Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells

Landry, Jacques; Chrétien, Pierre; Laszlo, Andrei; Lambert, Herman

doi:10.1002/jcp.1041470113

Cited by 136 publications

(81 citation statements)

References 21 publications

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“…Separately, heat shock proteins induced during inflammation have a critical role in cytoprotection. Phagocytosis and bacterial infection induce heat shock protein synthesis, and these events have been shown to protect cells against subsequent exposure to cytotoxic forms of stress (52)(53)(54)(55)(56)(57)(58). Thus, induction of the heat shock response during inflammation could provide both regulatory and cytoprotective functions.…”

Section: Discussionmentioning

confidence: 99%

Arachidonate is a potent modulator of human heat shock gene transcription.

Jurivich

Sistonen

Sarge

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

173

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Cell and tissue injury activate the inflammatory response through the action(s) of arachidonic acid and its metabolites, leading to the expression of acute-phase proteins and inflammatory cytokines. At the molecular level, little is known how arachidonic acid regulates the inflammatory response. As inflammation is also associated with local increase in tiue temperatures, we eamned whether aridonic acid was directly involved in the heat shock response. Transcriptional Run-On Assays. In vitro nuclear run-on analysis was done as described (25 Abbreviations: HSE, heat shock element; HSF, heat shock factor.

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Section: Discussionmentioning

confidence: 99%

Arachidonate is a potent modulator of human heat shock gene transcription.

Jurivich

Sistonen

Sarge

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

173

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“…Both intra-and extra-lenticularly, the major post-translational sHsp modification is phosphorylation, the levels of which generally increase with age and under stress conditions [115][116][117][118][119]. For example, Bc is phosphorylated at three serine residues, Ser19, Ser45 and Ser59 [118,120,121]; phosphorylation at Ser45 is mediated by p44/p42 MAPK, at Ser59 by MAPKAPK-2 [118,122], whilst the kinase responsible for phosphorylation at Ser19 remains to be identified.…”

Section: Phosphorylationmentioning

confidence: 99%

Small heat-shock proteins: important players in regulating cellular proteostasis

Treweek

Meehan

Ecroyd

et al. 2014

Cell. Mol. Life Sci.

180

177

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Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of posttranslational modifications in sHsp chaperone function, particularly in the context of disease. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 2 Abstract (word count = 159)Small heat-shock proteins (sHsps) are a diverse family of intracellular molecular chaperone proteins that play a critical role in preventing protein unfolding, misfolding and aggregation, particularly under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) and thereby avoid the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. There has been much research into the structure and mechanism of chaperone action of sHsps over approximately the past 30 years, and significant progress has been made of late, however, there are still many unanswered questions relating to these aspects of sHsps. In this review, we outline some of the recent advances in understanding the structure and function of mammalian sHsps, particularly in the context of their many and varied roles in disease.

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“…For Hsp27, the extent of phosphorylation is high (5,14), and phosphorylation is required for thermotolerance (19,49,50). For ␣B-crystallin, the extent of phosphorylation is low (6,13), and the role of phosphorylation in thermotolerance is not known.…”

Section: Shsps Protect Cap-dependent Translation After Heat Shockmentioning

confidence: 99%

Translational Thermotolerance Provided by Small Heat Shock Proteins Is Limited to Cap-dependent Initiation and Inhibited by 2-Aminopurine

Doerwald

Onnekink

Genesen

et al. 2003

Journal of Biological Chemistry

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Heat shock results in inhibition of general protein synthesis. In thermotolerant cells, protein synthesis is still rapidly inhibited by heat stress, but protein synthesis recovers faster than in naive heat-shocked cells, a phenomenon known as translational thermotolerance. Here we investigate the effect of overexpressing a single heat shock protein on cap-dependent and cap-independent initiation of translation during recovery from a heat shock. When overexpressing ␣B-crystallin or Hsp27, cap-dependent initiation of translation was protected but no effect was seen on cap-independent initiation of translation. When Hsp70 was overexpressed however, both cap-dependent and -independent translation were protected. This finding indicates a difference in the mechanism of protection mediated by small or large heat shock proteins. Phosphorylation of ␣B-crystallin and Hsp27 is known to significantly decrease their chaperone activity; therefore, we tested phosphorylation mutants of these proteins in this system. ␣B-crystallin needs to be in its non-phosphorylated state to give protection, whereas phosphorylated Hsp27 is more potent in protection than the unphosphorylatable form. This indicates that chaperone activity is not a prerequisite for protection of translation by small heat shock proteins after heat shock. Furthermore, we show that in the presence of 2-aminopurine, an inhibitor of kinases, among which is double-stranded RNA-activated kinase, the protective effect of overexpressing ␣B-crystallin is abolished. The synthesis of the endogenous Hsps induced by the heat shock to test for thermotolerance is also blocked by 2-aminopurine. Most likely the protective effect of ␣B-crystallin requires synthesis of the endogenous heat shock proteins. Translational thermotolerance would then be a co-operative effect of different heat shock proteins.

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Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells

Cited by 136 publications

References 21 publications

Arachidonate is a potent modulator of human heat shock gene transcription.

Arachidonate is a potent modulator of human heat shock gene transcription.

Small heat-shock proteins: important players in regulating cellular proteostasis

Translational Thermotolerance Provided by Small Heat Shock Proteins Is Limited to Cap-dependent Initiation and Inhibited by 2-Aminopurine

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