Regulation of mRNA stability by CCCH-type zinc-finger proteins in immune cells
Open accessAbstract
Current studies using knockout mice have revealed that some Cys–Cys–Cys–His (CCCH)-type zinc-finger proteins, namely tristetraprolin (TTP), Roquin and Regnase-1, play important roles in the immune system. These proteins are closely associated with the fate of their target RNAs in normal immune responses. However, the functions of many RNA-binding proteins have not been characterized precisely. To understand the molecular mechanisms of RNA metabolism in the immune system, investigation of TTP/Roquin/Regnase-1 might provide new knowledge. In this review, we will discuss the current understanding of these proteins in immune regulation and homeostasis and discuss RNA metabolism in the immune system.
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Regnase-1 degrades IL-6 mRNA, while Arid5a protects IL-6 mRNA from Regnase-1-mediated degradation.
“Regnase-1 degrades IL-6 mRNA (87), while Arid5a protects IL-6 mRNA from Regnase-1-mediated degradation (88).”
From IL-6 in inflammation, autoimmunity and cancer (2021) · cites this paper as [87]
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Bartel (2004) · doi:10.1016/s0092-8674(04)00045-5 · Cited by 34,714 · see citing works
Pathogen Recognition and Innate Immunity
Akira, S., Uematsu, S., & Takeuchi, O. (2006) · Cell · doi:10.1016/j.cell.2006.02.015 · Cited by 11,974 · see citing works
Self-citationPattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895 · see citing works
Self-citationApproaching the asymptote? Evolution and revolution in immunology.Preprint
Janeway, C. (1989) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1989.054.01.003 · Cited by 3,396 · see citing works
Caput, D., Beutler, B., Hartog, K., Thayer, R. M., Brown-Shimer, S. L., & Cerami, A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.6.1670 · Cited by 1,516 · see citing works
Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
Kedersha, N., Stoecklin, G., Ayodele, M. O., Yacono, P. W., Lykke‐Andersen, J., Fritzler, M. J., Scheuner, D. L., Kaufman, R. J., Golan, D. E., & Anderson, P. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502088 · Cited by 1,494 · see citing works
Impaired On/Off Regulation of TNF Biosynthesis in Mice Lacking TNF AU-Rich Elements
Kontoyiannis, D. L., Pasparakis, M., Pizarro, T. T., Cominelli, F., & Kollias, G. A. (1999) · Immunity · doi:10.1016/s1074-7613(00)80038-2 · Cited by 1,329 · see citing works
Feedback Inhibition of Macrophage Tumor Necrosis Factor-α Production by Tristetraprolin
Carballo, E., Lai, W. S., & Blackshear, P. J. (1998) · Science · doi:10.1126/science.281.5379.1001 · Cited by 1,162 · see citing works
Transcriptional control of the inflammatory response
Medzhitov, R., & Horng, T. (2009) · Nature Reviews Immunology · doi:10.1038/nri2634 · Cited by 1,035 · see citing works
Anti-inflammatory lipid mediators and insights into the resolution of inflammation
Lawrence, T., Willoughby, D. A., & Gilroy, D. W. (2002) · Nature reviews. Immunology · doi:10.1038/nri915 · Cited by 863 · see citing works
Vinuesa, C. G., Cook, M. C., Angelucci, C., Athanasopoulos, V., Rui, L., Hill, K. M., Yu, D., Domaschenz, H., Whittle, B., Lambe, T., et al. (2005) · Nature · doi:10.1038/nature03555 · Cited by 862 · see citing works
Involvement of MicroRNA in AU-Rich Element-Mediated mRNA Instability
Jing, Q., Huang, S., Guth, S., Zarubin, T., Motoyama, A. B., Chen, J., Padova, F. D., Lin, S., Gram, H., & Han, J. (2005) · Cell · doi:10.1016/j.cell.2004.12.038 · Cited by 849 · see citing works
Taylor, G. A., Carballo, E., Lee, D. M., Lai, W. S., Thompson, M. J., Patel, D. D., Schenkman, D. I., Gilkeson, G. S., Broxmeyer, H. E., Haynes, B. F., et al. (1996) · Immunity · doi:10.1016/s1074-7613(00)80411-2 · Cited by 765 · see citing works
