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Journal articles on the topic 'RNA localization and translation'

Author: Grafiati

Published: 11 March 2023

Last updated: 31 July 2025

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1

Gáspár, Imre, and Anne Ephrussi. "RNA localization feeds translation." Science 357, no. 6357 (2017): 1235–36. http://dx.doi.org/10.1126/science.aao5796.

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Gavis, E. R., L. Lunsford, S. E. Bergsten, and R. Lehmann. "A conserved 90 nucleotide element mediates translational repression of nanos RNA." Development 122, no. 9 (1996): 2791–800. http://dx.doi.org/10.1242/dev.122.9.2791.

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Correct formation of the Drosophila body plan requires restriction of nanos activity to the posterior of the embryo. Spatial regulation of nanos is achieved by a combination of RNA localization and localization-dependent translation such that only posteriorly localized nanos RNA is translated. Cis-acting sequences that mediate both RNA localization and translational regulation lie within the nanos 3′ untranslated region. We have identified a discrete translational control element within the nanos 3′ untranslated region that acts independently of the localization signal to mediate translational

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3

Lasko, Paul. "Cup-ling oskar RNA localization and translational control." Journal of Cell Biology 163, no. 6 (2003): 1189–91. http://dx.doi.org/10.1083/jcb.200311123.

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RNA localization and spatially restricted translational control can serve to deploy specific proteins to particular places within a cell. oskar (osk) RNA is a key initiatior of posterior patterning and germ cell specification in Drosophila, and its localization and translation are under elaborate control. In this issue, Wilhelm et al. (2003) show that the protein Cup both promotes osk localization and participates in repressing translation of unlocalized osk.

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Rongo, C., E. R. Gavis, and R. Lehmann. "Localization of oskar RNA regulates oskar translation and requires Oskar protein." Development 121, no. 9 (1995): 2737–46. http://dx.doi.org/10.1242/dev.121.9.2737.

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The site of oskar RNA and protein localization within the oocyte determines where in the embryo primordial germ cells form and where the abdomen develops. Initiation of oskar RNA localization requires the activity of several genes. We show that ovaries mutant for any of these genes lack Oskar protein. Using various transgenic constructs we have determined that sequences required for oskar RNA localization and translational repression map to the oskar 3′UTR, while sequences involved in the correct temporal activation of translation reside outside the oskar 3′UTR. Upon localization of oskar RNA

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Rosana, Albert Remus R., Denise S. Whitford, Richard P. Fahlman, and George W. Owttrim. "Cyanobacterial RNA Helicase CrhR Localizes to the Thylakoid Membrane Region and Cosediments with Degradosome and Polysome Complexes in Synechocystis sp. Strain PCC 6803." Journal of Bacteriology 198, no. 15 (2016): 2089–99. http://dx.doi.org/10.1128/jb.00267-16.

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ABSTRACTThe cyanobacteriumSynechocystissp. strain PCC 6803 encodes a single DEAD box RNA helicase, CrhR, whose expression is tightly autoregulated in response to cold stress. Subcellular localization and proteomic analysis results indicate that CrhR localizes to both the cytoplasmic and thylakoid membrane regions and cosediments with polysome and RNA degradosome components. Evidence is presented that either functional RNA helicase activity or a C-terminal localization signal was required for polysome but not thylakoid membrane localization. Polysome fractionation and runoff translation analysi

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Bergsten, S. E., and E. R. Gavis. "Role for mRNA localization in translational activation but not spatial restriction of nanos RNA." Development 126, no. 4 (1999): 659–69. http://dx.doi.org/10.1242/dev.126.4.659.

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Patterning of the anterior-posterior body axis during Drosophila development depends on the restriction of Nanos protein to the posterior of the early embryo. Synthesis of Nanos occurs only when maternally provided nanos RNA is localized to the posterior pole by a large, cis-acting signal in the nanos 3′ untranslated region (3′UTR); translation of unlocalized nanos RNA is repressed by a 90 nucleotide Translational Control Element (TCE), also in the 3′UTR. We now show quantitatively that the majority of nanos RNA in the embryo is not localized to the posterior pole but is distributed throughout

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Mansfield, Jennifer H., James E. Wilhelm, and Tulle Hazelrigg. "Ypsilon Schachtel, aDrosophilaY-box protein, acts antagonistically to Orb in theoskarmRNA localization and translation pathway." Development 129, no. 1 (2002): 197–209. http://dx.doi.org/10.1242/dev.129.1.197.

