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KSRP, many functions for a single protein
Abstract
KSRP is a single-strand nucleic acids binding protein that affects RNA fate at multiple levels. KSRP modular structure and its complex pattern of post-translational modifications underpin the interaction with a wide spectrum of RNA target sequences, as well as with other RNA-binding proteins and molecular adaptors. These interactions are important to the regulation of different steps of mRNA metabolism and, in turn, modulate several aspects of cellular proliferation and differentiation. In this review we will discuss in detail KSRP ability to i) promote decay of labile mRNAs interacting with some components of the mRNA decay machinery and ii) favor the maturation of a select group of microRNA precursors.
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“Some ARE-BPs are decay-promoting factors, such as KH-type splicing regulatory proteins (KSRPs), that interact with AREs and recruit RNA degradation machinery to the mRNA.”
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2 retracted
Fukuda, T., Yamagata, K., Fujiyama, S., Matsumoto, T., Koshida, I., Yoshimura, K., Mihara, M., Naitou, M., Endoh, H., Nakamura, T., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1577 · Cited by 428
RetractedA TARBP2 mutation in human cancer impairs microRNA processing and DICER1 function
Melo, S. A., Ropero, S., Moutinho, C., Aaltonen, L. A., Yamamoto, H., Calin, G. A., Rossi, S., Fernandez, A. F., Carneiro, F., Oliveira, C., et al. (2009) · Nature Genetics · doi:10.1038/ng.317 · Cited by 373
RetractedMicroRNA expression profiles classify human cancers
Lu, J., Getz, G., Miska, E. A., Alvarez-Saavedra, E., Lamb, J., Peck, D., Sweet-Cordero, A., Ebert, B. L., Mak, R. H., Ferrando, A. A., et al. (2005) · Nature · doi:10.1038/nature03702 · Cited by 9,539
(2008) · doi:10.1038/nrg2290 · Cited by 5,199
Many roads to maturity: microRNA biogenesis pathways and their regulation
Winter, J., Jung, S., Keller, S., Gregory, R. I., & Diederichs, S. (2009) · Nature Cell Biology · doi:10.1038/ncb0309-228 · Cited by 2,656
Impaired microRNA processing enhances cellular transformation and tumorigenesis
Kumar, M. S., Lu, J., Mercer, K. L., Golub, T. R., & Jacks, T. (2007) · Nature Genetics · doi:10.1038/ng2003 · Cited by 1,463
Selective Blockade of MicroRNA Processing by Lin28
Viswanathan, S. R., Daley, G. Q., & Gregory, R. I. (2008) · Science · doi:10.1126/science.1154040 · Cited by 1,437
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
The Many Pathways of RNA Degradation
Houseley, J., & Tollervey, D. (2009) · Cell · doi:10.1016/j.cell.2009.01.019 · Cited by 1,229
Extensive post-transcriptional regulation of microRNAs and its implications for cancer
Thomson, J. M., Newman, M., Parker, J. S., Morin-Kensicki, E. M., Wright, T., & Hammond, S. M. (2006) · Genes & Development · doi:10.1101/gad.1444406 · Cited by 877
AU Binding Proteins Recruit the Exosome to Degrade ARE-Containing mRNAs
Chen, C.-Y., Gherzi, R., Ong, S.-E., Chan, E. L., Raijmakers, R., Pruijn, G. J. M., Stoecklin, G., Moroni, C., Mann, M., & Karin, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00578-5 · Cited by 865
let-7 microRNAs in development, stem cells and cancer
Büssing, I., Slack, F. J., & Großhans, H. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.07.001 · Cited by 607
The RNA-binding protein KSRP promotes the biogenesis of a subset of microRNAs
Trabucchi, M., Briata, P., Garcia-Mayoral, M., Haase, A. D., Filipowicz, W., Ramos, A., Gherzi, R., & Rosenfeld, M. G. (2009) · Nature · doi:10.1038/nature08025 · Cited by 607
Self-citationThe RNA-induced Silencing Complex: A Versatile Gene-silencing Machine
Pratt, A. J., & MacRae, I. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900012200 · Cited by 602
The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
Guil, S., & Cáceres, J. F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1250 · Cited by 567
Structure and function of KH domains
Valverde, R., Edwards, L., & Regan, L. (2008) · The FEBS Journal · doi:10.1111/j.1742-4658.2008.06411.x · Cited by 506
A High-Resolution Structure of the Pre-microRNA Nuclear Export Machinery
