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Thematische Bibliographien / RNP granule / Zeitschriftenartikel

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Zeitschriftenartikel zum Thema „RNP granule“

Autor: Grafiati

Veröffentlicht am 24. Juni 2021

Zuletzt aktualisiert am 29. Juli 2025

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1

Krüger, Timothy, Mario Hofweber, and Susanne Kramer. "SCD6 induces ribonucleoprotein granule formation in trypanosomes in a translation-independent manner, regulated by its Lsm and RGG domains." Molecular Biology of the Cell 24, no. 13 (2013): 2098–111. http://dx.doi.org/10.1091/mbc.e13-01-0068.

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Ribonucleoprotein (RNP) granules are cytoplasmic, microscopically visible structures composed of RNA and protein with proposed functions in mRNA decay and storage. Trypanosomes have several types of RNP granules, but lack most of the granule core components identified in yeast and humans. The exception is SCD6/Rap55, which is essential for processing body (P-body) formation. In this study, we analyzed the role of trypanosome SCD6 in RNP granule formation. Upon overexpression, the majority of SCD6 aggregates to multiple granules enriched at the nuclear periphery that recruit both P-body and str

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Perelman, Rebecca T., Andreas Schmidt, Umar Khan, and Nils G. Walter. "Spontaneous Confinement of mRNA Molecules at Biomolecular Condensate Boundaries." Cells 12, no. 18 (2023): 2250. http://dx.doi.org/10.3390/cells12182250.

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Cellular biomolecular condensates, termed ribonucleoprotein (RNP) granules, are often enriched in messenger RNA (mRNA) molecules relative to the surrounding cytoplasm. Yet, the spatial localization and diffusion of mRNAs in close proximity to phase separated RNP granules are not well understood. In this study, we performed single-molecule fluorescence imaging experiments of mRNAs in live cells in the presence of two types of RNP granules, stress granules (SGs) and processing bodies (PBs), which are distinct in their molecular composition and function. We developed a photobleaching- and noise-c

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Aoki, Scott T., Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. "PGL germ granule assembly protein is a base-specific, single-stranded RNase." Proceedings of the National Academy of Sciences 113, no. 5 (2016): 1279–84. http://dx.doi.org/10.1073/pnas.1524400113.

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Cellular RNA-protein (RNP) granules are ubiquitous and have fundamental roles in biology and RNA metabolism, but the molecular basis of their structure, assembly, and function is poorly understood. Using nematode “P-granules” as a paradigm, we focus on the PGL granule scaffold protein to gain molecular insights into RNP granule structure and assembly. We first identify a PGL dimerization domain (DD) and determine its crystal structure. PGL-1 DD has a novel 13 α-helix fold that creates a positively charged channel as a homodimer. We investigate its capacity to bind RNA and discover unexpectedly

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Davis, Michael, Andrea Montalbano, Megan P. Wood, and Jennifer A. Schisa. "Biphasic adaptation to osmotic stress in the C. elegans germ line." American Journal of Physiology-Cell Physiology 312, no. 6 (2017): C741—C748. http://dx.doi.org/10.1152/ajpcell.00364.2016.

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Cells respond to environmental stress in multiple ways. In the germ line, heat shock and nutritive stress trigger the assembly of large ribonucleoprotein (RNP) granules via liquid-liquid phase separation (LLPS). The RNP granules are hypothesized to maintain the quality of oocytes during stress. The goal of this study was to investigate the cellular response to glucose in the germ line and determine if it is an osmotic stress response. We found that exposure to 500 mM glucose induces the assembly of RNP granules in the germ line within 1 h. Interestingly, the RNP granules are maintained for up

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Hanazawa, Momoyo, Masafumi Yonetani, and Asako Sugimoto. "PGL proteins self associate and bind RNPs to mediate germ granule assembly in C. elegans." Journal of Cell Biology 192, no. 6 (2011): 929–37. http://dx.doi.org/10.1083/jcb.201010106.