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Subcellular localization of mRNAs within the Drosophila oocyte is an essential step in body patterning. Yps, a Drosophila Y-box protein, is a component of an ovarian ribonucleoprotein complex that also contains Exu, a protein that plays an essential role in mRNA localization. Y-box proteins are known translational regulators, suggesting that this complex might regulate translation as well as mRNA localization. Here we examine the role of the yps gene in these events. We show that yps interacts genetically with orb, a positive regulator of oskar mRNA localization and translation. The nature of

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Rajgor, Dipen, and Catherine M. Shanahan. "RNA granules and cytoskeletal links." Biochemical Society Transactions 42, no. 4 (2014): 1206–10. http://dx.doi.org/10.1042/bst20140067.

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In eukaryotic cells, non-translating mRNAs can accumulate into cytoplasmic mRNP (messenger ribonucleoprotein) granules such as P-bodies (processing bodies) and SGs (stress granules). P-bodies contain the mRNA decay and translational repression machineries and are ubiquitously expressed in mammalian cells and lower eukaryote species including Saccharomyces cerevisiae, Drosophila melanogaster and Caenorhabditis elegans. In contrast, SGs are only detected during cellular stress when translation is inhibited and form from aggregates of stalled pre-initiation complexes. SGs and P-bodies are related

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MARZI, S. "Ribosomal localization of translation initiation factor IF2." RNA 9, no. 8 (2003): 958–69. http://dx.doi.org/10.1261/rna.2116303.

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10

Vazquez-Pianzola, Paula, and Beat Suter. "Conservation of the RNA Transport Machineries and Their Coupling to Translation Control across Eukaryotes." Comparative and Functional Genomics 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/287852.

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Restriction of proteins to discrete subcellular regions is a common mechanism to establish cellular asymmetries and depends on a coordinated program of mRNA localization and translation control. Many processes from the budding of a yeast to the establishment of metazoan embryonic axes and the migration of human neurons, depend on this type of cell polarization. How factors controlling transport and translation assemble to regulate at the same time the movement and translation of transported mRNAs, and whether these mechanisms are conserved across kingdoms is not yet entirely understood. In thi

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Anderson, Paul, and Nancy Kedersha. "RNA granules." Journal of Cell Biology 172, no. 6 (2006): 803–8. http://dx.doi.org/10.1083/jcb.200512082.

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Cytoplasmic RNA granules in germ cells (polar and germinal granules), somatic cells (stress granules and processing bodies), and neurons (neuronal granules) have emerged as important players in the posttranscriptional regulation of gene expression. RNA granules contain various ribosomal subunits, translation factors, decay enzymes, helicases, scaffold proteins, and RNA-binding proteins, and they control the localization, stability, and translation of their RNA cargo. We review the relationship between different classes of these granules and discuss how spatial organization regulates messenger

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Zhang, Linzhu, Yaguang Zhang, Su Zhang, et al. "Translational Regulation by eIFs and RNA Modifications in Cancer." Genes 13, no. 11 (2022): 2050. http://dx.doi.org/10.3390/genes13112050.

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Translation is a fundamental process in all living organisms that involves the decoding of genetic information in mRNA by ribosomes and translation factors. The dysregulation of mRNA translation is a common feature of tumorigenesis. Protein expression reflects the total outcome of multiple regulatory mechanisms that change the metabolism of mRNA pathways from synthesis to degradation. Accumulated evidence has clarified the role of an increasing amount of mRNA modifications at each phase of the pathway, resulting in translational output. Translation machinery is directly affected by mRNA modifi

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Yoon, Young J., Bin Wu, Adina R. Buxbaum, et al. "Glutamate-induced RNA localization and translation in neurons." Proceedings of the National Academy of Sciences 113, no. 44 (2016): E6877—E6886. http://dx.doi.org/10.1073/pnas.1614267113.

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Localization of mRNA is required for protein synthesis to occur within discrete intracellular compartments. Neurons represent an ideal system for studying the precision of mRNA trafficking because of their polarized structure and the need for synapse-specific targeting. To investigate this targeting, we derived a quantitative and analytical approach. Dendritic spines were stimulated by glutamate uncaging at a diffraction-limited spot, and the localization of single β-actin mRNAs was measured in space and time. Localization required NMDA receptor activity, a dynamic actin cytoskeleton, and the

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Castagnetti, S., M. W. Hentze, A. Ephrussi, and F. Gebauer. "Control of oskar mRNA translation by Bruno in a novel cell-free system from Drosophila ovaries." Development 127, no. 5 (2000): 1063–68. http://dx.doi.org/10.1242/dev.127.5.1063.