Okada, C., Yamashita, E., Lee, S. J., Shibata, S., Katahira, J., Nakagawa, A., Yoneda, Y., & Tsukihara, T. (2009) · Science · doi:10.1126/science.1178705 · Cited by 484
Hao, S., & Baltimore, D. (2009) · Nature Immunology · doi:10.1038/ni.1699 · Cited by 480
Post-transcriptional regulation of microRNA expression
Obernosterer, G., Leuschner, P. J. F., Alenius, M., & Martinez, J. (2006) · RNA · doi:10.1261/rna.2322506 · Cited by 474
Gherzi, R., Lee, K.-Y., Briata, P., Wegmüller, D., Moroni, C., Karin, M., & Chen, C.-Y. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.002 · Cited by 454
Self-citationMK2‐induced tristetraprolin:14‐3‐3 complexes prevent stress granule association and ARE‐mRNA decay
Stoecklin, G., Stubbs, T., Kedersha, N., Wax, S., Rigby, W. F., Blackwell, T. K., & Anderson, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600163 · Cited by 448
Phosphorylation of the Human MicroRNA-Generating Complex Mediates MAPK/Erk Signaling
Paroo, Z., Ye, X., Chen, S., & Liu, Q. (2009) · Cell · doi:10.1016/j.cell.2009.06.044 · Cited by 366
Posttranscriptional Regulation of miRNAs Harboring Conserved Terminal Loops
Michlewski, G., Guil, S., Semple, C. A., & Cáceres, J. F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.013 · Cited by 335
A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer.
Min, H., Turck, C. W., Nikolic, J. M., & Black, D. L. (1997) · Genes & Development · doi:10.1101/gad.11.8.1023 · Cited by 329
Post‐transcriptional regulation of gene expression by degradation of messenger RNAs
Bevilacqua, A., Ceriani, M. C., Capaccioli, S., & Nicolin, A. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10272 · Cited by 316
Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis
Michlewski, G., & Cáceres, J. F. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1874 · Cited by 269
Brook, M., Tchen, C. R., Santalucı́a, T., McIlrath, J. M., Arthur, J. S. C., Saklatvala, J., & Clark, A. R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2408-2418.2006 · Cited by 250
Briata, P., Forcales, S. V., Ponassi, M., Corte, G., Chen, C., Karin, M., Puri, P., & Gherzi, R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.021 · Cited by 240
Self-citationNuclear HuR accumulation through phosphorylation by Cdk1Preprint
Kim, H. H., Abdelmohsen, K., Lal, A., Pullmann, R., Yang, X., Galbán, S., Srikantan, S., Martindale, J. L., Blethrow, J. D., Shokat, K. M., et al. (2008) · Genes & Development · doi:10.1101/gad.1645808 · Cited by 212
Linker, K., Pautz, A., Fechir, M., Hubrich, T., Greeve, J. C., & Kleinert, H. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki797 · Cited by 209
Ruggiero, T., Trabucchi, M., Santa, F. D., Zupo, S., Harfe, B. D., McManus, M. T., Rosenfeld, M. G., Briata, P., & Gherzi, R. (2009) · The FASEB Journal · doi:10.1096/fj.09-131342 · Cited by 208
Self-citationRole of HuR in Skeletal Myogenesis through Coordinate Regulation of Muscle Differentiation Genes
Figueroa, A., Cuadrado, A., Fan, J., Atasoy, U., Muscat, G. E. O., Muñoz‐Cánoves, P., Gorospe, M., & Múñoz, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.14.4991-5004.2003 · Cited by 195
Davis-Smyth, T., DUNCAN, R. C., Zheng, T., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31679 · Cited by 187
The AU-Rich Transcriptome: More Than Interferons and Cytokines, and Its Role in Disease
Khabar, K. S. A. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.1 · Cited by 176
Control of mRNA decay by phosphorylation of tristetraprolin
Sandler, H., & Stoecklin, G. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360491 · Cited by 176
Modulation of mRNA stability as a novel therapeutic approach
Eberhardt, W., Doller, A., Akool, E.-S., & Pfeilschifter, J. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.01.002 · Cited by 173
Diverse molecular interactions of the hnRNP K protein
Bomsztyk, K., SEUNINGEN, I. V., Suzuki, H., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00041-0 · Cited by 161
Lellek, H., Kirsten, R., Diehl, I., Apostel, F., Buck, F., & Greeve, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001786200 · Cited by 150
Lin, J., Li, M.-L., & Shih, S. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn901 · Cited by 148