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Germ granules are germ lineage–specific ribonucleoprotein (RNP) complexes, but how they are assembled and specifically segregated to germ lineage cells remains unclear. Here, we show that the PGL proteins PGL-1 and PGL-3 serve as the scaffold for germ granule formation in Caenorhabditis elegans. Using cultured mammalian cells, we found that PGL proteins have the ability to self-associate and recruit RNPs. Depletion of PGL proteins from early C. elegans embryos caused dispersal of other germ granule components in the cytoplasm, suggesting that PGL proteins are essential for the architecture of

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Moon, Sungjin, and Sim Namkoong. "Ribonucleoprotein Granules: Between Stress and Transposable Elements." Biomolecules 13, no. 7 (2023): 1027. http://dx.doi.org/10.3390/biom13071027.

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Transposable elements (TEs) are DNA sequences that can transpose and replicate within the genome, leading to genetic changes that affect various aspects of host biology. Evolutionarily, hosts have also developed molecular mechanisms to suppress TEs at the transcriptional and post-transcriptional levels. Recent studies suggest that stress-induced formation of ribonucleoprotein (RNP) granules, including stress granule (SG) and processing body (P-body), can play a role in the sequestration of TEs to prevent transposition, suggesting an additional layer of the regulatory mechanism for TEs. RNP gra

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An, Haiyan, Jing Tong Tan, and Tatyana A. Shelkovnikova. "Stress granules regulate stress-induced paraspeckle assembly." Journal of Cell Biology 218, no. 12 (2019): 4127–40. http://dx.doi.org/10.1083/jcb.201904098.

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Eukaryotic cells contain a variety of RNA-protein macrocomplexes termed RNP granules. Different types of granules share multiple protein components; however, the crosstalk between spatially separated granules remains unaddressed. Paraspeckles and stress granules (SGs) are prototypical RNP granules localized exclusively in the nucleus and cytoplasm, respectively. Both granules are implicated in human diseases, such as amyotrophic lateral sclerosis. We characterized the composition of affinity-purified paraspeckle-like structures and found a significant overlap between the proteomes of paraspeck

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Ripin, Nina, and Roy Parker. "Are stress granules the RNA analogs of misfolded protein aggregates?" RNA 28, no. 1 (2021): 67–75. http://dx.doi.org/10.1261/rna.079000.121.

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Ribonucleoprotein granules are ubiquitous features of eukaryotic cells. Several observations argue that the formation of at least some RNP granules can be considered analogous to the formation of unfolded protein aggregates. First, unfolded protein aggregates form from the exposure of promiscuous protein interaction surfaces, while some mRNP granules form, at least in part, by promiscuous intermolecular RNA–RNA interactions due to exposed RNA surfaces when mRNAs are not engaged with ribosomes. Second, analogous to the role of protein chaperones in preventing misfolded protein aggregation, cell

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Zhang, Haidao, Ekaterina Kapitonova, Adriana Orrego, Christos Spanos, Joanna Strachan, and Elizabeth H. Bayne. "Fission yeast Caprin protein is required for efficient heterochromatin establishment." PLOS Genetics 21, no. 3 (2025): e1011620. https://doi.org/10.1371/journal.pgen.1011620.

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Heterochromatin is a key feature of eukaryotic genomes that serves important regulatory and structural roles in regions such as centromeres. In fission yeast, maintenance of existing heterochromatic domains relies on positive feedback loops involving histone methylation and non-coding RNAs. However, requirements for de novo establishment of heterochromatin are less well understood. Here, through a cross-based assay we have identified a novel factor influencing the efficiency of heterochromatin establishment. We determine that the previously uncharacterised protein is an ortholog of human Capri

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De Graeve, Fabienne, and Florence Besse. "Neuronal RNP granules: from physiological to pathological assemblies." Biological Chemistry 399, no. 7 (2018): 623–35. http://dx.doi.org/10.1515/hsz-2018-0141.

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Abstract Neuronal cells rely on macro- and micro-cellular compartmentalization to rapidly process information, and respond locally to external stimuli. Such a cellular organization is achieved via the assembly of neuronal ribonucleoprotein (RNP) granules, dynamic membrane-less organelles enriched in RNAs and associated regulatory proteins. In this review, we discuss how these high-order structures transport mRNAs to dendrites and axons, and how they contribute to the spatio-temporal regulation of localized mRNA translation. We also highlight how recent biophysical studies have shed light on th

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An, Haiyan, and Tatyana A. Shelkovnikova. "Stress granules regulate paraspeckles: RNP granule continuum at work." Cell Stress 3, no. 12 (2019): 385–87. http://dx.doi.org/10.15698/cst2019.12.207.