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The coupled regulation of oskar mRNA localization and translation in time and space is critical for correct anteroposterior patterning of the Drosophila embryo. Localization-dependent translation of oskar mRNA, a mechanism whereby oskar RNA localized at the posterior of the oocyte is selectively translated and the unlocalized RNA remains in a translationally repressed state, ensures that Oskar activity is present exclusively at the posterior pole. Genetic experiments indicate that translational repression involves the binding of Bruno protein to multiple sites, the Bruno Response Elements (BRE

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Yeter-Alat, Hilal, Naïma Belgareh-Touzé, Agnès Le Saux, et al. "The RNA Helicase Ded1 from Yeast Is Associated with the Signal Recognition Particle and Is Regulated by SRP21." Molecules 29, no. 12 (2024): 2944. http://dx.doi.org/10.3390/molecules29122944.

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The DEAD-box RNA helicase Ded1 is an essential yeast protein involved in translation initiation that belongs to the DDX3 subfamily. The purified Ded1 protein is an ATP-dependent RNA-binding protein and an RNA-dependent ATPase, but it was previously found to lack substrate specificity and enzymatic regulation. Here we demonstrate through yeast genetics, yeast extract pull-down experiments, in situ localization, and in vitro biochemical approaches that Ded1 is associated with, and regulated by, the signal recognition particle (SRP), which is a universally conserved ribonucleoprotein complex requ

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Pyhtila, B., T. Zheng, P. J. Lager, J. D. Keene, M. C. Reedy, and C. V. Nicchitta. "Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum." RNA 14, no. 3 (2008): 445–53. http://dx.doi.org/10.1261/rna.721108.

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Zurla, C., J. Jung, and P. J. Santangelo. "Can we observe changes in mRNA “state”? Overview of methods to study mRNA interactions with regulatory proteins relevant in cancer related processes." Analyst 141, no. 2 (2016): 548–62. http://dx.doi.org/10.1039/c5an01959a.

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RNA binding proteins (RBP) regulate the editing, localization, stabilization, translation, and degradation of ribonucleic acids (RNA) through their interactions with specificcis-acting elements within target RNAs.

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Muench, Douglas G., and Nam-Il Park. "Messages on the move: the role of the cytoskeleton in mRNA localization and translation in plant cellsThis review is one of a selection of papers published in the Special Issue on Plant Cell Biology." Canadian Journal of Botany 84, no. 4 (2006): 572–80. http://dx.doi.org/10.1139/b05-167.

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The cytoskeleton plays an important role in numerous cellular processes, including subcellular mRNA localization and translation. Several examples of mRNA localization have emerged in plant cells, and these appear to function in protein targeting, the establishment of polarity, and cell-to-cell trafficking. The identification of several cytoskeleton-associated RNA-binding proteins in plant cells has made available candidate proteins that mediate the interaction between mRNA and the cytoskeleton, and possibly play a role in mRNA localization and translational control. We propose a model that li

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Minshall, Nicola, Michel Kress, Dominique Weil, and Nancy Standart. "Role of p54 RNA Helicase Activity and Its C-terminal Domain in Translational Repression, P-body Localization and Assembly." Molecular Biology of the Cell 20, no. 9 (2009): 2464–72. http://dx.doi.org/10.1091/mbc.e09-01-0035.

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The RNA helicase p54 (DDX6, Dhh1, Me31B, Cgh-1, RCK) is a prototypic component of P-(rocessing) bodies in cells ranging from yeast to human. Previously, we have shown that it is also a component of the large cytoplasmic polyadenylation element-binding protein translation repressor complex in Xenopus oocytes and that when tethered to the 3′ untranslated region, Xp54 represses reporter mRNA translation. Here, we examine the role of the p54 helicase activity in translational repression and in P-body formation. Mutagenesis of conserved p54 helicase motifs activates translation in the tethered func

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Fastenau, Caitlyn, Helen Cifuentes, Grant Kauwe, and Tara Tracy. "THE ROLE OF CAPRIN-1 PROTEIN DYSREGULATION IN SYNAPSE DECLINE LEADING TO PROGRESSION OF TAUOPATHIES." Innovation in Aging 3, Supplement_1 (2019): S835—S836. http://dx.doi.org/10.1093/geroni/igz038.3078.

