEXT complex in the recognition and degradation of certain mRNAs.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The RNA exosome has specialized functions in RNA splicing and regulation of AU-rich element (ARE)-containing transcripts.
“In addition to RNA turnover, the RNA exosome has specialized functions in RNA splicing and the regulation of AU-rich element (ARE)-containing transcripts44–47.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [44]
The Discussion (page not available in our copy) reports a connection between splicing factors and recruitment of the nuclear RNA exosome for mRNA degradation. It does not establish that the exosome regulates splicing itself, and no passage found in searches for “AU-rich” or “ARE-containing transcripts” addresses regulation of those transcripts. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Rickinson, A. B. (2002) · PubMed · doi:10.1016/s0168-1702(01)00436-1 · Cited by 2,182 · see citing works
The highways and byways of mRNA decay
Garneau, N. L., Wilusz, J., & Wilusz, C. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2104 · Cited by 1,294 · see citing works
RNA Degradation by the Exosome Is Promoted by a Nuclear Polyadenylation Complex
LaCava, J., Houseley, J. M., Saveanu, C., Petfalski, E., Thompson, E., Jacquier, A., & Tollervey, D. W. (2005) · Cell · doi:10.1016/j.cell.2005.04.029 · Cited by 870 · see citing works
Wyers, F., Rougemaille, M., Badis, G., Rousselle, J.-C., Dufour, M., Boulay, J., Regnault, B., Devaux, F., Namane, A., Séraphin, B., et al. (2005) · Cell · doi:10.1016/j.cell.2005.04.030 · Cited by 843 · see citing works
Hir, H. L., Gatfield, D., Izaurralde, E., & Moore, M. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4987 · Cited by 842 · see citing works
EBV Persistence in Memory B Cells In Vivo
Babcock, G. J., Decker, L. L., Volk, M. S., & Thorley‐Lawson, D. A. (1998) · Immunity · doi:10.1016/s1074-7613(00)80622-6 · Cited by 829 · see citing works
A New Yeast Poly(A) Polymerase Complex Involved in RNA Quality Control
Vaňáčová, Š., Wolf, J., Martin, G., Blank, D., Dettwiler, S., Friedlein, A., Langen, H., Keith, G., & Keller, W. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030189 · Cited by 567 · see citing works
Reconstitution, Activities, and Structure of the Eukaryotic RNA Exosome
Liu, Q., Greimann, J. C., & Lima, C. D. (2006) · Cell · doi:10.1016/j.cell.2006.10.037 · Cited by 544 · see citing works
Laichalk, L. L., & Thorley‐Lawson, D. A. (2004) · Journal of Virology · doi:10.1128/jvi.79.2.1296-1307.2005 · Cited by 538 · see citing works
Cho, E., Takagi, T., Moore, C. R., & Buratowski, S. (1997) · Genes & Development · doi:10.1101/gad.11.24.3319 · Cited by 478 · see citing works
Interaction Profiling Identifies the Human Nuclear Exosome Targeting Complex
Lubas, M., Christensen, M. S., Kristiansen, M. S., Domanski, M., Falkenby, L. G., Lykke‐Andersen, S., Andersen, J., Dziembowski, A., & Jensen, T. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.028 · Cited by 422 · see citing works
Splicing Factors SRp20 and 9G8 Promote the Nucleocytoplasmic Export of mRNA
Huang, Y., & STEITZ, J. A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00233-7 · Cited by 396 · see citing works
The Clothes Make the mRNA: Past and Present Trends in mRNP Fashion
Singh, G., Pratt, G. A., Yeo, G. W.-M., & Moore, M. J. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-080111-092106 · Cited by 387 · see citing works
How cells get the message: dynamic assembly and function of mRNA–protein complexes
Müller-McNicoll, M., & Neugebauer, K. M. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3434 · Cited by 386 · see citing works
Splicing is required for rapid and efficient mRNA export in metazoans
Luo, M., & Reed, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14937 · Cited by 379 · see citing works
Identification of a Regulated Pathway for Nuclear Pre-mRNA Turnover
Bousquet‐Antonelli, C., Presutti, C., & Tollervey, D. W. (2000) · Cell · doi:10.1016/s0092-8674(00)00065-9 · Cited by 377 · see citing works
