Intracellular localization and interaction of mRNA binding proteins as detected by FRET
Open accessAbstract
Background: A number of RNA binding proteins (BPs) bind to A+U rich elements (AREs), commonly present within 3'UTRs of highly regulated RNAs. Individual RNA-BPs proteins can modulate RNA stability, RNA localization, and/or translational efficiency. Although biochemical studies have demonstrated selectivity of ARE-BPs for individual RNAs, less certain is the in vivo composition of RNA-BP multiprotein complexes and how their composition is affected by signaling events and intracellular localization. Using FRET, we previously demonstrated that two ARE-BPs, HuR and AUF1, form stable homomeric and heteromeric associations in the nucleus and cytoplasm. In the current study, we use immuno-FRET of endogenous proteins to examine the intracellular localization and interactions of HuR and AUF1 as well as KSRP, TIA-1, and Hedls. These results were compared to those obtained with their exogenously expressed, fluorescently labeled counterparts. Results: All ARE-BPs examined were found to colocalize and to form stable associations with selected other RNA-BPs in one or more cellular locations variably including the nucleus, cytoplasm (in general), or in stress granules or P bodies. Interestingly, FRET based interaction of the translational suppressor, TIA-1, and the decapping protein, Hedls, was found to occur at the interface of stress granules and P bodies, dynamic sites of intracellular RNA storage and/or turnover. To explore the physical interactions of RNA-BPs with ARE containing RNAs,in vitro transcribed Cy3-labeled RNA was transfected into cells. Interestingly, Cy3-RNA was found to coalesce in P body like punctate structures and, by FRET, was found to interact with the RNA decapping proteins, Hedls and Dcp1. Conclusions: Biochemical methodologies, such as co-immunoprecipitation, and cell biological approaches such as standard confocal microscopy are useful in demonstrating the possibility of proteins and/or proteins and RNAs interacting. However, as demonstrated herein, colocalization of proteins and proteins and RNA is not always indicative of interaction. To this point, using FRET and immuno-FRET, we have demonstrated that RNA-BPs can visually colocalize without producing a FRET signal. In contrast, proteins that appear to be delimited to one or another intracellular compartment can be shown to interact when those compartments are juxtaposed.
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?
HuR interacts with AUF1, KSRP, and TIA-1 in the nucleus and cytoplasmic stress granules.
“Fluorescence resonance energy transfer (FRET) and biochemical techniques revealed that HuR interacts with AUF1, KSRP, and TIA-1 in the nucleus and cytoplasmic stress granules (David et al. 2007; David Gerecht et al. 2010).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as David Gerecht et al. 2010
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
1 retracted
Gherzi, R., Trabucchi, M., Ponassi, M., Ruggiero, T., Corte, G., Moroni, C., Chen, C., Khabar, K. S. A., Andersen, J., & Briata, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0050005 · Cited by 148 · see citing works
RetractedEukaryotic stress granules: the ins and outs of translation.
Buchan, J., & Parker, R. (2009) · Molecules and Cells · doi:10.1016/j.molcel.2009.11.020 · Cited by 1,517 · 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
P bodies and the control of mRNA translation and degradation
Parker, R., & Sheth, U. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.011 · Cited by 1,335 · see citing works
mRNA stability in mammalian cells
Ross, J. (1995) · Microbiological Reviews · doi:10.1128/mr.59.3.423-450.1995 · Cited by 1,324 · see citing works
Kedersha, N., Gupta, M., Li, W., Miller, I. J., & Anderson, P. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.7.1431 · Cited by 1,260 · see citing works
Stress granules: the Tao of RNA triage.