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Abstract Many neurodegenerative diseases are characterized by accumulation of proteins such as tau, a microtubule stabilization protein. Toxic tau forms tangles and affects neuronal synapse function, an early step of neurodegeneration. To focus on synapse function, we highlighted Caprin-1 protein. Through gene ontology, Caprin-1 is related to RNA granule proteins, important for transport and local translation in dendrites. Caprin-1 is of interest for neurodegeneration because it is a memory related protein, transports mRNA in RNA granules, and knock out mice demonstrate memory deficits. As we

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Toki, Naoko, Hazuki Takahashi, Harshita Sharma, et al. "SINEUP long non-coding RNA acts via PTBP1 and HNRNPK to promote translational initiation assemblies." Nucleic Acids Research 48, no. 20 (2020): 11626–44. http://dx.doi.org/10.1093/nar/gkaa814.

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Abstract SINEUPs are long non-coding RNAs (lncRNAs) that contain a SINE element, and which up-regulate the translation of target mRNA. They have been studied in a wide range of applications, as both biological and therapeutic tools, although the underpinning molecular mechanism is unclear. Here, we focused on the sub-cellular distribution of target mRNAs and SINEUP RNAs, performing co-transfection of expression vectors for these transcripts into human embryonic kidney cells (HEK293T/17), to investigate the network of translational regulation. The results showed that co-localization of target m

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Reznik, Boris, and Jens Lykke-Andersen. "Regulated and quality-control mRNA turnover pathways in eukaryotes." Biochemical Society Transactions 38, no. 6 (2010): 1506–10. http://dx.doi.org/10.1042/bst0381506.

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Gene expression can be regulated at multiple levels, including transcription, RNA processing, RNA localization, translation and, finally, RNA turnover. RNA degradation may occur at points along the processing pathway or during translation as it undergoes quality control by RNA surveillance systems. Alternatively, mRNAs may be subject to regulated degradation, often mediated by cis-encoded determinants in the mRNA sequence that, through the recruitment of trans factors, determine the fate of the mRNA. The aim of the present review is to highlight mechanisms of regulated and quality-control RNA

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Ji, Yingbiao, and Alexei V. Tulin. "Poly(ADP-Ribosyl)ation of hnRNP A1 Protein Controls Translational Repression in Drosophila." Molecular and Cellular Biology 36, no. 19 (2016): 2476–86. http://dx.doi.org/10.1128/mcb.00207-16.

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Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins (hnRNPs) regulates the posttranscriptional fate of RNA during development.DrosophilahnRNP A1, Hrp38, is required for germ line stem cell maintenance and oocyte localization. The mRNA targets regulated by Hrp38 are mostly unknown. We identified 428 Hrp38-associated gene transcripts in the fly ovary, including mRNA of the translational repressor Nanos. We found that Hrp38 binds to the 3′ untranslated region (UTR) of Nanos mRNA, which contains a translation control element. We have demonstrated that translation of the luciferase r

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van Eeden, Fredericus J. M., Isabel M. Palacios, Mark Petronczki, Matthew J. D. Weston, and Daniel St Johnston. "Barentsz is essential for the posterior localization of oskar mRNA and colocalizes with it to the posterior pole." Journal of Cell Biology 154, no. 3 (2001): 511–24. http://dx.doi.org/10.1083/jcb.200105056.

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The localization of Oskar at the posterior pole of the Drosophila oocyte induces the assembly of the pole plasm and therefore defines where the abdomen and germ cells form in the embryo. This localization is achieved by the targeting of oskar mRNA to the posterior and the localized activation of its translation. oskar mRNA seems likely to be actively transported along microtubules, since its localization requires both an intact microtubule cytoskeleton and the plus end–directed motor kinesin I, but nothing is known about how the RNA is coupled to the motor. Here, we describe barentsz, a novel

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Ohashi and Shiina. "Cataloguing and Selection of mRNAs Localized to Dendrites in Neurons and Regulated by RNA-Binding Proteins in RNA Granules." Biomolecules 10, no. 2 (2020): 167. http://dx.doi.org/10.3390/biom10020167.

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Spatiotemporal translational regulation plays a key role in determining cell fate and function. Specifically, in neurons, local translation in dendrites is essential for synaptic plasticity and long-term memory formation. To achieve local translation, RNA-binding proteins in RNA granules regulate target mRNA stability, localization, and translation. To date, mRNAs localized to dendrites have been identified by comprehensive analyses. In addition, mRNAs associated with and regulated by RNA-binding proteins have been identified using various methods in many studies. However, the results obtained

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Child, Jessica R., Qiang Chen, David W. Reid, Sujatha Jagannathan, and Christopher V. Nicchitta. "Recruitment of endoplasmic reticulum-targeted and cytosolic mRNAs into membrane-associated stress granules." RNA 27, no. 10 (2021): 1241–56. http://dx.doi.org/10.1261/rna.078858.121.