Endonucleolytic RNA cleavage by a eukaryotic exosome
Lebreton, A., Tomecki, R., Dziembowski, A., & Séraphin, B. (2008) · Nature · doi:10.1038/nature07480 · Cited by 335 · see citing works
Basu, U., Meng, F., Keim, C., Grinstein, V., Pefanis, E., Eccleston, J., Zhang, T., Myers, D. R., Wasserman, C. R., Wesemann, D. R., et al. (2011) · Cell · doi:10.1016/j.cell.2011.01.001 · Cited by 315 · see citing works
Noisy Splicing Drives mRNA Isoform Diversity in Human Cells
Pickrell, J. K., Pai, A. A., Gilad, Y., & Pritchard, J. K. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001236 · Cited by 311 · see citing works
Identification of a Nuclear Exosome Decay Pathway for Processed Transcripts
Meola, N., Domanski, M., Karadoulama, E., Chen, Y., Gentil, C., Pultz, D., Vitting-Seerup, K., Lykke-Andersen, S., Andersen, J. S., Sandelin, A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.025 · Cited by 290 · see citing works
Görnemann, J., Kotovic, K. M., Hujer, K., & Neugebauer, K. M. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.007 · Cited by 285 · see citing works
Nuclear Retention of mRNA in Mammalian Tissues
Bahar Halpern, K., Caspi, I., Lemze, D., Levy, M., Landen, S., Elinav, E., Ulitsky, I., & Itzkovitz, S. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.036 · Cited by 258 · see citing works
Interactions between mRNA Export Commitment, 3′-End Quality Control, and Nuclear Degradation
Libri, D., Dower, K., Boulay, J., Thomsen, R., Rosbash, M., & Jensen, T. H. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.23.8254-8266.2002 · Cited by 252 · see citing works
The human cap-binding complex is functionally connected to the nuclear RNA exosome
Andersen, P. R., Domanski, M., Kristiansen, M. S., Storvall, H., Ntini, E., Verheggen, C., Schein, A., Bunkenborg, J., Poser, I., Hallais, M., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2703 · Cited by 229 · see citing works
Origins and activities of the eukaryotic exosome
Lykke‐Andersen, S., Brodersen, D. E., & Jensen, T. H. (2009) · Journal of Cell Science · doi:10.1242/jcs.047399 · Cited by 169 · see citing works
mRNA export and the TREX complex
Katahira, J. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.12.001 · Cited by 162 · see citing works
CBC–ARS2 stimulates 3′-end maturation of multiple RNA families and favors cap-proximal processing
Hallais, M., Pontvianne, F., Andersen, P. R., Clerici, M., Lener, D., Benbahouche, N. E. H., Gostan, T., Vandermoere, F., Robert, M.-C., Cusack, S., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2720 · Cited by 159 · see citing works
Self-citationRrp47p Is an Exosome-Associated Protein Required for the 3′ Processing of Stable RNAs
Mitchell, P., Petfalski, E., Houalla, R., Podtelejnikov, A. V., Mann, M., & Tollervey, D. W. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6982-6992.2003 · Cited by 159 · see citing works
Process or perish: quality control in mRNA biogenesis
Fasken, M. B., & Corbett, A. H. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb945 · Cited by 135 · see citing works
The Human Nuclear Poly(A)-Binding Protein Promotes RNA Hyperadenylation and Decay
Bresson, S. M., & Conrad, N. K. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003893 · Cited by 128 · see citing works
Gruffat, H., Manet, É., & Sergeant, A. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf031 · Cited by 114 · see citing works
Self-citationLemay, J.-F., D'Amours, A., Lemieux, C., Lackner, D. H., St-Sauveur, V. G., Bähler, J., & Bachand, F. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.019 · Cited by 112 · see citing works
The Many Roles of the Highly Interactive HSV Protein ICP27, A Key Regulator of Infection
Sandri-Goldin, R. M. (2011) · Future Microbiology · doi:10.2217/fmb.11.119 · Cited by 111 · see citing works
Buisson, M., Manet, É., Trescol-Biémont, M.-C., Gruffat, H., Durand, B., & Sergeant, A. (1989) · Journal of Virology · doi:10.1128/jvi.63.12.5276-5284.1989 · Cited by 109 · see citing works