Anderson, P., & Kedersha, N. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2007.12.003 · Cited by 1,156 · see citing works
Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1
Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,000 · see citing works
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984 · see citing works
RNA granules: post-transcriptional and epigenetic modulators of gene expression
Anderson, P., & Kedersha, N. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2694 · Cited by 866 · see citing works
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 · see citing works
Dynamic Shuttling of Tia-1 Accompanies the Recruitment of mRNA to Mammalian Stress Granules
Kedersha, N., Cho, M., Li, W., Yacono, P. W., Chen, S., Farny, N. G., Golan, D. E., & Anderson, P. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1257 · Cited by 815 · see citing works
Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
Kedersha, N., & Anderson, P. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300963 · Cited by 735 · 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
Cloning and Characterization of HuR, a Ubiquitously Expressed Elav-like Protein
Ma, W.-J., Cheng, S., Campbell, C., Wright, A., & Furneaux, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8144 · Cited by 667 · see citing works
Mammalian Stress Granules and Processing Bodies
Kedersha, N., & Anderson, P. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)31005-7 · Cited by 664 · see citing works
Morrison, D. K. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.10.003 · Cited by 604 · see citing works
Purification, Characterization, and cDNA Cloning of an AU-Rich Element RNA-Binding Protein, AUF1
Zhang, W., Wagner, B., Ehrenman, K., Schaefer, A., DeMaria, C. T., Crater, D. L., DeHaven, K., Long, L., & Brewer, G. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7652 · Cited by 540 · see citing works
Phosphorylation of HuR by Chk2 Regulates SIRT1 Expression
Abdelmohsen, K., Pullmann, R., Lal, A., Kim, H. H., Galbán, S., Yang, X., Blethrow, J. D., Walker, M., Shubert, J., Gillespie, D. A., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.011 · Cited by 527 · see citing works
Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs
Lal, A., Mazan‐Mamczarz, K., Kawai, T., Yang, X., Martindale, J. L., & Gorospe, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600305 · Cited by 461 · see citing works
Multiple Processing Body Factors and the ARE Binding Protein TTP Activate mRNA Decapping
Fenger-Grøn, M., Fillman, C. L., Norrild, B., & Lykke‐Andersen, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.031 · Cited by 459 · see citing works
Ingelfinger, D., Arndt‐Jovin, D. J., Lührmann, R., & Achsel, T. (2002) · RNA · doi:10.1017/s1355838202021726 · Cited by 404 · see citing works
The Control of mRNA Decapping and P-Body Formation
Franks, T. M., & Lykke‐Andersen, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.001 · Cited by 399 · see citing works
Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs
Balagopal, V., & Parker, R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.005 · Cited by 391 · see citing works
Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
Fernández-Suárez, M., Baruah, H., Martínez-Hernández, L., Xie, K. T., Baskin, J. M., Bertozzi, C. R., & Ting, A. Y. (2007) · Nature Biotechnology · doi:10.1038/nbt1355 · Cited by 376 · see citing works
A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer.Preprint
Min, H., Turck, C. W., Nikolic, J. M., & Black, D. L. (1997) · Genes & Development · doi:10.1101/gad.11.8.1023 · Cited by 330 · see citing works
HuR binding to cytoplasmic mRNA is perturbed by heat shock
Gallouzi, I., Brennan, C. M., Stenberg, M. G., Swanson, M. S., Eversole, A., Maizels, N., & STEITZ, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3073 · Cited by 326 · see citing works
Inhibition of HIV-1 Infection by Small Interfering RNA-Mediated RNA Interference
Capodici, J., Karikó, K., & Weissman, D. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.9.5196 · Cited by 302 · see citing works
Anderson, P., & Kedersha, N. (2009) · Current Biology · doi:10.1016/j.cub.2009.03.013 · Cited by 302 · see citing works
Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencingPreprint
Eulálio, A., Rehwinkel, J., Stricker, M., Huntzinger, E., Yang, S.-F., Doerks, T., Dorner, S., Peer Bork, B., Boutros, M., & Izaurralde, E. (2007) · Genes & Development · doi:10.1101/gad.443107 · Cited by 297 · see citing works
Wagner, B. J., DeMaria, C. T., Sun, Y., Wilson, G. M., & Brewer, G. (1998) · Genomics · doi:10.1006/geno.1997.5142 · Cited by 274 · see citing works
AUF1 Binding Affinity to A+U-rich Elements Correlates with Rapid mRNA Degradation
DeMaria, C. T., & Brewer, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12179 · Cited by 261 · see citing works
Kontoyiannis, D. L., Kotlyarov, A., Carballo, E., Alexopoulou, L., Blackshear, P. J., Gaestel, M., Davis, R. J., Flavell, R. A., & Kollias, G. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.14.3760 · Cited by 255 · see citing works
Wilkie, G. S., & Davis, I. (2001) · Cell · doi:10.1016/s0092-8674(01)00312-9 · Cited by 247 · see citing works
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 236 · see citing works
Lipopolysaccharide-induced Methylation of HuR, an mRNA-stabilizing Protein, by CARM1
Li, H., Park, S., Kilburn, B., Jelinek, M. A., Henschen-Edman, A. H., Aswad, D. W., Stallcup, M. R., & Laird‐Offringa, I. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206187200 · Cited by 233 · see citing works
Signalling pathways regulating nucleo-cytoplasmic shuttling of the mRNA-binding protein HuR
Doller, A., Pfeilschifter, J. M., & Eberhardt, W. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.05.007 · Cited by 215 · see citing works
Functional cloning of BRF1, a regulator of ARE‐dependent mRNA turnover
Stoecklin, G., Colombi, M., Raineri, I., Leuenberger, S., Mallaun, M., Schmidlin, M., Gross, B., Lu, M., Kitamura, T., & Moroni, C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf444 · Cited by 212 · see citing works
Kulkarni, M. G., Ozgur, S., & Stoecklin, G. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380242 · Cited by 208 · see citing works
Nuclear 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 202 · see citing works
Linker, K., Pautz, A., Fechir, M., Hubrich, T., Greeve, J. C., & Kleinert, H. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki797 · Cited by 200 · see citing works
Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells
Galperin, E., Verkhusha, V., & Sorkin, A. (2004) · Nature Methods · doi:10.1038/nmeth720 · Cited by 199 · see citing works
Pullmann, R., Kim, H. H., Abdelmohsen, K., Lal, A., Martindale, J. L., Yang, X., & Gorospe, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00500-07 · Cited by 199 · see citing works
Doller, A., Huwiler, A., Müller, R., Radeke, H. H., Pfeilschifter, J. M., & Eberhardt, W. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0850 · Cited by 191 · see citing works
Translational Control of Cytochrome c by RNA-Binding Proteins TIA-1 and HuR
Kawai, T., Lal, A., Yang, X., Galbán, S., Mazan-Mamczarz, K., & Gorospe, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3295-3307.2006 · Cited by 187 · see citing works
Doller, A., Akool, E., Huwiler, A., Müller, R., Radeke, H. H., Pfeilschifter, J. M., & Eberhardt, W. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01530-07 · Cited by 187 · see citing works
Sun, L., Stoecklin, G., Way, S. V., Hinkovska‐Galcheva, V., Guo, R., Anderson, P., & Shanley, T. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607347200 · Cited by 184 · see citing works
Control of mRNA decay by phosphorylation of tristetraprolin
Sandler, H., & Stoecklin, G. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360491 · Cited by 176 · see citing works
Ming, X., Stoecklin, G., Lu, M., Looser, R., & Moroni, C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5778-5789.2001 · Cited by 174 · see citing works
miR-519 suppresses tumor growth by reducing HuR levels
Abdelmohsen, K., Kim, M. M., Srikantan, S., Mercken, E. M., Brennan, S. E., Wilson, G. M., de Cabo, R., & Gorospe, M. (2010) · Cell Cycle · doi:10.4161/cc.9.7.11164 · Cited by 146 · see citing works
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 · see citing works
Regulation of A + U-rich Element-directed mRNA Turnover Involving Reversible Phosphorylation of AUF1
Wilson, G. M., Lu, J., Sutphen, K., Sun, Y. M., Huynh, Y., & Brewer, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305772200 · Cited by 132 · see citing works