Lai, W. S., Carballo, E., Strum, J. R., Kennington, E. A., Phillips, R. S., & Blackshear, P. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4311 · Cited by 730 · see citing works
Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay
Matsushita, K., Takeuchi, O., Standley, D. M., Kumagai, Y., Kawagoe, T., Miyake, T., Satoh, T., Kato, H., Tsujimura, T., Nakamura, H., et al. (2009) · Nature · doi:10.1038/nature07924 · Cited by 677 · see citing works
Self-citationMK2‐induced tristetraprolin:14‐3‐3 complexes prevent stress granule association and ARE‐mRNA decay
Stoecklin, G., Stubbs, T., Kedersha, N., Wax, S. D., Rigby, W. F. C., Blackwell, T. K., & Anderson, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600163 · Cited by 518 · see citing works
Carballo, E., Lai, W. S., & Blackshear, P. J. (2000) · Blood · doi:10.1182/blood.v95.6.1891 · Cited by 442 · see citing works
Roquin represses autoimmunity by limiting inducible T-cell co-stimulator messenger RNA
Yu, D., Tan, A. H., Hu, X., Athanasopoulos, V., Simpson, N., Silva, D. G., Hutloff, A., Giles, K. M., Leedman, P. J., Lam, K., et al. (2007) · Nature · doi:10.1038/nature06253 · Cited by 414 · see citing works
Mino, T., Murakawa, Y., Fukao, A., Vandenbon, A., Wessels, H.-H., Ori, D., Uehata, T., Tartey, S., Akira, S., Suzuki, Y., et al. (2015) · Cell · doi:10.1016/j.cell.2015.04.029 · Cited by 390 · see citing works
Interactions of CCCH Zinc Finger Proteins with mRNA
Lai, W. S., Carballo, E., Thorn, J. M., Kennington, E. A., & Blackshear, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001696200 · Cited by 378 · see citing works
Multiple modes of RNA recognition by zinc finger proteins
Hall, T. M. T. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.04.004 · Cited by 365 · see citing works
Post-transcriptional regulation of gene expression in innate immunity
Carpenter, S. B., Ricci, E. P., Mercier, B. C., Moore, M. J., & Fitzgerald, K. A. (2014) · Nature reviews. Immunology · doi:10.1038/nri3682 · Cited by 361 · see citing works
Malt1-Induced Cleavage of Regnase-1 in CD4+ Helper T Cells Regulates Immune Activation
Uehata, T., Iwasaki, H., Vandenbon, A., Matsushita, K., Hernández-Cuellar, E., Kuniyoshi, K., Satoh, T., Mino, T., Suzuki, Y., Standley, D. M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.034 · Cited by 349 · see citing works
Self-citationRNA-binding proteins in immune regulation: a focus on CCCH zinc finger proteins
Fu, M., & Blackshear, P. J. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.129 · Cited by 335 · see citing works
Roquin Promotes Constitutive mRNA Decay via a Conserved Class of Stem-Loop Recognition Motifs
Leppek, K., Schott, J., Reitter, S., Poetz, F., Hammond, M. C., & Stoecklin, G. (2013) · Cell · doi:10.1016/j.cell.2013.04.016 · Cited by 313 · see citing works
The regulation of genes and genomes by small RNAs
Ambros, V., & Chen, X. (2007) · Development · doi:10.1242/dev.002006 · Cited by 305 · see citing works
MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling
Liang, J., Saad, Y., Lei, T., Wang, J., Qi, D., Yang, Q., Kolattukudy, P. E., & Fu, M. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20092641 · Cited by 297 · see citing works
Iwasaki, H., Takeuchi, O., Teraguchi, S., Matsushita, K., Uehata, T., Kuniyoshi, K., Satoh, T., Saitoh, T., Matsushita, M., Standley, D. M., et al. (2011) · Nature Immunology · doi:10.1038/ni.2137 · Cited by 288 · see citing works
Self-citationJeltsch, K. M., Hu, D., Brenner, S., Zöller, J., Heinz, G. A., Nagel, D., Vogel, K. U., Rehage, N., Warth, S. C., Edelmann, S. L., et al. (2014) · Nature Immunology · doi:10.1038/ni.3008 · Cited by 274 · see citing works
Microbe sensing, positive feedback loops, and the pathogenesis of inflammatory diseases
Beutler, B. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00733.x · Cited by 261 · see citing works
Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein.