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12

Van Treeck, Briana, David S. W. Protter, Tyler Matheny, Anthony Khong, Christopher D. Link, and Roy Parker. "RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome." Proceedings of the National Academy of Sciences 115, no. 11 (2018): 2734–39. http://dx.doi.org/10.1073/pnas.1800038115.

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Stress granules are higher order assemblies of nontranslating mRNAs and proteins that form when translation initiation is inhibited. Stress granules are thought to form by protein–protein interactions of RNA-binding proteins. We demonstrate RNA homopolymers or purified cellular RNA forms assemblies in vitro analogous to stress granules. Remarkably, under conditions representative of an intracellular stress response, the mRNAs enriched in assemblies from total yeast RNA largely recapitulate the stress granule transcriptome. We suggest stress granules are formed by a summation of protein–protein

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Ahmad, Adam, Yoel Bogoch, Gal Shvaizer, Noga Guler, Karine Levy, and Yaniv M. Elkouby. "The piRNA protein Asz1 is essential for germ cell and gonad development in zebrafish and exhibits differential necessities in distinct types of germ granules." PLOS Genetics 21, no. 1 (2025): e1010868. https://doi.org/10.1371/journal.pgen.1010868.

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Germ cells are essential for fertility, embryogenesis, and reproduction. Germline development requires distinct types of germ granules, which contains RNA-protein (RNP) complexes, including germ plasm in embryos, piRNA granules in gonadal germ cells, and the Balbiani body (Bb) in oocytes. However, the regulation of RNP assemblies in zebrafish germline development are still poorly understood. Asz1 is a piRNA protein in Drosophila and mice. Zebrafish Asz1 localizes to both piRNA and Bb granules, with yet unknown functions. Here, we hypothesized that Asz1 functions in germ granules and germline d

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Corbet, Giulia Ada, and Roy Parker. "RNP Granule Formation: Lessons from P-Bodies and Stress Granules." Cold Spring Harbor Symposia on Quantitative Biology 84 (2019): 203–15. http://dx.doi.org/10.1101/sqb.2019.84.040329.

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15

Lyonnais, Sébastien, S. Kashif Sadiq, Cristina Lorca-Oró, et al. "The HIV-1 Nucleocapsid Regulates Its Own Condensation by Phase-Separated Activity-Enhancing Sequestration of the Viral Protease during Maturation." Viruses 13, no. 11 (2021): 2312. http://dx.doi.org/10.3390/v13112312.

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A growing number of studies indicate that mRNAs and long ncRNAs can affect protein populations by assembling dynamic ribonucleoprotein (RNP) granules. These phase-separated molecular ‘sponges’, stabilized by quinary (transient and weak) interactions, control proteins involved in numerous biological functions. Retroviruses such as HIV-1 form by self-assembly when their genomic RNA (gRNA) traps Gag and GagPol polyprotein precursors. Infectivity requires extracellular budding of the particle followed by maturation, an ordered processing of ∼2400 Gag and ∼120 GagPol by the viral protease (PR). Thi

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Abolhassani-Dadras, S., G. H. Vázquez-Nin, O. M. Echeverría, and S. Fakan. "The use of an internal standard in the application of quantitative image-EELS in biology." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 50–51. http://dx.doi.org/10.1017/s0424820100162715.

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The energy filtering transmission electron microscope (EFTEM) is employed to examine the possibility of using ribosomes as internal standard for a quantitative in-situ study of phosphorus content of nuclear constituents in a biological section. The problems that can arise from different steps of such an experimental approach are discussed.Salivary gland cells from fourth instar larvae of Chironomus thummi are selected as test specimens because of their appropriate structure. The nucleus of these cells contains two types of granules, one of which (known as Balbiani ring granule, Brg) has an RNA

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Noble, Scott L., Brittany L. Allen, Lai Kuan Goh, Kristen Nordick, and Thomas C. Evans. "Maternal mRNAs are regulated by diverse P body–related mRNP granules during early Caenorhabditis elegans development." Journal of Cell Biology 182, no. 3 (2008): 559–72. http://dx.doi.org/10.1083/jcb.200802128.

