Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress

Cherkasov, Valeria; Hofmann, Sarah; Druffel-Augustin, Silke; Mogk, Axel; Tyedmers, Jens; Stoecklin, Georg; Bukau, Bernd

doi:10.1016/j.cub.2013.09.058

Cited by 210 publications

(266 citation statements)

References 43 publications

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“…Indeed, work in yeast and Drosophila spp. has concluded that chaperones are associated with stress granules and are necessary for the resumption of translation after severe heat stress (Cherkasov et al, 2013). While our experiments point to a clear interaction between sHSPs, specific translation factors, and HSP101, we also observed distinct cytosolic foci of CI and CII sHSPs that did not colocalize with either the identified translation factors or HSP101.…”

Section: Discussioncontrasting

confidence: 67%

Class I and II small heat-shock proteins protect protein translation factors during heat stress

et al. 2016

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The ubiquitous small heat shock proteins (sHSPs) are well documented to act in vitro as molecular chaperones to prevent the irreversible aggregation of heat-sensitive proteins. However, the in vivo activities of sHSPs remain unclear. To investigate the two most abundant classes of plant cytosolic sHSPs (class I [CI] and class II [CII]), RNA interference (RNAi) and overexpression lines were created in Arabidopsis (Arabidopsis thaliana) and shown to have reduced and enhanced tolerance, respectively, to extreme heat stress. Affinity purification of CI and CII sHSPs from heat-stressed seedlings recovered eukaryotic translation elongation factor (eEF) 1B (a-, b-, and g-subunits) and eukaryotic translation initiation factor 4A (three isoforms), although the association with CI sHSPs was stronger and additional proteins involved in translation were recovered with CI sHSPs. eEF1B subunits became partially insoluble during heat stress and, in the CI and CII RNAi lines, showed reduced recovery to the soluble cell fraction after heat stress, which was also dependent on HSP101. Furthermore, after heat stress, CI sHSPs showed increased retention in the insoluble fraction in the CII RNAi line and vice versa. Immunolocalization revealed that both CI and CII sHSPs were present in cytosolic foci, some of which colocalized with HSP101 and with eEF1Bg and eEF1Bb. Thus, CI and CII sHSPs have both unique and overlapping functions and act either directly or indirectly to protect specific translation factors in cytosolic stress granules.

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Section: Discussioncontrasting

confidence: 67%

Class I and II small heat-shock proteins protect protein translation factors during heat stress

et al. 2016

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“…Third, we do not observe an HSP104-dependent recovery (Supplemental Fig. S1), as in the case with heat stress granules (Cherkasov et al 2013). It is possible that in the absence of HSP70/40 proteins, distinct protein aggregates also form, and might even merge with stress granules under some conditions (Buchan et al 2013).…”

Section: Discussionmentioning

confidence: 52%

“…Several observations argue that the structures we observe are bona fide stress granules, as opposed to "heat stress granules" (Cherkasov et al 2013). First, Pab1-GFP foci in this work are cycloheximide sensitive and contain additional SG markers (Fig.…”

Section: Discussionmentioning

confidence: 79%

Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae

Walters

Muhlrad

Garcia

et al. 2015

RNA

118

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Stress granules and P-bodies are conserved assemblies of nontranslating mRNAs in eukaryotic cells that can be related to RNAprotein aggregates found in some neurodegenerative diseases. Herein, we examine how the Hsp70/Hsp40 protein chaperones affected the assembly and disassembly of stress granules and P-bodies in yeast. We observed that Hsp70 and the Ydj1 and Sis1 Hsp40 proteins accumulated in stress granules and defects in these proteins led to decreases in the disassembly and/or clearance of stress granules. We observed that individual Hsp40 proteins have different effects on stress granules with defects in Ydj1 leading to accumulation of stress granules in the vacuole and limited recovery of translation following stress, which suggests that Ydj1 promotes disassembly of stress granules to promote translation. In contrast, defects in Sis1 did not affect recovery of translation, accumulated cytoplasmic stress granules, and showed reductions in the targeting of stress granules to the vacuole. This demonstrates a new principle whereby alternative disassembly machineries lead to different fates of components within stress granules, thereby providing additional avenues for regulation of their assembly, composition, and function. Moreover, a role for Hsp70 and Hsp40 proteins in stress granule disassembly couples the assembly of these stress responsive structures to the proteostatic state of the cell.

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“…Various heat shock proteins (HSPs) localize to, and affect, disassembly of stress granules in humans, flies, and yeast. 24,33,74,78 An appealing model 78 is that when cellular stress leads to accumulation of unfolded proteins, titration of HSPs would cause slower stress granule disassembly and trapping of mRNAs in nontranslating states, thus helping cells conserve resources. As HSPs become available again either via increased synthesis, or from having dealt with other unfolded proteins, stress granules could once more be disassembled.…”

Section: Mrnp Granules Assemble Via Common Mechanismsmentioning

confidence: 99%

mRNP granules

2014

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Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress

Abstract: Chaperone-driven protein disaggregation directly coordinates timing of translation reinitiation with protein folding capacity during cellular protein quality surveillance, enabling efficient protein homeostasis.

Cited by 210 publications

References 43 publications

Class I and II small heat-shock proteins protect protein translation factors during heat stress

Class I and II small heat-shock proteins protect protein translation factors during heat stress

Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae

mRNP granules

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