Roles of YB-1 under arsenite-induced stress: Translational activation of HSP70 mRNA and control of the number of stress granules

Tanaka, Toru; Ohashi, Sachiyo; Kobayashi, Shunsuke

doi:10.1016/j.bbagen.2013.11.002

Cited by 25 publications

(32 citation statements)

References 40 publications

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“…We found that, while low expression levels of GFP-YB-1 do not interfere with arsenite-induced stress granules, above a threshold, stress granule assembly is significantly inhibited (Figure 4). In addition, arguing against a role of HSP70 (40), we observed that high level of YB-1 similarly leads to the inhibition of stress granule assembly when both the HSP70 activity and its expression were inhibited by VER-155008 plus puromycin treatment (Supplementary Figure S5B). The inhibitory effect of YB-1 expression on stress granule assembly could then rather result from the direct binding of YB-1 to mRNA.…”

Section: Resultsmentioning

confidence: 87%

“…To test this hypothesis, we chose YB-1, a cytoplasmic mRNA-binding protein (28) which could directly prevent mRNA aggregation for the following reasons: (i) YB-1 has a higher affinity for nonpolysomal than polysomal mRNA (39) so that it can then effectively compete for the binding to nonpolysomal mRNA with other RNA-binding proteins; (ii) YB-1 is dispensable for stress granule assembly as its silencing does not impede stress granule assembly (Supplementary Figure S5A); (iii) YB-1 is known to form stable isolated mRNPs (28). Importantly, YB-1 overexpression in cells could prevent stress granule assembly (40), though an increased HSP70 activity was put forward to explain such behavior.…”

Section: Resultsmentioning

confidence: 99%

“…We first controlled whether YB-1 in our conditions behaves as a negative regulator of stress granule assembly, as previously described (40). We found that, while low expression levels of GFP-YB-1 do not interfere with arsenite-induced stress granules, above a threshold, stress granule assembly is significantly inhibited (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

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Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules

et al. 2014

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The sequence of events leading to stress granule assembly in stressed cells remains elusive. We show here, using isotope labeling and ion microprobe, that proportionally more RNA than proteins are present in stress granules than in surrounding cytoplasm. We further demonstrate that the delivery of single strand polynucleotides, mRNA and ssDNA, to the cytoplasm can trigger stress granule assembly. On the other hand, increasing the cytoplasmic level of mRNA-binding proteins like YB-1 can directly prevent the aggregation of mRNA by forming isolated mRNPs, as evidenced by atomic force microscopy. Interestingly, we also discovered that enucleated cells do form stress granules, demonstrating that the translocation to the cytoplasm of nuclear prion-like RNA-binding proteins like TIA-1 is dispensable for stress granule assembly. The results lead to an alternative view on stress granule formation based on the following sequence of events: after the massive dissociation of polysomes during stress, mRNA-stabilizing proteins like YB-1 are outnumbered by the burst of nonpolysomal mRNA. mRNA freed of ribosomes thus becomes accessible to mRNA-binding aggregation-prone proteins or misfolded proteins, which induces stress granule formation. Within the frame of this model, the shuttling of nuclear mRNA-stabilizing proteins to the cytoplasm could dissociate stress granules or prevent their assembly.

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Section: Resultsmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 99%

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Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules

et al. 2014

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“…Moreover, the intracellular location(s) of oxidized RNA quality control in eukaryotic cells have been hypothesized to include stress granules and processing bodies (Thomas et al, 2011;Walters and Parker, 2014;Wurtmann and Wolin, 2009). For stress granules, this is supported by their recruitment of YB-1 and Auf1, and their formation under oxidative stress conditions when excess ROS cause oxidative damage (Bravard et al, 2010;Onishi et al, 2008;Tanaka et al, 2014). Similarly, processing bodies increase in size and number during oxidative stress, and they contain mRNA degradation machinery, a component of RNA quality control (Thomas et al, 2011;Walters and Parker, 2014).…”

Section: Introductionmentioning

confidence: 93%

Localized control of oxidized RNA

Zhan

Dhaliwal

Adjibade

et al. 2015

Journal of Cell Science

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The oxidation of biological molecules by reactive oxygen species (ROS) can render them inactive or toxic. This includes the oxidation of RNA, which appears to underlie the detrimental effects of oxidative stress, aging and certain neurodegenerative diseases. Here, we investigate the management of oxidized RNA in the chloroplast of the green alga Chlamydomonas reinhardtii. Our immunofluorescence microscopy results reveal that oxidized RNA (with 8-hydroxyguanine) is localized in the pyrenoid, a chloroplast microcompartment where CO 2 is assimilated by the Calvin cycle enzyme Rubisco. Results of genetic analyses support a requirement for the Rubisco large subunit (RBCL), but not Rubisco, in the management of oxidized RNA. An RBCL pool that can carry out such a 'moonlighting' function is revealed by results of biochemical fractionation experiments. We also show that human (HeLa) cells localize oxidized RNA to cytoplasmic foci that are distinct from stress granules, processing bodies and mitochondria. Our results suggest that the compartmentalization of oxidized RNA management is a general phenomenon and therefore has some fundamental significance.

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“…Based on this, the perceived YB-1-induced protective phenotype against oxidative stress was explained through a sequestration mechanism [98], for which the protein prevents the translation of 8-oxoG-containing mRNAs. However, following arsenite-induced oxidative stress, YB-1 translocates from mRNA processing bodies (P-bodies) to stress granules [100]. These structures are proposed to provide a protecting environment for RNA during stress.…”

Section: Quality Control Of Damaged Rnamentioning

confidence: 99%

Quality control of chemically damaged RNA

Simms

Zaher

2016

Cell. Mol. Life Sci.

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The “central dogma” of molecular biology describes how information contained in DNA is transformed into RNA and finally into proteins. In order for proteins to maintain their functionality in both the parent cell and subsequent generations, it is essential that the information encoded in DNA and RNA remains unaltered. DNA and RNA are constantly exposed to damaging agents, which can modify nucleic acids and change the information they encode. While much is known about how cells respond to damaged DNA, the importance of protecting RNA has only become appreciated over the past decade. Modification of the nucleobase through oxidation and alkylation has long been known to affect its base-pairing properties during DNA replication. Similarly, recent studies have begun to highlight some of the unwanted consequences of chemical damage on mRNA decoding during translation. Oxidation and alkylation of mRNA appear to have drastic effects on the speed and fidelity of protein synthesis. As some mRNAs can persist for days in certain tissues, it is not surprising that it has recently emerged that mRNA-surveillance and RNA-repair pathways have evolved to clear or correct damaged mRNA.

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Roles of YB-1 under arsenite-induced stress: Translational activation of HSP70 mRNA and control of the number of stress granules

Cited by 25 publications

References 40 publications

Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules

Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules

Localized control of oxidized RNA

Quality control of chemically damaged RNA

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