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Stress granules (SGs) are membraneless organelles composed of mRNAs and RNA binding proteins which undergo assembly in response to stress-induced inactivation of translation initiation. In general, SG recruitment is limited to a subpopulation of a given mRNA species and RNA-seq analyses of purified SGs revealed that signal sequence-encoding (i.e., endoplasmic reticulum [ER]-targeted) transcripts are significantly underrepresented, consistent with prior reports that ER localization can protect mRNAs from SG recruitment. Using translational profiling, cell fractionation, and single molecule mRNA

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Lee, K., M. A. Fajardo, and R. E. Braun. "A testis cytoplasmic RNA-binding protein that has the properties of a translational repressor." Molecular and Cellular Biology 16, no. 6 (1996): 3023–34. http://dx.doi.org/10.1128/mcb.16.6.3023.

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Translation of the mouse protamine 1 (Prm-1) mRNA is repressed for several days during male germ cell differentiation. With the hope of cloning genes that regulate the translational repression of Prm-1, we screened male germ cell cDNA expression libraries with the 3' untranslated region of the Prm-1 RNA. From this screen we obtained two independent clones that encode Prbp, a Prm-1 RNA-binding protein. Prbp contains two copies of a double-stranded-RNA-binding domain. In vitro, the protein binds to a portion of the Prm-1 3' untranslated region previously shown to be sufficient for translational

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Isoyama, Takeshi, Nobuhiko Kamoshita, Kotaro Yasui, et al. "Lower concentration of La protein required for internal ribosome entry on hepatitis C virus RNA than on poliovirus RNA." Journal of General Virology 80, no. 9 (1999): 2319–27. http://dx.doi.org/10.1099/0022-1317-80-9-2319.

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Translation initiation of poliovirus and hepatitis C virus (HCV) RNA occurs by entry of ribosomes to the internal RNA sequence, called the internal ribosomal entry site (IRES). Both IRES bind to the La protein and are thought to require the protein for their translation initiation activity, although they are greatly different in both the primary and predicted secondary structures. To compare the La protein requirement for these IRES, we took advantage of I-RNA from the yeast Saccharomyces cerevisiae, which has been reported to bind to La protein and block poliovirus IRES-mediated translation i

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Makeeva, Desislava S., Claire L. Riggs, Anton V. Burakov, et al. "Relocalization of Translation Termination and Ribosome Recycling Factors to Stress Granules Coincides with Elevated Stop-Codon Readthrough and Reinitiation Rates upon Oxidative Stress." Cells 12, no. 2 (2023): 259. http://dx.doi.org/10.3390/cells12020259.

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Upon oxidative stress, mammalian cells rapidly reprogram their translation. This is accompanied by the formation of stress granules (SGs), cytoplasmic ribonucleoprotein condensates containing untranslated mRNA molecules, RNA-binding proteins, 40S ribosomal subunits, and a set of translation initiation factors. Here we show that arsenite-induced stress causes a dramatic increase in the stop-codon readthrough rate and significantly elevates translation reinitiation levels on uORF-containing and bicistronic mRNAs. We also report the recruitment of translation termination factors eRF1 and eRF3, as

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Pedder, Christopher M., Dianne Ford, and John E. Hesketh. "Targeting of transcripts encoding membrane proteins in polarized epithelia: RNA–protein binding studies of the SGLT1 3′-UTR." Biochemical Society Transactions 36, no. 3 (2008): 525–27. http://dx.doi.org/10.1042/bst0360525.

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mRNA stability, mRNA translation and spatial localization of mRNA species within a cell can be governed by signals in the 3′-UTR (3′-untranslated region). Local translation of proteins is essential for the development of many eukaryotic cell types, such as the Drosophila embryo, where the spatial and temporal localization of bicoid and gurken mRNAs, among others, is required to establish morphogen gradients. More recent studies have suggested that mRNA localization also occurs with transcripts coding for membrane-based or secreted proteins, and that localization at organelles such as the endop

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Chouaib, Racha, Adham Safieddine, Xavier Pichon, et al. "A Dual Protein-mRNA Localization Screen Reveals Compartmentalized Translation and Widespread Co-translational RNA Targeting." Developmental Cell 54, no. 6 (2020): 773–91. http://dx.doi.org/10.1016/j.devcel.2020.07.010.

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Jansova, Denisa, Anna Tetkova, Marketa Koncicka, Michal Kubelka, and Andrej Susor. "Localization of RNA and translation in the mammalian oocyte and embryo." PLOS ONE 13, no. 3 (2018): e0192544. http://dx.doi.org/10.1371/journal.pone.0192544.