Lai, W. S., Stumpo, D. J., & Blackshear, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46259-4 · Cited by 244 · see citing works
TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elementsPreprint
Franks, T. M., & Lykke‐Andersen, J. (2007) · Genes & Development · doi:10.1101/gad.1494707 · Cited by 240 · see citing works
Genome-wide Analysis Identifies Interleukin-10 mRNA as Target of Tristetraprolin
Stoecklin, G., Tenenbaum, S. A., Mayo, T., Chittur, S. V., George, A. D., Baroni, T. E., Blackshear, P. J., & Anderson, P. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709657200 · Cited by 239 · see citing works
ARE‐mRNA degradation requires the 5′–3′ decay pathway
Stoecklin, G., Mayo, T., & Anderson, P. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400572 · Cited by 237 · see citing works
Tristetraprolin Down-Regulates IL-2 Gene Expression through AU-Rich Element-Mediated mRNA Decay
Ogilvie, R. L., Abelson, M., Hau, H. H., Louis, I. V.-S., Blackshear, P. J., & Bohjanen, P. R. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.2.953 · Cited by 204 · see citing works
Vogel, K. U., Edelmann, S. L., Jeltsch, K. M., Bertossi, A., Heger, K., Heinz, G. A., Zöller, J., Warth, S. C., Hoefig, K. P., Lohs, C., et al. (2013) · Immunity · doi:10.1016/j.immuni.2012.12.004 · Cited by 195 · see citing works
Clement, S. L., Scheckel, C., Stoecklin, G., & Lykke‐Andersen, J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00717-10 · Cited by 190 · see citing works
Glasmacher, E., Hoefig, K. P., Vogel, K. U., Rath, N., Du, L., Wolf, C., Kremmer, E., Wang, X., & Heissmeyer, V. (2010) · Nature Immunology · doi:10.1038/ni.1902 · Cited by 184 · see citing works
Post-transcriptional coordination of immunological responses by RNA-binding proteins
Kafasla, P., Skliris, A., & Kontoyiannis, D. L. (2014) · Nature Immunology · doi:10.1038/ni.2884 · Cited by 177 · see citing works
Smoak, K. A., & Cidlowski, J. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00679-06 · Cited by 175 · see citing works
The roles of TTP and BRF proteins in regulated mRNA decay
Sanduja, S., Blanco, F. F., & Dixon, D. A. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.28 · Cited by 164 · see citing works
Liang, J., Song, W., Tromp, G., Kolattukudy, P. E., & Fu, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002880 · Cited by 162 · see citing works
Linterman, M. A., Rigby, R. J., Wong, R. K., Silva, D., Withers, D. R., Anderson, G., Verma, N. K., Brink, R. A., Hutloff, A., Goodnow, C. C., et al. (2009) · Immunity · doi:10.1016/j.immuni.2008.12.015 · Cited by 152 · see citing works
Interferons limit inflammatory responses by induction of tristetraprolin
Sauer, I. M. (2006) · Blood · doi:10.1182/blood-2005-07-3058 · Cited by 151 · see citing works
Marchese, F. P., Aubareda, A., Tudor, C., Saklatvala, J., Clark, A. R., & Dean, J. L. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136473 · Cited by 149 · see citing works
Garg, A. V., Amatya, N., Chen, K., Cruz, J. A., Grover, P., Whibley, N., Conti, H. R., Hernandez Mir, G., Sirakova, T., Childs, E. C., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.07.021 · Cited by 145 · see citing works
Brooks, S. A., Connolly, J. E., & Rigby, W. F. C. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.12.7263 · Cited by 138 · see citing works
Pratama, A., Ramiscal, R. R., Silva, D. G., Das, S. K., Athanasopoulos, V., Fitch, J., Botelho, N. K., Chang, P.-P., Hu, X., Hogan, J. J., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.01.011 · Cited by 134 · see citing works
Stoecklin, G., Lu, M., Rattenbacher, B., & Moroni, C. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.10.3506-3515.2003 · Cited by 126 · see citing works
Tristetraprolin Mediates Interferon-γ mRNA Decay*