Winzen, R., Thakur, B. K., Dittrich‐Breiholz, O., Shah, M., Redich, N., Dhamija, S., Kracht, M., & Holtmann, H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01493-07 · Cited by 142
The ARE‐dependent mRNA‐destabilizing activity of BRF1 is regulated by protein kinase B
Schmidlin, M., Lu, M., Leuenberger, S. A., Stoecklin, G., Mallaun, M., Gross, B., Gherzi, R., Heß, D., Hemmings, B. A., & Moroni, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600477 · Cited by 138
RNAi-mediated HuR Depletion Leads to the Inhibition of Muscle Cell Differentiation
van der Giessen, K., Marco, S. D., Clair, E., & Gallouzi, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308889200 · Cited by 126
García‐Mayoral, M. F., Hollingworth, D., Masino, L., Díaz‐Moreno, I., Kelly, G. P., Gherzi, R., Chou, C., Chen, C., & Ramos, A. (2007) · Structure · doi:10.1016/j.str.2007.03.006 · Cited by 123
Tethering KSRP, a Decay-Promoting AU-Rich Element-Binding Protein, to mRNAs Elicits mRNA Decay
Chou, C., Mulky, A., Maitra, S., Lin, W., Gherzi, R., Kappes, J. C., & Chen, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3695-3706.2006 · Cited by 118
Wilson, G. M., Lu, J., Sutphen, K., Suarez, Y., Sinha, S., Brewer, B. Y., Villanueva-Feliciano, E. C., Ysla, R. M., Charles, S., & Brewer, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305775200 · Cited by 114
Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding
Díaz‐Moreno, I., Hollingworth, D., Frenkiel, T. A., Kelly, G. P., Martin, S. R., Howell, S. A., García‐Mayoral, M. F., Gherzi, R., Briata, P., & Ramos, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1558 · Cited by 106
Self-citationMaitra, S., Chou, C., Luber, C. A., Lee, K., Mann, M., & Chen, C. (2008) · RNA · doi:10.1261/rna.983708 · Cited by 90
Li, H., Chen, W., Zhou, Y., Abidi, P., Sharpe, O., Robinson, W. H., Kraemer, F. B., & Liu, J. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m800375-jlr200 · Cited by 85
Rehbein, M., Wege, K., Buck, F., Schweizer, M., Richter, D., & Kindler, S. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01058.x · Cited by 71
Nechama, M., Ben‐Dov, I. Z., Briata, P., Gherzi, R., & Naveh‐Many, T. (2008) · The FASEB Journal · doi:10.1096/fj.08-107250 · Cited by 65
Self-citationThe sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
García‐Mayoral, M. F., Díaz‐Moreno, I., Hollingworth, D., & Ramos, A. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn509 · Cited by 65
Rehbein, M., Kindler, S., Horke, S., & Richter, D. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00114-5 · Cited by 64
Identification of a set of KSRP target transcripts upregulated by PI3K-AKT signaling
Ruggiero, T., Trabucchi, M., Ponassi, M., Corte, G., Chen, C., Al‐Haj, L., Khabar, K. S. A., Briata, P., & Gherzi, R. (2007) · BMC Molecular Biology · doi:10.1186/1471-2199-8-28 · Cited by 63
Self-citationDíaz‐Moreno, I., Hollingworth, D., Kelly, G. P., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq216 · Cited by 44
TTP at Ser245 Phosphorylation by AKT is Required for Binding to 14-3-3
Chiba, S., Tokuhara, M., Morita, E. H., et al. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvn178 · Cited by 12
Research works printed but not linked: 2
- R. Gherzi, M. Trabucchi, M. Ponassi, T. Ruggiero, G. Corte, C. Moroni, C.-Y. Chen, K.S. Khabar, J.S. Andersen, and Briata P: The RNA-binding protein KSRP promotes decay of beta-catenin mRNA and is inactivated by PI3K- AKT signaling. PLoS Biol. 5, e5 (2006)
- M. Nechama, Y. Peng, O. Bell, P. Briata, R. Gherzi, D.R. Schoenberg, and T. Naveh-Many: KSRP-PMR1- exosome association determines parathyroid hormone mRNA levels and stability in transfected cells. BMC Cell Biol. 10, 70 (2009)
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Singh, A. B., Kan, C. F. K., Shende, V., Dong, B., & Liu, J. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m049429 · Cited by 35
Singh, A. B., Li, H., Kan, C. F. K., Dong, B., Nicolls, M. R., & Liu, J. (2014) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.112.301131 · Cited by 32
Metadata
- Authors
- Briata, P.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2011
- Volume
- 16
- Issue
- 1
- Pages
- 1787
- ISSN
- 1093-9946
- 1093-4715
- DOI
- 10.2741/3821
- Cited by
- 49
- References
- 55
- Language
- en
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