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Peculis, B. A., and J. G. Gall. "Localization of the nucleolar protein NO38 in amphibian oocytes." Journal of Cell Biology 116, no. 1 (1992): 1–14. http://dx.doi.org/10.1083/jcb.116.1.1.

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To examine the role of primary amino acid sequence in the localization of proteins within the nucleus, we studied the nucleolar protein NO38 of amphibian oocytes. We synthesized NO38 transcripts in vitro, injected them into the oocyte cytoplasm, and followed the distribution of the translation products. The injected RNA contained a short sequence encoding an epitope derived from the human c-myc protein. We used an mAb against this epitope to detect translation products from injected RNAs by Western blots and by immunofluoresent staining of cytological preparations. When full-length transcripts

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Nakamura, Akira, Reiko Amikura, Kazuko Hanyu, and Satoru Kobayashi. "Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex duringDrosophilaoogenesis." Development 128, no. 17 (2001): 3233–42. http://dx.doi.org/10.1242/dev.128.17.3233.

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Embryonic patterning in Drosophila is regulated by maternal factors. Many such factors become localized as mRNAs within the oocyte during oogenesis and are translated in a spatio-temporally regulated manner. These processes are controlled by trans-acting proteins, which bind to the target RNAs to form a ribonucleoprotein (RNP) complex. We report that a DEAD-box protein, Me31B, forms a cytoplasmic RNP complex with oocyte-localizing RNAs and Exuperantia, a protein involved in RNA localization. During early oogenesis, loss of Me31B causes premature translation of oocyte-localizing RNAs within nur

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Kraut-Cohen, Judith, Evgenia Afanasieva, Liora Haim-Vilmovsky, et al. "Translation- and SRP-independent mRNA targeting to the endoplasmic reticulum in the yeast Saccharomyces cerevisiae." Molecular Biology of the Cell 24, no. 19 (2013): 3069–84. http://dx.doi.org/10.1091/mbc.e13-01-0038.

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mRNAs encoding secreted/membrane proteins (mSMPs) are believed to reach the endoplasmic reticulum (ER) in a translation-dependent manner to confer protein translocation. Evidence exists, however, for translation- and signal recognition particle (SRP)–independent mRNA localization to the ER, suggesting that there are alternate paths for RNA delivery. We localized endogenously expressed mSMPs in yeast using an aptamer-based RNA-tagging procedure and fluorescence microscopy. Unlike mRNAs encoding polarity and secretion factors that colocalize with cortical ER at the bud tip, mSMPs and mRNAs encod

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Gray, Nicola K., Lenka Hrabálková, Jessica P. Scanlon, and Richard W. P. Smith. "Poly(A)-binding proteins and mRNA localization: who rules the roost?" Biochemical Society Transactions 43, no. 6 (2015): 1277–84. http://dx.doi.org/10.1042/bst20150171.

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RNA-binding proteins are often multifunctional, interact with a variety of protein partners and display complex localizations within cells. Mammalian cytoplasmic poly(A)-binding proteins (PABPs) are multifunctional RNA-binding proteins that regulate multiple aspects of mRNA translation and stability. Although predominantly diffusely cytoplasmic at steady state, they shuttle through the nucleus and can be localized to a variety of cytoplasmic foci, including those associated with mRNA storage and localized translation. Intriguingly, PABP sub-cellular distribution can alter dramatically in respo

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Yasuda, Kyota, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G. Macara, and Stavroula Mili. "The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules." Journal of Cell Biology 203, no. 5 (2013): 737–46. http://dx.doi.org/10.1083/jcb.201306058.

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RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promot

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Saffman, Emma E., Sylvia Styhler, Katherine Rother, Weihua Li, Stéphane Richard, and Paul Lasko. "Premature Translation of oskar in Oocytes Lacking the RNA-Binding Protein Bicaudal-C." Molecular and Cellular Biology 18, no. 8 (1998): 4855–62. http://dx.doi.org/10.1128/mcb.18.8.4855.

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ABSTRACT Bicaudal-C (Bic-C) is required duringDrosophila melanogaster oogenesis for several processes, including anterior-posterior patterning. The gene encodes a protein with five copies of the KH domain, a motif found in a number of RNA-binding proteins. Using antibodies raised against the BIC-C protein, we show that multiple isoforms of the protein exist in ovaries and that the protein, like the RNA, accumulates in the developing oocyte early in oogenesis. BIC-C protein expressed in mammalian cells can bind RNA in vitro, and a point mutation in one of the KH domains that causes a strong Bic

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Evans Bergsten, S., T. Huang, S. Chatterjee, and E. R. Gavis. "Recognition and long-range interactions of a minimal nanos RNA localization signal element." Development 128, no. 3 (2001): 427–35. http://dx.doi.org/10.1242/dev.128.3.427.