Chapter 26 Real‐Time and Quantitative Imaging of Mammalian Stress Granules and Processing Bodies
Kedersha, N., Tisdale, S., Hickman, T. T., & Anderson, P. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)02626-8 · Cited by 123 · see citing works
Cok, S. J., Acton, S. J., Sexton, A., & Morrison, A. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308475200 · Cited by 111 · see citing works
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 104 · see citing works
Suswam, E. A., Nabors, B., Huang, Y., Yang, X., & King, P. H. (2004) · International Journal of Cancer · doi:10.1002/ijc.20675 · Cited by 100 · see citing works
Doller, A., Schlepckow, K., Schwalbe, H., Pfeilschifter, J. M., & Eberhardt, W. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01373-09 · Cited by 98 · see citing works
Assembly of AUF1 Oligomers on U-rich RNA Targets by Sequential Dimer Association
Wilson, G. M., Sun, Y. M., Lu, H., & Brewer, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33374 · Cited by 93 · see citing works
Maitra, S., Chou, C., Luber, C. A., Lee, K., Mann, M., & Chen, C. (2008) · RNA · doi:10.1261/rna.983708 · Cited by 91 · see citing works
Structural Determinants in AUF1 Required for High Affinity Binding to A + U-rich Elements
DeMaria, C. T., Sun, Y. M., Long, L., Wagner, B. J., & Brewer, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27635 · Cited by 90 · see citing works
Panyi, G., Bagdány, M., Bodnár, A., Vámosi, G., Szentesi, G., Jenei, A., Mátyus, L., Varga, S., Waldmann, T. A., Gáspár, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0438057100 · Cited by 86 · see citing works
Phosphorylated HuR shuttles in cycles
Kim, H. H., & Gorospe, M. (2008) · Cell Cycle · doi:10.4161/cc.7.20.6884 · Cited by 84 · see citing works
Regulation of Neuron-Specific Alternative Splicing of Neurofibromatosis Type 1 Pre-mRNA
Zhu, H., Hinman, M. N., Hasman, R. A., Mehta, P., & Lou, H. J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01509-07 · Cited by 82 · see citing works
TIA-1: Structural and Functional Studies on a New Class of Cytolytic Effector Molecule
Anderson, P. (1995) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-79414-8_8 · Cited by 77 · see citing works
Pan, Y., Chen, H., & Kilberg, M. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507802200 · Cited by 73 · see citing works
FRET-detectable interactions between the ARE binding proteins, HuR and p37AUF1
David, P. S., Tanveer, R., & Port, J. D. (2007) · RNA · doi:10.1261/rna.501707 · Cited by 72 · see citing works
Self-citationModification at HuR(S242) alters HuR localization and proliferative influence
Kim, H. H., Yang, X., Kuwano, Y., & Gorospe, M. (2008) · Cell Cycle · doi:10.4161/cc.7.21.6895 · Cited by 70 · see citing works
Pedro-Segura, E., Vergara, S. V., Rodríguez‐Navarro, S., Parker, R., Thiele, D. J., & Puig, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804910200 · Cited by 68 · see citing works
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 64 · see citing works
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 · see citing works
AUF1 and HuR Proteins Stabilize Interleukin-8 mRNA in Human Saliva
Palanisamy, V., Park, N. J., Wang, J., & Wong, D. T. (2008) · Journal of Dental Research · doi:10.1177/154405910808700803 · Cited by 58 · see citing works
König, P., Krasteva‐Christ, G., Tag, C., König, I. R., Arens, C., & Kummer, W. (2006) · Laboratory Investigation · doi:10.1038/labinvest.3700443 · Cited by 56 · see citing works
Liposome-mediated RNA transfection should be used with caution
Barreau, C., Dutertre, S., Paillard, L., & Osborne, H. B. (2006) · RNA · doi:10.1261/rna.191706 · Cited by 51 · see citing works
Characteristics of the Intron Involvement in the Mitogen-induced Expression of Zfp-36
Lai, W. S., Thompson, M. J., & Blackshear, P. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.506 · Cited by 48 · see citing works
14‐3‐3σ is a p37 AUF1‐binding protein that facilitates AUF1 transport and AU‐rich mRNA decay
He, C., & Schneider, R. J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601264 · Cited by 46 · see citing works
Visualizing protein–RNA interactions inside cells by fluorescence resonance energy transfer
Lorenz, M. (2008) · RNA · doi:10.1261/rna.1307809 · Cited by 45 · see citing works
Intron-exon organization and chromosomal localization of the human TIA-1 gene.