Ogilvie, R. L., Sternjohn, J., Rattenbacher, B., Vlasova, I., Williams, D. A., Hau, H. H., Blackshear, P., & Bohjanen, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901229200 · Cited by 118 · see citing works
Carballo, E., & Blackshear, P. J. (2001) · Blood · doi:10.1182/blood.v98.8.2389 · Cited by 117 · see citing works
Interleukin-6 as a Therapeutic Target in Candidate Inflammatory Diseases
Nishimoto, N. (2010) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2009.313 · Cited by 115 · see citing works
RC3H1 post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-κB pathway
Murakawa, Y., Hinz, M., Mothes, J., Schuetz, A., Uhl, M., Wyler, E., Yasuda, T., Mastrobuoni, G., Friedel, C. C., Dölken, L., et al. (2015) · Nature Communications · doi:10.1038/ncomms8367 · Cited by 112 · see citing works
Tristetraprolin Regulates CXCL1 (KC) mRNA Stability
Datta, S., Biswas, R., Novotny, M., Pavicic, P. G., Herjan, T., Mandal, P., & Hamilton, T. A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.4.2545 · Cited by 107 · see citing works
Loss of Roquin induces early death and immune deregulation but not autoimmunity
Bertossi, A., Aichinger, M., Sansonetti, P., Lech, M., Neff, F., Pál, M., Wunderlich, F. T., Anders, H., Klein, L., & Schmidt‐Supprian, M. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110578 · Cited by 107 · see citing works
Zhao, W., Liu, M., D’Silva, N. J., & Kirkwood, K. L. (2011) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2010.0154 · Cited by 106 · see citing works
Tristetraprolin Impairs NF-κB/p65 Nuclear Translocation
Schichl, Y. M., Resch, U., Hofer-Warbinek, R., & de Martin, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031237 · Cited by 92 · see citing works
RNA-destabilizing Factor Tristetraprolin Negatively Regulates NF-κB Signaling
Liang, J., Lei, T., Song, Y., Yanes, N., Qi, Y., & Fu, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024745 · Cited by 91 · see citing works
The ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs
Athanasopoulos, V., Barker, A. J., Yu, D., Tan, A. H., Srivastava, M., Contreras, N., Wang, J., Lam, K., Brown, S. H. J., Goodnow, C. C., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07628.x · Cited by 84 · see citing works
MCPIP1/Regnase-1 Restricts IL-17A- and IL-17C-Dependent Skin Inflammation
Monin, L., Gudjonsson, J. E., Childs, E. E., Amatya, N., Xing, X., Verma, A. H., Coleman, B. M., Garg, A. V., Killeen, M., Mathers, A., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601551 · Cited by 82 · see citing works
Chen, Y., Huang, Y.-L., Lin, N., Chen, H., Chiu, W.-C., & Chang, C. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.093 · Cited by 81 · see citing works
Roquin binds microRNA-146a and Argonaute2 to regulate microRNA homeostasis
Srivastava, M., Duan, G., Kershaw, N. J., Athanasopoulos, V., Yeo, J. H. C., Ose, T., Hu, D., Brown, S. H. J., Jergic, S., Patel, H. R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7253 · Cited by 69 · see citing works
Roquin-2 Promotes Ubiquitin-Mediated Degradation of ASK1 to Regulate Stress Responses
Maruyama, T., Araki, T., Kawarazaki, Y., Naguro, I., Heynen, S., Aza‐Blanc, P., Ronai, Z. A., Matsuzawa, A., & Ichijo, H. (2014) · Science Signaling · doi:10.1126/scisignal.2004822 · Cited by 68 · see citing works
Gaba, A., Grivennikov, S. I., Vu, M., Stumpo, D. J., Blackshear, P. J., & Karin, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201126 · Cited by 67 · see citing works
Attenuation of AMPK signaling by ROQUIN promotes T follicular helper cell formation
Ramiscal, R. R., Parish, I. A., Lee, R. S., Babon, J. J., Blagih, J., Pratama, A., Martin, J. L., Hawley, N., Cappello, J. Y., Cañete, P. F., et al. (2015) · eLife · doi:10.7554/elife.08698 · Cited by 57 · see citing works
Insulin Increases Tristetraprolin and Decreases VEGF Gene Expression in Mouse 3T3–L1 Adipocytes