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Processing bodies (P bodies) are conserved mRNA–protein (mRNP) granules that are thought to be cytoplasmic centers for mRNA repression and degradation. However, their specific functions in vivo remain poorly understood. We find that repressed maternal mRNAs and their regulators localize to P body–like mRNP granules in the Caenorhabditis elegans germ line. Surprisingly, several distinct types of regulated granules form during oocyte and embryo development. 3′ untranslated region elements direct mRNA targeting to one of these granule classes. The P body factor CAR-1/Rap55 promotes association of

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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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Kim, Younghoon, Christian Eckmann, Clifford P. Brangwynne, and Sua Myong. "DEAD Box Helicases in Rnp Granule." Biophysical Journal 106, no. 2 (2014): 71a. http://dx.doi.org/10.1016/j.bpj.2013.11.471.

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Hakes, Anna C., and Elizabeth R. Gavis. "Plasticity of Drosophila germ granules during germ cell development." PLOS Biology 21, no. 4 (2023): e3002069. http://dx.doi.org/10.1371/journal.pbio.3002069.

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Compartmentalization of RNAs and proteins into membraneless structures called granules is a ubiquitous mechanism for organizing and regulating cohorts of RNAs. Germ granules are ribonucleoprotein (RNP) assemblies required for germline development across the animal kingdom, but their regulatory roles in germ cells are not fully understood. We show that after germ cell specification, Drosophila germ granules enlarge through fusion and this growth is accompanied by a shift in function. Whereas germ granules initially protect their constituent mRNAs from degradation, they subsequently target a sub

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Tauber, Devin, Gabriel Tauber, and Roy Parker. "Mechanisms and Regulation of RNA Condensation in RNP Granule Formation." Trends in Biochemical Sciences 45, no. 9 (2020): 764–78. http://dx.doi.org/10.1016/j.tibs.2020.05.002.

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Burke, James M., Evan T. Lester, Devin Tauber, and Roy Parker. "RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules." Journal of Biological Chemistry 295, no. 6 (2020): 1426–38. http://dx.doi.org/10.1074/jbc.ra119.011638.

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Stress granules (SGs) are ribonucleoprotein (RNP) assemblies that form in eukaryotic cells as a result of limited translation in response to stress. SGs form during viral infection and are thought to promote the antiviral response because many viruses encode inhibitors of SG assembly. However, the antiviral endoribonuclease RNase L also alters SG formation, whereby only small punctate SG-like bodies that we term RNase L–dependent bodies (RLBs) form during RNase L activation. How RLBs relate to SGs and their mode of biogenesis is unknown. Herein, using immunofluorescence, live-cell imaging, and

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Petrauskas, Arnas, Daniel L. Fortunati, Arvind Reddy Kandi, et al. "Structured and disordered regions of Ataxin-2 contribute differently to the specificity and efficiency of mRNP granule formation." PLOS Genetics 20, no. 5 (2024): e1011251. http://dx.doi.org/10.1371/journal.pgen.1011251.

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Ataxin-2 (ATXN2) is a gene implicated in spinocerebellar ataxia type II (SCA2), amyotrophic lateral sclerosis (ALS) and Parkinsonism. The encoded protein is a therapeutic target for ALS and related conditions. ATXN2 (or Atx2 in insects) can function in translational activation, translational repression, mRNA stability and in the assembly of mRNP-granules, a process mediated by intrinsically disordered regions (IDRs). Previous work has shown that the LSm (Like-Sm) domain of Atx2, which can help stimulate mRNA translation, antagonizes mRNP-granule assembly. Here we advance these findings through

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Zhang, Yi, Jiayu Gu, and Qiming Sun. "Aberrant Stress Granule Dynamics and Aggrephagy in ALS Pathogenesis." Cells 10, no. 9 (2021): 2247. http://dx.doi.org/10.3390/cells10092247.

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Stress granules are conserved cytosolic ribonucleoprotein (RNP) compartments that undergo dynamic assembly and disassembly by phase separation in response to stressful conditions. Gene mutations may lead to aberrant phase separation of stress granules eliciting irreversible protein aggregations. A selective autophagy pathway called aggrephagy may partially alleviate the cytotoxicity mediated by these protein aggregates. Cells must perceive when and where the stress granules are transformed into toxic protein aggregates to initiate autophagosomal engulfment for subsequent autolysosomal degradat

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Ivanov, P. "RNP stress-granule formation is inhibited by microtubule disruption." Cell Biology International 27, no. 3 (2003): 207–8. http://dx.doi.org/10.1016/s1065-6995(02)00341-4.