Kawakami, A., Tian, Q., Streuli, M., Poe, M., Edelhoff, S., Distèche, C. M., & Anderson, P. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.10.4937 · Cited by 43 · see citing works
Turnover in the Alps: an mRNA perspective
Newbury, S. F., Mühlemann, O., & Stoecklin, G. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400628 · Cited by 36 · see citing works
Clark, A. R., Dean, J. L. E., & Saklatvala, J. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24919 · Cited by 34 · see citing works
Identification of FUSE-binding proteins as interacting partners of TIA proteins
Rothé, F., Gueydan, C., Bellefroid, E., Huez, G. A., & Kruys, V. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.112 · Cited by 33 · see citing works
Cayli, S., Klug, J., Chapiro, J., Fröhlich, S., Krasteva, G., Orel, L., & Meinhardt, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037952 · Cited by 31 · see citing works
Huranová, M., Jablonski, J. A., Benda, A., Hof, M., Staněk, D., & Caputi, M. (2009) · RNA · doi:10.1261/rna.1678209 · Cited by 30 · see citing works
Control of the ATP synthase β subunit expression by RNA-binding proteins TIA-1, TIAR, and HuR
Izquierdo, J. M. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.07.114 · Cited by 28 · see citing works
Caveolin-1 and -2 in airway epithelium: expression and in situ association as detected by FRET-CLSM
Krasteva‐Christ, G., Pfeil, U., Dráb, M., Kummer, W., & König, P. (2006) · Respiratory Research · doi:10.1186/1465-9921-7-108 · Cited by 26 · see citing works
Headley, V. V., Tanveer, R., Greene, S. M., Zweifach, A., & Port, J. D. (2004) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000012841.03400.42 · Cited by 21 · see citing works
Self-citationβ‐Dystroglycan modulates the interplay between actin and microtubules in human‐adhered platelets
Cerecedo, D., Cisneros, B., Suárez‐Sánchez, R., Hernández-González, E. O., & Galván, I. J. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07048.x · Cited by 19 · see citing works
RNA localization: visualization in real-time
Singer, R. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00605-5 · Cited by 17 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Alternative RISC assembly: Binding and repression of microRNA–mRNA duplexes by human Ago proteins
Janas, M. M., Wang, B., Harris, A., Aguiar, M., Shaffer, J. M., Subrahmanyam, Y. V. B. K., Behlke, M. A., Wucherpfennig, K. W., Gygi, S. P., Gagnon, É., et al. (2012) · RNA · doi:10.1261/rna.035675.112 · Cited by 128 · see citing works
Bronicki, L. M., & Jasmin, B. J. (2013) · RNA · doi:10.1261/rna.039164.113 · Cited by 126 · see citing works
Subramaniam, D., Ramalingam, S., Linehan, D. C., Dieckgraefe, B. K., Postier, R. G., Houchen, C. W., Jensen, R. A., & Anant, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016958 · Cited by 78 · see citing works
Hallmarks of cancer and AU ‐rich elements
Khabar, K. S. A. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1368 · Cited by 77 · see citing works
Targeting the Multifaceted HuR Protein, Benefits and Caveats
Zucal, C., D’Agostino, V., Loffredo, R., Mantelli, B., Thongon, N., Lal, P., Latorre, E., & Provenzani, A. (2015) · Current Drug Targets · doi:10.2174/1389450116666150223163632 · Cited by 65 · see citing works
DSCR1 interacts with FMRP and is required for spine morphogenesis and local protein synthesis
Wang, W., Zhu, J. Z., Chang, K. T., & Min, K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.190 · Cited by 52 · see citing works
Horowitz, S. A., & Bardwell, J. C. A. (2016) · RNA Biology · doi:10.1080/15476286.2016.1247147 · Cited by 35 · see citing works
5′-AMP-activated protein kinase alpha regulates stress granule biogenesis
Mahboubi, H., Barisé, R., & Stochaj, U. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.015 · Cited by 29 · see citing works
Stress granules in colorectal cancer: Current knowledge and potential therapeutic applications