Cao, H., Urban, J. F., & Anderson, R. A. (2008) · Obesity · doi:10.1038/oby.2008.65 · Cited by 52 · see citing works
Probert, L., Akassoglou, K., Alexopoulou, L., Douni, E. K., Haralambous, S., Hill, S., Kassiotis, G., Kontoyiannis, D. L., Pasparakis, M., Plows, D., et al. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.59.4.518 · Cited by 43 · see citing works
Transcriptional regulation of tristetraprolin by NF-κB signaling in LPS-stimulated macrophages
Chen, Y., Jiang, Y.-W., Su, Y.-L., Lee, S.-C., Chang, M.-S., & Chang, C. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-2302-8 · Cited by 33 · see citing works
Intrinsic mRNA stability helps compose the inflammatory symphony
Anderson, P. J. (2009) · Nature Immunology · doi:10.1038/ni0309-233 · Cited by 31 · see citing works
New Insights into the RNA-Binding and E3 Ubiquitin Ligase Activities of Roquins
Zhang, Q., Fan, L., Hou, F., Dong, A., Wang, Y., & Tong, Y. (2015) · Scientific Reports · doi:10.1038/srep15660 · Cited by 30 · see citing works
Suppression of IL-12 Production by Tristetraprolin through Blocking NF-кB Nuclear Translocation
Gu, L., Ning, H., Qian, X., Huang, Q. R., Hou, R., Almourani, R., Fu, M., Blackshear, P. J., & Liu, J. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300126 · Cited by 30 · see citing works
Murata, T., Morita, N., Hikita, K., Kiuchi, K., Kiuchi, K., & Kaneda, N. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.09.031 · Cited by 22 · see citing works
Emergence and evolution of Zfp36l3
Gingerich, T. J., Stumpo, D. J., Lai, W. S., Randall, T. A., Steppan, S. J., & Blackshear, P. J. (2015) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2015.10.016 · Cited by 15 · see citing works
Flagged first, then by citations
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Hirano, T. (2021) · International Immunology · doi:10.1093/intimm/dxaa078 · Cited by 1,453 · see citing works
“Regnase-1 degrades IL-6 mRNA (87), while Arid5a protects IL-6 mRNA from Regnase-1-mediated degradation (88).”
BackgroundDecoding Toll-like receptors: Recent insights and perspectives in innate immunity
Kawai, T., Ikegawa, M., Ori, D., & Akira, S. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.004 · Cited by 559 · see citing works
Self-citationPleiotropy and specificity: insights from the interleukin 6 family of cytokines
Murakami, M., Kamimura, D., & Hirano, T. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.027 · Cited by 533 · see citing works
RNA-binding proteins control gene expression and cell fate in the immune system
Turner, M., & Díaz‐Muñoz, M. D. (2017) · Nature Immunology · doi:10.1038/s41590-017-0028-4 · Cited by 200 · see citing works
Li, X., Han, M., Zhang, H., Liu, F., Pan, Y., Zhu, J., Liao, Z., Chen, X., & Zhang, B. (2022) · Biomarker Research · doi:10.1186/s40364-021-00345-1 · Cited by 149 · see citing works
Owen, A. M., Fults, J. B., Patil, N. K., Hernandez, A., & Bohannon, J. K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.622614 · Cited by 126 · see citing works
Control of RNA Stability in Immunity
Akira, S., & Maeda, K. (2021) · Annual Review of Immunology · doi:10.1146/annurev-immunol-101819-075147 · Cited by 83 · see citing works
Self-citationRakhra, G., & Rakhra, G. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06556-x · Cited by 72 · see citing works
A positive feedback loop controls Toxoplasma chronic differentiation
Licon, M. H., Giuliano, C. J., Chan, A. W., Chakladar, S., Eberhard, J. N., Shallberg, L. A., Chandrasekaran, S., Waldman, B. S., Koshy, A. A., Hunter, C. A., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01358-2 · Cited by 59 · see citing works
Role of CCCH-Type Zinc Finger Proteins in Human Adenovirus Infections
Hajikhezri, Z., Darweesh, M. F., Akusjärvi, G., & Punga, T. (2020) · Viruses · doi:10.3390/v12111322 · Cited by 55 · see citing works