Self-citationFan, J., Kuai, B., Wu, G., Wu, X., Chi, B., Wang, L., Wang, K., Shi, Z., Zhang, H., Chen, S., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696139 · Cited by 102 · see citing works
Hiriart, E., Gruffat, H., Buisson, M., Mikaélian, I., Keppler, S. J., Méresse, P., Mercher, T., Bernard, O., Sergeant, A., & Manet, É. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501725200 · Cited by 102 · see citing works
Self-citationCo‐transcriptional degradation of aberrant pre‐mRNA by Xrn2
Davidson, L., Kerr, A. R. W., & West, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.101 · Cited by 93 · see citing works
Epstein-Barr Virus mRNA Export Factor EB2 Is Essential for Production of Infectious Virus
Gruffat, H., Batisse, J., Pich, D., Neuhierl, B., Manet, É., Hammerschmidt, W., & Sergeant, A. (2002) · Journal of Virology · doi:10.1128/jvi.76.19.9635-9644.2002 · Cited by 88 · see citing works
Self-citationHiriart, E., Farjot, G., Gruffat, H., Nguyen, M. V. C., Sergeant, A., & Manet, É. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208656200 · Cited by 84 · see citing works
Self-citationQuality control of mRNP in the nucleus
Schmid, M., & Jensen, T. H. (2008) · Chromosoma · doi:10.1007/s00412-008-0166-4 · Cited by 83 · see citing works
Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
Giacometti, S., Benbahouche, N. E. H., Domanski, M., Robert, M.-C., Meola, N., Lubas, M., Bukenborg, J., Andersen, J., Schulze, W. M., Verheggen, C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.046 · Cited by 83 · see citing works
Self-citationHan, Z., & Swaminathan, S. (2006) · Journal of Virology · doi:10.1128/jvi.02570-05 · Cited by 83 · see citing works
Sahin, B. B., Patel, D., & Conrad, N. K. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000799 · Cited by 79 · see citing works
Crossing the borders: Poly(A)-binding proteins working on both sides of the fence
Lemay, J., Lemieux, C., St-André, O., & Bachand, F. (2010) · RNA Biology · doi:10.4161/rna.7.3.11649 · Cited by 74 · see citing works
Fasken, M. B., Leung, S. W., Banerjee, A., Kodani, M., Chavez, R., Bowman, E. A., Purohit, M. K., Rubinson, M. E., Rubinson, E. H., & Corbett, A. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.271494 · Cited by 69 · see citing works
Hiriart, E., Bardouillet, L., Manet, É., Gruffat, H., Pénin, F., Montserret, R., Farjot, G., & Sergeant, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305925200 · Cited by 67 · see citing works
Self-citationVerma, D., Bais, S., Gaillard, M., & Swaminathan, S. (2010) · Journal of Virology · doi:10.1128/jvi.01359-10 · Cited by 63 · see citing works
Epstein-Barr Virus SM Protein Functions as an Alternative Splicing Factor
Verma, D., & Swaminathan, S. (2008) · Journal of Virology · doi:10.1128/jvi.00344-08 · Cited by 63 · see citing works
Rrp6, Rrp47 and Cofactors of the Nuclear Exosome
Butler, J. S., & Mitchell, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7841-7_8 · Cited by 62 · see citing works
Nicewonger, J. D., Suck, G., Bloch, D. B., & Swaminathan, S. (2004) · Journal of Virology · doi:10.1128/jvi.78.17.9412-9422.2004 · Cited by 62 · see citing works
Structure of the RBM7–ZCCHC8 core of the NEXT complex reveals connections to splicing factors
Falk, S., Finogenova, K., Melko, M., Benda, C., Lykke‐Andersen, S., Jensen, T. H., & Conti, E. (2016) · Nature Communications · doi:10.1038/ncomms13573 · Cited by 52 · see citing works
Comparison of the yeast and human nuclear exosome complexes
Sloan, K. E., Schneider, C., & Watkins, N. J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120061 · Cited by 46 · see citing works
Post‐transcriptional gene regulation by gamma herpesviruses
Swaminathan, S. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20465 · Cited by 43 · see citing works
Juillard, F., Hiriart, E., Sergeant, N., Vingtdeux, V., Drobecq, H., Sergeant, A., Manet, É., & Gruffat, H. (2009) · Journal of Virology · doi:10.1128/jvi.01276-09 · Cited by 43 · see citing works
Self-citationNuclear noncoding RNA surveillance: is the end in sight?