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Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant elements within the nos 3′ untranslated region. We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2′ localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster an

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Shi, Yijiang, Joseph Gera, and Alan Lichtenstein. "Interleukin-6 (IL-6) Enhances C-MYC Translation IN MULTIPLE MYELOMA (MM) CELLS: ROLE of IL-6-INDUCED EFFECTS On the C-MYC RNA-Binding PROTEIN, HNRNPA1." Blood 114, no. 22 (2009): 3839. http://dx.doi.org/10.1182/blood.v114.22.3839.3839.

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Abstract Abstract 3839 Poster Board III-775 Our previous work (Cancer Research 68:10215, 2008) demonstrated that IL-6 enhanced c-myc protein expression in MM cells and function of the RNA-binding protein, hnRNPA1 (A1), was required. This occurred by way of enhanced cap-independent translation mediated via the internal ribosome entry site (IRES) in the 5'UTR of the myc RNA. IRES-dependent translation is the fail safe mechanism for protein expression when cap-dependent translation is suppressed by mTOR inhibition (with curtailed RNA cap-ribosome binding) and is especially important when an mRNA

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Fernández-Moya, Sandra M., Janina Ehses, Karl E. Bauer, et al. "RGS4 RNA Secondary Structure Mediates Staufen2 RNP Assembly in Neurons." International Journal of Molecular Sciences 22, no. 23 (2021): 13021. http://dx.doi.org/10.3390/ijms222313021.

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RNA-binding proteins (RBPs) act as posttranscriptional regulators controlling the fate of target mRNAs. Unraveling how RNAs are recognized by RBPs and in turn are assembled into neuronal RNA granules is therefore key to understanding the underlying mechanism. While RNA sequence elements have been extensively characterized, the functional impact of RNA secondary structures is only recently being explored. Here, we show that Staufen2 binds complex, long-ranged RNA hairpins in the 3′-untranslated region (UTR) of its targets. These structures are involved in the assembly of Staufen2 into RNA granu

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Blanco-Urrejola, Maite, Adhara Gaminde-Blasco, María Gamarra, et al. "RNA Localization and Local Translation in Glia in Neurological and Neurodegenerative Diseases: Lessons from Neurons." Cells 10, no. 3 (2021): 632. http://dx.doi.org/10.3390/cells10030632.

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Cell polarity is crucial for almost every cell in our body to establish distinct structural and functional domains. Polarized cells have an asymmetrical morphology and therefore their proteins need to be asymmetrically distributed to support their function. Subcellular protein distribution is typically achieved by localization peptides within the protein sequence. However, protein delivery to distinct cellular compartments can rely, not only on the transport of the protein itself but also on the transport of the mRNA that is then translated at target sites. This phenomenon is known as local pr

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Islam, Shabana, Robert K. Montgomery, John J. Fialkovich, and Richard J. Grand. "Developmental and Regional Expression and Localization of mRNAs Encoding Proteins Involved in RNA Translocation." Journal of Histochemistry & Cytochemistry 53, no. 12 (2005): 1501–9. http://dx.doi.org/10.1369/jhc.5a6655.2005.

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RNA localization is a regulated component of gene expression of fundamental importance in development and differentiation. Several RNA binding proteins involved in RNA localization during development in Drosophila have been identified, of which Y14, Mago, Pumilio, and IMP-1 are known to be expressed in adult mammalian intestine. The present study was undertaken to define the developmental and regional expression of these proteins, as well as Staufen-1, in mouse intestinal cells and in other tissues and cell lines using RT-PCR, and localization using in situ hybridization and immunohistochemist

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Gao, Yuanhui, Hui Cao, Denggao Huang, Linlin Zheng, Zhenyu Nie, and Shufang Zhang. "RNA-Binding Proteins in Bladder Cancer." Cancers 15, no. 4 (2023): 1150. http://dx.doi.org/10.3390/cancers15041150.