Legrand, N., Dixon, D. A., & Sobolewski, C. (2020) · World Journal of Gastroenterology · doi:10.3748/wjg.v26.i35.5223 · Cited by 29 · see citing works
Tardif, C., Nadeau, G., Labrecque, S., Côté, D. C., Lavoie‐Cardinal, F., & Koninck, P. D. (2019) · Neurophotonics · doi:10.1117/1.nph.6.1.015002 · Cited by 23 · see citing works
Post-translational and transcriptional dynamics – regulating extracellular vesicle biology
Claridge, B., Kastaniegaard, K., Stensballe, A., & Greening, D. W. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1551135 · Cited by 21 · see citing works
RNA Granules and Their Role in Neurodegenerative Diseases
Sidibé, H., & Velde, C. V. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-31434-7_8 · Cited by 20 · see citing works
mRNA stability as a function of striated muscle oxidative capacity
D’Souza, D. M., Lai, R. Y. J., Shuen, M., & Hood, D. A. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00085.2012 · Cited by 20 · see citing works
Šimková, E., & Staněk, D. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131114929 · Cited by 13 · see citing works
Detection of long mRNA sequences by a Y-shaped DNA probe with three target-binding segments
He, S., Zhao, X., Chen, F., Chen, C., Gong, H., & Cai, C. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341633 · Cited by 12 · see citing works
Bire, S., Ishac, N., & Rouleux‐Bonnin, F. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3625-0_13 · Cited by 3 · see citing works
Adrenergic Receptor Signaling in Heart Failure
Port, J. D., Sucharov, C. C., & Bristow, M. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-323-60987-6.00006-5 · Cited by 2 · see citing works
Self-citationDesigning a Compact, Low-Cost FRET Microscopy Platform for the Undergraduate Classroom
Rupel, J. W., Sdao, S. M., Johnston, K. E., Nethery, E. T., Gabardi, K., Ratliff, B. A., Simmons, Z. J., Postlewaite, J. T., Kita, A. M., Rogers, J. D., et al. (2020) · The Biophysicist · doi:10.35459/tbp.2019.000117 · Cited by 1 · see citing works
Improvements and Applications of in situ Proximity Ligation Assays
Grannas, K. (2015) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1 · see citing works
Investigating RNA granules formation during caliciviruses infection
Al-Sailawi, M. (2015) · Surrey Research Insight Open Access (The University of Surrey)
Desenvolvimento de Primer universal de SBE para codificação espectral de SNP
Cordeiro, M. (2012) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
- Authors
- David Gerecht, P. S., Taylor, M. A., & Port, J. D.
- Affiliations
- Case Western Reserve University (US)
- University of Colorado Anschutz (US)
- Corresponding author
- Port, J David
- Venue
- BMC Cell Biology
- Published
- 2010-09-15
- Volume
- 11
- Issue
- 1
- Pages
- 69-69
- ISSN
- 1471-2121 (ISSN-L)
- PMC
- PMC2949623
- OpenAlex
- W1983342911
- Cited by
- 22
- References
- 87
- Citations by year
- 2023: 1 · 2020: 3 · 2019: 2 · 2018: 1 · 2016: 3 · 2015: 4 · 2013: 1 · 2012: 5
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- BMC Cell Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL051239, HL 51239)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- RNA-binding proteins, AU-rich elements, HuR, AUF1, KSRP, TIA-1, P-bodies, stress granules, protein-protein interaction, RNA-protein interactions, RNA decapping, DCP1, 3' untranslated region, translational regulation, protein colocalization
- MeSH terms
- ELAV-Like Protein 1, Heterogeneous Nuclear Ribonucleoprotein D0, Animals, Antigens, Surface, Cell Line, Cricetinae, Protein Binding, RNA, Messenger, RNA-Binding Proteins, 3' Untranslated Regions, Protein Transport, Fluorescence Resonance Energy Transfer, Heterogeneous-Nuclear Ribonucleoprotein D, Poly(A)-Binding Proteins, Multiprotein Complexes, ELAV Proteins, Protein Multimerization
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