RNA binding motif 47 (RBM47): emerging roles in vertebrate development, RNA editing and cancer
Shivalingappa, P. K. M., Sharma, V., Shiras, A., & Bapat, S. A. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04256-5 · Cited by 52 · see citing works
Wang, G., & Zheng, C. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa059 · Cited by 51 · see citing works
Regnase-1 controls colon epithelial regeneration via regulation of mTOR and purine metabolism
Nagahama, Y., Shimoda, M., Mao, G., Singh, S. K., Kozakai, Y., Sun, X., Motooka, D., Nakamura, S., Tanaka, H., Satoh, T., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809575115 · Cited by 49 · see citing works
Self-citationGuillemin, A., Kumar, A., Wencker, M., & Ricci, E. P. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.796012 · Cited by 44 · see citing works
Huang, M., Wang, Z., Yao, L., Zhang, L., Gou, X., Mo, H., Li, H., Hu, L., & Zhou, X. (2023) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2023.106794 · Cited by 44 · see citing works
Zinc finger proteins of Plasmodium falciparum
Ngwa, C. J., Farrukh, A., & Pradel, G. (2021) · Cellular Microbiology · doi:10.1111/cmi.13387 · Cited by 39 · see citing works
The tandem zinc finger RNA binding domain of members of the tristetraprolin protein family
Lai, W. S., Wells, M. L., Perera, L., & Blackshear, P. J. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1531 · Cited by 29 · see citing works
Lai, W. S., Stumpo, D. J., Wells, M. L., Gruzdev, A., Hicks, S. N., Nicholson, C. O., Yang, Z., Faccio, R., Webster, M. W., Passmore, L. A., et al. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00029-19 · Cited by 26 · see citing works
PIN and CCCH Zn-finger domains coordinate RNA targeting in ZC3H12 family endoribonucleases
Garg, A., Roske, Y., Yamada, S., Uehata, T., Takeuchi, O., & Heinemann, U. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab316 · Cited by 28 · see citing works
Extracellular mRNA transported to the nucleus exerts translation-independent function
Tomita, T., Kato, M., Mishima, T., Matsunaga, Y., Sanjo, H., Ito, K.-I., Minagawa, K., Matsui, T., Oikawa, H., Takahashi, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23969-1 · Cited by 25 · see citing works
Pi, B., Pan, J., Xiao, M., Hu, X., Zhang, L., Chen, M., Liu, B., Ruan, Y., & Huang, Y. (2021) · BMC Plant Biology · doi:10.1186/s12870-021-03340-8 · Cited by 25 · see citing works
Ok, K., Filipović, M. R., & Michel, S. L. J. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100402 · Cited by 23 · see citing works
Bioinorganic Chemistry of Zinc in Relation to the Immune System
Kepp, K. P. (2021) · ChemBioChem · doi:10.1002/cbic.202100554 · Cited by 21 · see citing works
Tants, J., Becker, L. M., McNicoll, F., Müller-McNicoll, M., & Schlundt, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac212 · Cited by 20 · see citing works
Cadmium Exchange with Zinc in the Non-Classical Zinc Finger Protein Tristetraprolin
Brandis, J. E. P., Zalesak‐Kravec, S., Kane, M. A., & Michel, S. L. J. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c03808 · Cited by 20 · see citing works
Overcoming the limitations of cytokines to improve cancer therapy
Trani, C. A. D., Cirella, A., Arrizabalaga, L., Fernández-Sendin, M., Bella, Á., Aranda, F., Melero, I., & Berraondo, P. (2022) · International review of cytology · doi:10.1016/bs.ircmb.2022.05.002 · Cited by 20 · see citing works
Miladi, M., Sokhoyan, E., Houwaart, T., Heyne, S., Costa, F., Grüning, B. A., & Backofen, R. (2019) · GigaScience · doi:10.1093/gigascience/giz150 · Cited by 18 · see citing works
Innate immune sensing of pathogens and its post-transcriptional regulations by RNA-binding proteins
Tse, K. M., & Takeuchi, O. (2023) · Archives of Pharmacal Research · doi:10.1007/s12272-023-01429-2 · Cited by 19 · see citing works