Wolin, S. L., Sim, S., & Chen, X. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.03.005 · Cited by 41 · see citing works
Nag, A., & STEITZ, J. A. (2012) · RNA Biology · doi:10.4161/rna.19431 · Cited by 40 · see citing works
Batisse, J., Manet, É., Middeldorp, J. M., Sergeant, A., & Gruffat, H. (2005) · Journal of Virology · doi:10.1128/jvi.79.22.14102-14111.2005 · Cited by 39 · see citing works
Self-citationJuillard, F., Bazot, Q., Mure, F., Tafforeau, L., Macri, C., Rabourdin‐Combe, C., Lotteau, V., Manet, É., & Gruffat, H. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks319 · Cited by 38 · see citing works
Self-citationQuality control of mRNP biogenesis: Networking at the transcription site
Eberle, A. B., & Visa, N. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.033 · Cited by 35 · see citing works
Ricci, E. P., Mure, F., Gruffat, H., Décimo, D., Medina‐Palazon, C., Ohlmann, T., & Manet, É. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp497 · Cited by 33 · see citing works
Self-citationBoyer, J. L., Swaminathan, S., & Silverstein, S. J. (2002) · Journal of Virology · doi:10.1128/jvi.76.18.9420-9433.2002 · Cited by 33 · see citing works
The RNA polymerase C-terminal domain
David, C. J., & Manley, J. L. (2011) · Transcription · doi:10.4161/trns.2.5.17272 · Cited by 25 · see citing works
Guo, T. B., Boros, L. G., Chan, K. C., Hikim, A. P. S., Hudson, A. P., Swerdloff, R. S., Mitchell, A. P., & Salameh, W. A. (2003) · Journal of Andrology · doi:10.1002/j.1939-4640.2003.tb02664.x · Cited by 23 · see citing works
Mure, F., Panthu, B., Zanella‐Cléon, I., Delolme, F., Manet, É., Ohlmann, T., & Gruffat, H. (2017) · Journal of Virology · doi:10.1128/jvi.01917-17 · Cited by 18 · see citing works
Self-citationHessing, M., van Schijndel, H. B., van Grunsven, W. M. J., Wolf, H. J., & Middeldorp, J. M. (1992) · Journal of Chromatography A · doi:10.1016/0021-9673(92)85479-d · Cited by 17 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [52]Mure F Epstein-Barr virus protein EB2 stimulates translation initiation of mRNAs through direct interactions with both PABP and eIF4G J. Virol. 2018 92 e01917 17 29142127 PMC5774873
Cited by
Sorted by citations
Insights into epigenetic patterns in mammalian early embryos
Xu, R., Li, C., Liu, X., & Gao, S. (2021) · Protein & Cell · doi:10.1007/s13238-020-00757-z · Cited by 216 · see citing works
Garland, W., Müller, I. I., Wu, M., Schmid, M., Imamura, K., Rib, L., Sandelin, A., Helin, K., & Jensen, T. H. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.004 · Cited by 93 · see citing works
SRSF3: Newly discovered functions and roles in human health and diseases
More, D. A., & Kumar, A. (2020) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2020.151099 · Cited by 58 · see citing works
Wagner, R. E., & Frye, M. (2021) · BioEssays · doi:10.1002/bies.202000242 · Cited by 50 · see citing works
Targeting RNA splicing modulation: new perspectives for anticancer strategy?