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An, Haiyan, Camille Rabesahala de Meritens, and Tatyana A. Shelkovnikova. "Connecting the “dots”: RNP granule network in health and disease." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1868, no. 8 (2021): 119058. http://dx.doi.org/10.1016/j.bbamcr.2021.119058.

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Mittag, Tanja, and Roy Parker. "Multiple Modes of Protein–Protein Interactions Promote RNP Granule Assembly." Journal of Molecular Biology 430, no. 23 (2018): 4636–49. http://dx.doi.org/10.1016/j.jmb.2018.08.005.

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Lehtiniemi, Tiina, and Noora Kotaja. "Germ granule-mediated RNA regulation in male germ cells." Reproduction 155, no. 2 (2018): R77—R91. http://dx.doi.org/10.1530/rep-17-0356.

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Germ cells have exceptionally diverse transcriptomes. Furthermore, the progress of spermatogenesis is accompanied by dramatic changes in gene expression patterns, the most drastic of them being near-to-complete transcriptional silencing during the final steps of differentiation. Therefore, accurate RNA regulatory mechanisms are critical for normal spermatogenesis. Cytoplasmic germ cell-specific ribonucleoprotein (RNP) granules, known as germ granules, participate in posttranscriptional regulation in developing male germ cells. Particularly, germ granules provide platforms for the PIWI-interact

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Protter, David S. W., Bhalchandra S. Rao, Briana Van Treeck, et al. "Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly." Cell Reports 22, no. 6 (2018): 1401–12. http://dx.doi.org/10.1016/j.celrep.2018.01.036.

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Decker, Carolyn J., and Roy Parker. "CAR-1 and Trailer hitch: driving mRNP granule function at the ER?" Journal of Cell Biology 173, no. 2 (2006): 159–63. http://dx.doi.org/10.1083/jcb.200601153.

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The targeting of messenger RNAs (mRNAs) to specific subcellular sites for local translation plays an important role in diverse cellular and developmental processes in eukaryotes, including axis formation, cell fate determination, spindle pole regulation, cell motility, and neuronal synaptic plasticity. Recently, a new conserved class of Lsm proteins, the Scd6 family, has been implicated in controlling mRNA function. Depletion or mutation of members of the Scd6 family, Caenorhabditis elegans CAR-1 and Drosophila melanogaster trailer hitch, lead to a variety of developmental phenotypes, which in

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Nielsen, Finn C., Jacob Nielsen, Mette A. Kristensen, Grete Koch, and Jan Christiansen. "Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domains." Journal of Cell Science 115, no. 10 (2002): 2087–97. http://dx.doi.org/10.1242/jcs.115.10.2087.

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The IGF-II mRNA-binding proteins (IMPs), which are composed of two RNA recognition motifs, (RRM) and four hnRNP K homology (KH) domains, have been implicated in subcytoplasmic localization of mRNAs during embryogenesis. The IMP family originated via two gene duplications before the divergence of vertebrates, and IMP homologues consisting of only the four KH motifs have been identified in Drosophila and Caenorhabditis elegans. Here we characterise the trafficking of GFP-IMP1 fusion proteins and determine the structural determinants for proper cytoplasmic localization. GFP-IMP1 is present in lar

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Huang, S., T. J. Deerinck, M. H. Ellisman, and D. L. Spector. "In vivo analysis of the stability and transport of nuclear poly(A)+ RNA." Journal of Cell Biology 126, no. 4 (1994): 877–99. http://dx.doi.org/10.1083/jcb.126.4.877.