ZC3H4—a novel Cys-Cys-Cys-His-type zinc finger protein—is essential for early embryogenesis in mice†
Su, J., Miao, X., Archambault, D., Mager, J., & Cui, W. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa215 · Cited by 17 · see citing works
ZC3H11A loss of function enhances NF-κB signaling through defective IκBα protein expression
Darweesh, M. F., Younis, S., Hajikhezri, Z., Ali, A., Jin, C., Punga, T., Gupta, S., Essand, M., Andersson, L., & Akusjärvi, G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1002823 · Cited by 15 · see citing works
Wu, H., Lu, A., Yuan, J., Yu, Y., Lv, C., & Lu, J. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01994-5 · Cited by 14 · see citing works
Asadi, M. R., Talebi, M., Gharesouran, J., Sabaie, H., Jalaiei, A., Arsang‐Jang, S., Taheri, M. N., Sayad, A., & Rezazadeh, M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.933019 · Cited by 13 · see citing works
Chiu, H. C., Chiu, H.-P., Yu, H.-P., Lin, L.-H., Chen, Z.-P., Lin, Y., & Lin, R.-J. (2021) · Journal of Virology · doi:10.1128/jvi.01665-21 · Cited by 12 · see citing works
Unraveling the RNA Binding Properties of the Iron–Sulfur Zinc Finger Protein CPSF30
Pritts, J. D., Hursey, M. S., Michalek, J. L., Batelu, S., Stemmler, T. L., & Michel, S. L. J. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b01065 · Cited by 11 · see citing works
Clayer, E., Frank, D. O., Anderton, H., Zhang, S., Kueh, A. J., Heim, V. J., Nutt, S. L., Chopin, M., & Bouillet, P. (2022) · Immunology and Cell Biology · doi:10.1111/imcb.12521 · Cited by 10 · see citing works
Pritts, J. D., Oluyadi, A. A., Huang, W., Shimberg, G. D., Kane, M. A., Wilks, A., & Michel, S. L. J. (2021) · Biochemistry · doi:10.1021/acs.biochem.0c00940 · Cited by 9 · see citing works
The evolution and immunomodulatory role of Zc3h12 proteins in zebrafish (Danio rerio)
Yang, S., Xu, X., Zhang, A., Wang, Y., Ji, G., Sun, C., & Li, H. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124214 · Cited by 9 · see citing works
ZFP36 ring finger protein like 1 significantly suppresses human coronavirus OC43 replication
Momin, T., Villasenor, A., Singh, A., Darweesh, M. F., Singh, A. D., & Rajput, M. (2023) · PeerJ · doi:10.7717/peerj.14776 · Cited by 8 · see citing works
Synthetic short mRNA prevents metastasis via innate-adaptive immunity
Hayashi, H., Seki, S., Tomita, T., Kato, M., Ashihara, N., Chano, T., Sanjo, H., Kawade, M., Yan, C., Sakai, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57123-y · Cited by 6 · see citing works
Fattahi, F., Asadi, M., Abed, S., Kouchakali, G., Kazemi, M., Derakhshan, S. M., & Khaniani, M. S. (2024) · Metabolic Brain Disease · doi:10.1007/s11011-024-01431-7 · Cited by 5 · see citing works
Stoltzfus, A. T., Campbell, C. J., Worth, M. M., Hom, K., Stemmler, T. L., & Michel, S. L. J. (2022) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01980-1 · Cited by 5 · see citing works
ZFP36 Facilitates Senecavirus A (SVA) replication by inhibiting the production of type I interferon
Yin, M., Guan, L., Zhang, M., Li, X., & Qian, P. (2024) · Virus Research · doi:10.1016/j.virusres.2024.199498 · Cited by 4 · see citing works
Cysteine-rich zinc finger proteins and the nuclear factor kappa-B pathway
Stoltzfus, A. T., & Michel, S. L. J. (2024) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2024.1503390 · Cited by 4 · see citing works
Ward, S. K., Wadley, A. F., Tsai, C. (., Benke, P. J., Emrick, L., Fisher, K. S., Houck, K. M., Dai, H., Undiagnosed Diseases Network, Sacoto, M. J. G., et al. (2023) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.63399 · Cited by 4 · see citing works
CCCH-type zinc finger proteins are required for meiotic progression and RNA clearance in Arabidopsis