Lv, X., Sun, X., Gao, Y., Song, X., Hu, X., Gong, L., Li, H., He, M., & Wei, M. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03279-w · Cited by 52 · see citing works
Wu, Y., Liu, W., Chen, J., Liu, S., Wang, M., Yang, L., Chen, C., Qi, M., Xu, Y., Qiao, Z., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.055 · Cited by 51 · see citing works
Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation
Gockert, M., Schmid, M., Jakobsen, L., Jens, M., Andersen, J., & Jensen, T. H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac001 · Cited by 45 · see citing works
Alternative Splicing of ALS Genes: Misregulation and Potential Therapies
Perrone, B., Cognata, V. L., Sprovieri, T., Ungaro, C., Conforti, F. L., Andò, S., & Cavallaro, S. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00717-0 · Cited by 45 · see citing works
Non-canonical functions of spliceosome components in cancer progression
Ivanova, O. M., Anufrieva, K. S., Kazakova, A. N., Malyants, I. K., Shnaider, P. V., Lukina, M. M., & Shender, V. О. (2023) · Cell Death and Disease · doi:10.1038/s41419-022-05470-9 · Cited by 44 · see citing works
Exploring the multifunctionality of SR proteins
Slišković, I., Eich, H., & Müller-McNicoll, M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210325 · Cited by 40 · see citing works
Oncogenic SRSF3 in health and diseases
Jia, R., & Zheng, Z. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83368 · Cited by 29 · see citing works
Nuclear mRNA decay: regulatory networks that control gene expression
Rambout, X., & Maquat, L. E. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-024-00712-2 · Cited by 29 · see citing works
Roles of RNA-binding proteins in neurological disorders, COVID-19, and cancer
Sanya, D. R. A., Cava, C., & Onésime, D. (2022) · Human Cell · doi:10.1007/s13577-022-00843-w · Cited by 26 · see citing works
Ruiz, J. C., Hunter, O. V., & Conrad, N. K. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007596 · Cited by 23 · see citing works
Biological function and molecular mechanism of SRSF3 in cancer and beyond (Review)
Xiong, J., Chen, Y., Wang, W., & Sun, J. (2021) · Oncology Letters · doi:10.3892/ol.2021.13139 · Cited by 21 · see citing works
Zhao, L., Li, Y., Zhao, Y., Liu, Q., Lu, Y., & Ping, J. (2022) · Veterinary Microbiology · doi:10.1016/j.vetmic.2022.109343 · Cited by 16 · see citing works
Bazin, J., Elvira‐Matelot, E., Blein, T., Jauvion, V., Bouteiller, N., Cao, J., Crespi, M. D., & Vaucheret, H. (2023) · The Plant Cell · doi:10.1093/plcell/koad091 · Cited by 16 · see citing works
SRSF3 Depletion Leads to an Increase in SF3B4 Expression in SNU-368 HCC Cells
Lee, J., Seo, G., Hur, W., Yoon, S. K., Nam, S. W., & LEE, J.-H. (2020) · Anticancer Research · doi:10.21873/anticanres.14160 · Cited by 11 · see citing works
Querl, L., & Krebber, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910241 · Cited by 10 · see citing works
Homeobox B9 Promotes Colon Cancer Progression by Targeting SRSF3
Yuan, L., Cheng, F., Wu, Z., Li, X., & Shen, W. (2023) · Digestive Diseases and Sciences · doi:10.1007/s10620-023-07977-3 · Cited by 6 · see citing works
RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response
Birot, A., Kilchert, C., Kuś, K., Priest, E., Alwash, A. A., Castelló, A., Mohammed, S., & Vasiljeva, L. (2021) · Life Science Alliance · doi:10.26508/lsa.202101111 · Cited by 5 · see citing works
Circular RNA hsa_circ_0081343 modulates trophoblast autophagy through Rbm8a nuclear translocation
Zheng, L., Tang, R., Fang, J., Hu, H., Ahmad, F., Tang, Q., Liu, J., Zhong, M., & Li, J. (2024) · Placenta · doi:10.1016/j.placenta.2024.09.019 · Cited by 4 · see citing works
The RNA-binding protein SRSF3 controls epicardial formation by regulating splicing and proliferation
Lupu, I.-E., Bruche, S., Chakrabarti, A. M., McCracken, I. R., Dang, Q., Carsana, T., Val, S. D., Redpath, A. N., & Smart, N. (2026) · Development · doi:10.1242/dev.204918 · Cited by 4 · see citing works