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We have studied the distribution of poly(A)+ RNA in the mammalian cell nucleus and its transport through nuclear pores by fluorescence and electron microscopic in situ hybridization. Poly(A)+ RNA was detected in the nucleus as a speckled pattern which includes interchromatin granule clusters and perichromatin fibrils. When cells are fractionated by detergent and salt extraction as well as DNase I digestion, the majority of the nuclear poly(A)+ RNA was found to remain associated with the nonchromatin RNP-enriched fraction of the nucleus. After inhibition of RNA polymerase II transcription for 5

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Hofweber, Mario, and Dorothee Dormann. "Friend or foe—Post-translational modifications as regulators of phase separation and RNP granule dynamics." Journal of Biological Chemistry 294, no. 18 (2018): 7137–50. http://dx.doi.org/10.1074/jbc.tm118.001189.

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Bakthavachalu, Baskar, Joern Huelsmeier, Indulekha P. Sudhakaran, et al. "RNP-Granule Assembly via Ataxin-2 Disordered Domains Is Required for Long-Term Memory and Neurodegeneration." Neuron 98, no. 4 (2018): 754–66. http://dx.doi.org/10.1016/j.neuron.2018.04.032.

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Percipalle, Piergiorgio, Jian Zhao, Brian Pope, Alan Weeds, Uno Lindberg, and Bertil Daneholt. "Actin Bound to the Heterogeneous Nuclear Ribonucleoprotein Hrp36 Is Associated with Balbiani Ring mRNA from the Gene to Polysomes." Journal of Cell Biology 153, no. 1 (2001): 229–36. http://dx.doi.org/10.1083/jcb.153.1.229.

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In the salivary glands of the dipteran Chironomus tentans, a specific messenger ribonucleoprotein (mRNP) particle, the Balbiani ring (BR) granule, can be visualized during its assembly on the gene and during its nucleocytoplasmic transport. We now show with immunoelectron microscopy that actin becomes associated with the BR particle concomitantly with transcription and is present in the particle in the nucleoplasm. DNase I affinity chromatography experiments with extracts from tissue culture cells indicate that both nuclear and cytoplasmic actin are bound to the heterogeneous RNP (hnRNP) prote

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Murakami, Tetsuro, Seema Qamar, Julie Qiaojin Lin, et al. "ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function." Neuron 88, no. 4 (2015): 678–90. http://dx.doi.org/10.1016/j.neuron.2015.10.030.

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Chukrallah, Lauren G., Sarah Potgieter, Lisa Chueh, and Elizabeth M. Snyder. "Two RNA binding proteins, ADAD2 and RNF17, interact to form a heterogeneous population of novel meiotic germ cell granules with developmentally dependent organelle association." PLOS Genetics 19, no. 7 (2023): e1010519. http://dx.doi.org/10.1371/journal.pgen.1010519.

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Mammalian male germ cell differentiation relies on complex RNA biogenesis events, many of which occur in non-membrane bound organelles termed RNA germ cell granules that are rich in RNA binding proteins (RBPs). Though known to be required for male germ cell differentiation, we understand little of the relationships between the numerous granule subtypes. ADAD2, a testis specific RBP, is required for normal male fertility and forms a poorly characterized granule in meiotic germ cells. This work aimed to understand the role of ADAD2 granules in male germ cell differentiation by clearly defining t

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Shorter, James, and J. Paul Taylor. "Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly." Rare Diseases 1, no. 1 (2013): e25200. http://dx.doi.org/10.4161/rdis.25200.

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Tian, Siran, Harrison A. Curnutte, and Tatjana Trcek. "RNA Granules: A View from the RNA Perspective." Molecules 25, no. 14 (2020): 3130. http://dx.doi.org/10.3390/molecules25143130.

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RNA granules are ubiquitous. Composed of RNA-binding proteins and RNAs, they provide functional compartmentalization within cells. They are inextricably linked with RNA biology and as such are often referred to as the hubs for post-transcriptional regulation. Much of the attention has been given to the proteins that form these condensates and thus many fundamental questions about the biology of RNA granules remain poorly understood: How and which RNAs enrich in RNA granules, how are transcripts regulated in them, and how do granule-enriched mRNAs shape the biology of a cell? In this review, we

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Lindquist, Michael E., Aaron W. Lifland, Thomas J. Utley, Philip J. Santangelo, and James E. Crowe. "Respiratory Syncytial Virus Induces Host RNA Stress Granules To Facilitate Viral Replication." Journal of Virology 84, no. 23 (2010): 12274–84. http://dx.doi.org/10.1128/jvi.00260-10.