Xue, J., Bu, J.-H., Wang, X.-L., Shi, J.-Q., Sheng-Ze, W., Chen, X., Meng-Xiao, W., Lv, Y.-L., Peng, Y.-J., Yang, N., et al. (2026) · The Plant Cell · doi:10.1093/plcell/koag048 · Cited by 3 · see citing works
Breaking self‐regulation of Regnase‐1 promotes its own protein expression
Piboonprai, K., Millius, A., Shimoda, M., Tanaka, H., Akira, S., & Maeda, K. (2023) · Genes to Cells · doi:10.1111/gtc.13018 · Cited by 3 · see citing works
Self-citationThe Role of Ribonucleases in RNA Damage, Inactivation and Degradation
Hia, F., & Takeuchi, O. (2021) · Springer eBooks · doi:10.1007/978-3-030-76571-2_5 · Cited by 3 · see citing works
Hirano, M., Nochi, K., Matsugi, M., Furukawa, C., Takeda, H., Sakurai, Y., Kurosaki, Y., Sawasaki, T., Yasuda, J., Takahashi, H., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110545 · Cited by 2 · see citing works
Mirzaei, F., Jahromi, A. M., Molavi, H., Kabelitz, D., Kalantar, K., & Meri, S. (2025) · RNA Biology · doi:10.1080/15476286.2025.2581385 · Cited by 2 · see citing works
RNA-Binding Proteins in Dinoflagellates
Berdieva, M. A., Safonov, P., & Skarlato, S. O. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27010462 · Cited by 2 · see citing works
Mammalian Cis-Acting RNA Sequence Elements
Louis, I. V.-S., & Sagarsky, C. (2018) · InTech eBooks · doi:10.5772/intechopen.72124 · Cited by 2 · see citing works
Miladi, M., Sokhoyan, E., Houwaart, T., Heyne, S., Costa, F., Grüning, B., & Backofen, R. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/550335 · Cited by 2 · see citing works
Shen, C., Chen, Z., Jiang, J., Zhang, Y., Xu, W. M., Peng, R., Zuo, W., Jiang, Q., Fan, Y., Fang, X., et al. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1034567 · Cited by 1 · see citing works
Introduction: Dynamics of RNA Regulation in the Immune System Special Issue
Akira, S., & Maeda, K. (2017) · International Immunology · doi:10.1093/intimm/dxx028 · Cited by 1 · see citing works
Self-citationRNA-binding Protein ZC3H18 Enhances Cell Proliferation and Metastasis in Lung AdenocarcinomaPreprint
Ke, M., Chen, Y., Zeng, L., & Yang, S. (2023) · Research Square · doi:10.21203/rs.3.rs-2783463/v1
Production of stable and pure ZC3H11A – An extensively disordered RNA binding protein
Fekry, M. I., Stenberg, G., Dobritzsch, D., & Danielson, U. H. (2024) · Protein Expression and Purification · doi:10.1016/j.pep.2024.106542
Dou, Y., Mishra, A., & Fletcher, H. M. (2024) · Molecular Oral Microbiology · doi:10.1111/omi.12482
Tian, X., Tian, C.-R., Lu, X.-S., WEN-bo, H. A. O., Zheng, Z., He, J.-J., Zhu, X., & Zheng, X.-N. (2026) · Animals · doi:10.3390/ani16172704
- Authors
- Maeda, K., & Akira, S.
- Affiliations
- Immunology Frontier Research Center, The University of Osaka (JP)
- Corresponding author
- Akira, Shizuo
- Venue
- International Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2017-03-27
- Volume
- 29
- Issue
- 4
- Pages
- 149-155
- ISSN
- 0953-8178 (ISSN-L)
- 1460-2377
- PMC
- PMC5890888
- OpenAlex
- W2602505844
- Cited by
- 64
- References
- 73
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 7 · 2023: 14 · 2022: 9 · 2021: 14 · 2020: 5 · 2019: 5 · 2018: 2 · 2017: 2
- FWCI
- 0.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- International Immunology (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science
- National Institutes of Health (5P01AI070167)
- 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
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Keywords
- mRNA stability, tristetraprolin, Roquin, Regnase-1, RNA-binding proteins, RNA metabolism, immune regulation, immune homeostasis, knockout mice
- MeSH terms
- Animals, Humans, Immune System, Immunity, Ribonucleases, RNA, Messenger, Transcription Factors, RNA-Binding Proteins, RNA Stability, Ubiquitin-Protein Ligases, Tristetraprolin, Immunomodulation
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