Majerčiak, V., Alvarado-Hernandez, B., Ma, Y., Duduskar, S. N., Lobanov, A. V., Cam, M., & Zheng, Z. (2024) · mBio · doi:10.1128/mbio.03172-24 · Cited by 4 · see citing works
SRp20: A potential therapeutic target for human tumors
Wang, H., & Jiang, Y. (2021) · Pathology - Research and Practice · doi:10.1016/j.prp.2021.153444 · Cited by 4 · see citing works
RNA-interactome capture identifies SRSF3 as a key protein for herpesviral gene expression
Vogt, C., van Ham, M., Bhowmik, R., Argoetti, A., Depledge, D. P., Steinbrück, L., Götting, J., Henkel, C., Granados, A. C., Mandel‐Gutfreund, Y., et al. (2025) · PNAS Nexus · doi:10.1093/pnasnexus/pgaf225 · Cited by 2 · see citing works
Roles of the RNA-binding protein SRSF3 in development and cellular differentiation
Brooks, E. C., Griffin, C. W., & Fantauzzo, K. A. (2026) · Differentiation · doi:10.1016/j.diff.2026.100958 · Cited by 2 · see citing works
SRSF3 is a key regulator of epicardial formationPreprint
Lupu, I.-E., Bruche, S., Chakrabarti, A. M., McCracken, I. R., Carsana, T., Redpath, A. N., & Smart, N. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.25.470003 · Cited by 2 · see citing works
EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery
Wijeratne, H. R. S., Runnebohm, A. M., Barron, M. P., Hampton, A. J., Li, R., Peck Justice, S. A., Lenceski, S. H., Rooney, J. D., Smith-Kinnaman, W. R., Chang, G. S., et al. (2026) · doi:10.64898/2026.01.26.701775 · Cited by 1 · see citing works
Tang, S., Patel, A., Takeda, K., Peden, K., & Krause, P. R. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014146 · Cited by 1 · see citing works
Gruffat, H., Mure, F., & Manet, É. (2019) · médecine/sciences · doi:10.1051/medsci/2019015 · Cited by 1 · see citing works
Self-citationBazin, J., Elvira‐Matelot, E., Blein, T., Jauvion, V., Bouteiller, N., Cao, J., Crespi, M. D., & Vaucheret, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.10.503523 · Cited by 1 · see citing works
Zheng, L., Tang, R., Fang, J., Hu, H., Tang, Q., Liu, J., Zhong, M., & Li, J. (2023) · Research Square · doi:10.21203/rs.3.rs-2600975/v1
Hierarchical assembly and functional resilience of the mammalian RNA exosomePreprint
Navalayeu, T., Beer, N., Bebjaková, M., Kalis, R., Stejskal, K., Krššáková, G., Fasching, N., Herzog, V. A., Popitsch, N. P., Roitinger, E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.14.643291
ORF57/MTA in KSHV biology and pathogenesis: update from 2015
Zheng, Z.-M., & Majerciak, V. (2026) · Journal of Medical Virology · doi:10.1002/jmv.70979
Cellular assembly and functional resilience of the mammalian RNA exosome
Navalayeu, T., Beer, N., Bebjaková, M., Kalis, R., Hohmann, U., Stejskal, K., Krššáková, G., Fasching, N., Herzog, V. A., Popitsch, N. P., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00824-x
- Authors
- Mure, F., Corbin, A., Benbahouche, N. E. H., Bertrand, E., Manet, E., & Gruffat, H.
- Affiliations
- Lyon 1 Université (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Gruffat, Henri
- Venue
- Scientific Reports
- Published
- 2018-08-27
- Volume
- 8
- Issue
- 1
- Pages
- 12901-12901
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC6110769
- OpenAlex
- W2888005468
- Cited by
- 38
- References
- 65
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 3 · 2019: 5
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Aarhus Universitet
- University of Oxford
- Agence Nationale de la Recherche (ANR-11-LABX-0048)
- Institut National de la Santé et de la Recherche Médicale
- Radboud Universiteit
- Fondation ARC pour la Recherche sur le Cancer
- Ligue Contre le Cancer
- 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 › Nuclear Structure and Function
- Keywords
- SRSF3, RNA exosome, mRNA degradation, Epstein-Barr virus, splicing factors, mRNA stability, mRNA export, translation (biology), RNA-binding proteins, nuclear quality control
- MeSH terms
- Serine-Arginine Splicing Factors, Cell Nucleus, HeLa Cells, Humans, RNA Splicing, RNA, Messenger, Blotting, Western, RNA-Binding Proteins, RNA Stability, Immunoprecipitation, Exosomes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review