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ABSTRACT Mammalian cell cytoplasmic RNA stress granules are induced during various conditions of stress and are strongly associated with regulation of host mRNA translation. Several viruses induce stress granules during the course of infection, but the exact function of these structures during virus replication is not well understood. In this study, we showed that respiratory syncytial virus (RSV) induced host stress granules in epithelial cells during the course of infection. We also showed that stress granules are distinct from cytoplasmic viral inclusion bodies and that the RNA binding prot

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Tatavarty, Vedakumar, Marius F. Ifrim, Mikhail Levin, et al. "Single-molecule imaging of translational output from individual RNA granules in neurons." Molecular Biology of the Cell 23, no. 5 (2012): 918–29. http://dx.doi.org/10.1091/mbc.e11-07-0622.

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Dendritic RNAs are localized and translated in RNA granules. Here we use single-molecule imaging to count the number of RNA molecules in each granule and to record translation output from each granule using Venus fluorescent protein as a reporter. For RNAs encoding activity-regulated cytoskeletal-associated protein (ARC) or fragile X mental retardation protein (FMRP), translation events are spatially clustered near individual granules, and translational output from individual granules is either sporadic or bursty. The probability of bursty translation is greater for Venus-FMRP RNA than for Ven

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Dougherty, M. K., C. Saul, L. Carman, M. D. Nelson, and J. C. Tudor. "0028 Sleep Duration Influences the Kinetics of Stress Granule Formation." Sleep 43, Supplement_1 (2020): A11—A12. http://dx.doi.org/10.1093/sleep/zsaa056.027.

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Abstract Introduction Stress granules are non-membrane bound aggregates of messenger ribonucleoproteins that are biomarkers of cellular stress. It has been shown in cells in vitro that suppression of the mammalian target of rapamycin (mTOR) pathway and its non-mammalian orthologue target of rapamycin (TOR) is associated with an increase in stress granule formation. It has also been shown that the mTOR pathway is suppressed in response to sleep deprivation in mice. Despite the possible connection via the TOR/mTOR pathway, there has not been any previous evidence linking sleep deprivation with s

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Moujaber, Ossama, and Ursula Stochaj. "Cytoplasmic RNA Granules in Somatic Maintenance." Gerontology 64, no. 5 (2018): 485–94. http://dx.doi.org/10.1159/000488759.

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Cytoplasmic RNA granules represent subcellular compartments that are enriched in protein-bound RNA species. RNA granules are produced by evolutionary divergent eukaryotes, including yeast, mammals, and plants. The functions of cytoplasmic RNA granules differ widely. They are dictated by the cell type and physiological state, which in turn is determined by intrinsic cell properties and environmental factors. RNA granules provide diverse cellular functions. However, all of the granules contribute to aspects of RNA metabolism. This is exemplified by transcription, RNA storage, silencing, and degr

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Hubstenberger, Arnaud, Cristiana Cameron, Scott L. Noble, Sean Keenan, and Thomas C. Evans. "Modifiers of solid RNP granules control normal RNP dynamics and mRNA activity in early development." Journal of Cell Biology 211, no. 3 (2015): 703–16. http://dx.doi.org/10.1083/jcb.201504044.

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Ribonucleoproteins (RNPs) often coassemble into supramolecular bodies with regulated dynamics. The factors controlling RNP bodies and connections to RNA regulation are unclear. During Caenorhabditis elegans oogenesis, cytoplasmic RNPs can transition among diffuse, liquid, and solid states linked to mRNA regulation. Loss of CGH-1/Ddx6 RNA helicase generates solid granules that are sensitive to mRNA regulators. Here, we identified 66 modifiers of RNP solids induced by cgh-1 mutation. A majority of genes promote or suppress normal RNP body assembly, dynamics, or metabolism. Surprisingly, polyaden

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Formicola, Nadia, Marjorie Heim, Jérémy Dufourt, et al. "Tyramine induces dynamic RNP granule remodeling and translation activation in the Drosophila brain." eLife 10 (April 23, 2021). http://dx.doi.org/10.7554/elife.65742.