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RNA-binding proteins (RBPs) are key regulators of transcription and translation, with highly dynamic spatio-temporal regulation. They are usually involved in the regulation of RNA splicing, polyadenylation, and mRNA stability and mediate processes such as mRNA localization and translation, thereby affecting the RNA life cycle and causing the production of abnormal protein phenotypes that lead to tumorigenesis and development. Accumulating evidence supports that RBPs play critical roles in vital life processes, such as bladder cancer initiation, progression, metastasis, and drug resistance. Unc

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Lie, Y. S., and P. M. Macdonald. "Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation." Development 126, no. 6 (1999): 1129–38. http://dx.doi.org/10.1242/dev.126.6.1129.

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The product of the oskar gene directs posterior patterning in the Drosophila oocyte, where it must be deployed specifically at the posterior pole. Proper expression relies on the coordinated localization and translational control of the oskar mRNA. Translational repression prior to localization of the transcript is mediated, in part, by the Bruno protein, which binds to discrete sites in the 3′ untranslated region of the oskar mRNA. To begin to understand how Bruno acts in translational repression, we performed a yeast two-hybrid screen to identify Bruno-interacting proteins. One interactor, d

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Jansova, Denisa, Daria Aleshkina, Anna Jindrova, et al. "Single Molecule RNA Localization and Translation in the Mammalian Oocyte and Embryo." Journal of Molecular Biology 433, no. 19 (2021): 167166. http://dx.doi.org/10.1016/j.jmb.2021.167166.

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Nicchitta, Christopher V., Rachel S. Lerner, Samuel B. Stephens, Rebecca D. Dodd, and Brook Pyhtila. "Pathways for compartmentalizing protein synthesis in eukaryotic cells: the template-partitioning model." Biochemistry and Cell Biology 83, no. 6 (2005): 687–95. http://dx.doi.org/10.1139/o05-147.

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mRNAs encoding signal sequences are translated on endoplasmic reticulum (ER) - bound ribosomes, whereas mRNAs encoding cytosolic proteins are translated on cytosolic ribosomes. The partitioning of mRNAs to the ER occurs by positive selection; cytosolic ribosomes engaged in the translation of signal-sequence-bearing proteins are engaged by the signal-recognition particle (SRP) pathway and subsequently trafficked to the ER. Studies have demonstrated that, in addition to the SRP pathway, mRNAs encoding cytosolic proteins can also be partitioned to the ER, suggesting that RNA partitioning in the e

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Sawicka, Kirsty, Martin Bushell, Keith A. Spriggs, and Anne E. Willis. "Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein." Biochemical Society Transactions 36, no. 4 (2008): 641–47. http://dx.doi.org/10.1042/bst0360641.

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PTB (polypyrimidine-tract-binding protein) is a ubiquitous RNA-binding protein. It was originally identified as a protein with a role in splicing but it is now known to function in a large number of diverse cellular processes including polyadenylation, mRNA stability and translation initiation. Specificity of PTB function is achieved by a combination of changes in the cellular localization of this protein (its ability to shuttle from the nucleus to the cytoplasm is tightly controlled) and its interaction with additional proteins. These differences in location and trans-acting factor requiremen

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Kashida, Shunnichi, Dan Ohtan Wang, Hirohide Saito, and Zoher Gueroui. "Nanoparticle-based local translation reveals mRNA as a translation-coupled scaffold with anchoring function." Proceedings of the National Academy of Sciences 116, no. 27 (2019): 13346–51. http://dx.doi.org/10.1073/pnas.1900310116.

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The spatial regulation of messenger RNA (mRNA) translation is central to cellular functions and relies on numerous complex processes. Biomimetic approaches could bypass these endogenous complex processes, improve our comprehension of the regulation, and allow for controlling local translation regulations and functions. However, the causality between local translation and nascent protein function remains elusive. Here, we developed a nanoparticle (NP)-based strategy to magnetically control mRNA spatial patterns in mammalian cell extracts and investigate how local translation impacts nascent pro

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Markussen, F. H., A. M. Michon, W. Breitwieser, and A. Ephrussi. "Translational control of oskar generates short OSK, the isoform that induces pole plasma assembly." Development 121, no. 11 (1995): 3723–32. http://dx.doi.org/10.1242/dev.121.11.3723.

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At the posterior pole of the Drosophila oocyte, oskar induces a tightly localized assembly of pole plasm. This spatial restriction of oskar activity has been thought to be achieved by the localization of oskar mRNA, since mislocalization of the RNA to the anterior induces anterior pole plasm. However, ectopic pole plasm does not form in mutant ovaries where oskar mRNA is not localized, suggesting that the unlocalized mRNA is inactive. As a first step towards understanding how oskar activity is restricted to the posterior pole, we analyzed oskar translation in wild type and mutants. We show tha

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