2014
DOI: 10.1016/j.bbagen.2013.11.002
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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

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Cited by 25 publications
(32 citation statements)
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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%
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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%
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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%
“…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%