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Ribonucleoprotein (RNP) granules are dynamic condensates enriched in regulatory RNA binding proteins (RBPs) and RNAs under tight spatiotemporal control. Extensive recent work has investigated the molecular principles underlying RNP granule assembly, unraveling that they form through the self-association of RNP components into dynamic networks of interactions. How endogenous RNP granules respond to external stimuli to regulate RNA fate is still largely unknown. Here, we demonstrate through high-resolution imaging of intact Drosophila brains that Tyramine induces a reversible remodeling of somat

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Chen, Ruoyu, William Stainier, Jeremy Dufourt, Mounia Lagha, and Ruth Lehmann. "Direct observation of translational activation by a ribonucleoprotein granule." Nature Cell Biology, July 4, 2024. http://dx.doi.org/10.1038/s41556-024-01452-5.

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AbstractBiomolecular condensates organize biochemical processes at the subcellular level and can provide spatiotemporal regulation within a cell. Among these, ribonucleoprotein (RNP) granules are storage hubs for translationally repressed mRNA. Whether RNP granules can also activate translation and how this could be achieved remains unclear. Here, using single-molecule imaging, we demonstrate that the germ cell-determining RNP granules in Drosophila embryos are sites for active translation of nanos mRNA. Nanos translation occurs preferentially at the germ granule surface with the 3′ UTR buried

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Shichino, Yuichi, and Shintaro Iwasaki. "Expanding toolkit for RNP granule transcriptomics." Polymer Journal, April 23, 2025. https://doi.org/10.1038/s41428-025-01035-7.

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Abstract Ribonucleoprotein (RNP) granules—membraneless organelles formed through the condensation of RNA and proteins—play pivotal roles in diverse biological processes and diseases, opening new directions in molecular biology. Identifying the RNA composition of these granules is crucial for understanding their formation and functions. However, conventional approaches based on the simple immunoprecipitation of specific granule markers struggle to capture the precise nature of RNP granules. This review summarizes recent advances in granule transcriptome analysis, including the use of purificati

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Zhang, Guoqiang, Yongru Xu, Xiaona Wang, et al. "Dynamic FMR1 granule phase switch instructed by m6A modification contributes to maternal RNA decay." Nature Communications 13, no. 1 (2022). http://dx.doi.org/10.1038/s41467-022-28547-7.

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AbstractMaternal RNA degradation is critical for embryogenesis and is tightly controlled by maternal RNA-binding proteins. Fragile X mental-retardation protein (FMR1) binds target mRNAs to form ribonucleoprotein (RNP) complexes/granules that control various biological processes, including early embryogenesis. However, how FMR1 recognizes target mRNAs and how FMR1-RNP granule assembly/disassembly regulates FMR1-associated mRNAs remain elusive. Here we show that Drosophila FMR1 preferentially binds mRNAs containing m6A-marked “AGACU” motif with high affinity to contributes to maternal RNA degrad

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Freibaum, Brian D., James Messing, Peiguo Yang, Hong Joo Kim, and J. Paul Taylor. "High-fidelity reconstitution of stress granules and nucleoli in mammalian cellular lysate." Journal of Cell Biology 220, no. 3 (2021). http://dx.doi.org/10.1083/jcb.202009079.

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Liquid–liquid phase separation (LLPS) is a mechanism of intracellular organization that underlies the assembly of a variety of RNP granules. Fundamental biophysical principles governing LLPS during granule assembly have been revealed by simple in vitro systems, but these systems have limitations when studying the biology of complex, multicomponent RNP granules. Visualization of RNP granules in cells has validated key principles revealed by simple in vitro systems, but this approach presents difficulties for interrogating biophysical features of RNP granules and provides limited ability to mani

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Glineburg, M. Rebecca, and Carolee Nguyen. "Diverse roles of stress-responsive RNP granules in oogenesis and infertility." Biology of Reproduction, March 21, 2025. https://doi.org/10.1093/biolre/ioaf057.

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Abstract Effectively responding to cellular stress (e.g. nutrient deprivation, oxidative stress) is essential for cell and organismal survival. A protective mechanism is especially critical in developing oocytes, where a prolonged quiescent state and the inability to divide render oocytes highly susceptible to accumulating stress that can result in cell death if unaddressed. Despite the common view that stress granules are the primary stress-responsive ribonucleoprotein (RNP) granule, accumulating evidence shows that in ovaries, other RNP granules also uniquely mediate gene regulation in respo

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