Chaperones: needed for both the good times and the bad times

Quinlan, Roy A.; Ellis, R. John

doi:10.1098/rstb.2013.0091

Cited by 26 publications

(21 citation statements)

References 139 publications

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“…These are known to play a role not only in protein folding but also in telomere maintenance, perturbations in which can force the cell cycle towards senescence [50,51]. In addition, heat shock proteins are a class of chaperones known to react to stress conditions [52] and they are induced under cellular oxidative stress [53]. We found alterations of both cytoplasmic and mitochondrial heat shock proteins such as Hsp27, Hsp70 and Hsp90.…”

Section: Discussionmentioning

confidence: 92%

Quantitative and integrated proteome and microRNA analysis of endothelial replicative senescence

Yentrapalli

Azimzadeh

Kraemer

et al. 2015

Journal of Proteomics

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Section: Discussionmentioning

confidence: 92%

Quantitative and integrated proteome and microRNA analysis of endothelial replicative senescence

Yentrapalli

Azimzadeh

Kraemer

et al. 2015

Journal of Proteomics

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“…sHSPs are perhaps under-appreciated in the chaperone research field, although the review by Quinlan and Ellis (2013) stated: "we return to first principles, and shine the spotlight on the role of chaperones in biomolecular assemblies, as first defined for nucleosomes by Laskey et al (1978)". This initial concept is now widened to include the modulation of many assembled polymers during normal cell growth and development.…”

Section: Stress Proteins and Molecular Chaperones In Cells And In Lifementioning

confidence: 97%

Gravitational Effects on Human Physiology

Atomi

2015

Subcellular Biochemistry

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Physical working capacity decreases with age and also in microgravity. Regardless of age, increased physical activity can always improve the physical adaptability of the body, although the mechanisms of this adaptability are unknown. Physical exercise produces various mechanical stimuli in the body, and these stimuli may be essential for cell survival in organisms. The cytoskeleton plays an important role in maintaining cell shape and tension development, and in various molecular and/or cellular organelles involved in cellular trafficking. Both intra and extracellular stimuli send signals through the cytoskeleton to the nucleus and modulate gene expression via an intrinsic property, namely the "dynamic instability" of cytoskeletal proteins. αB-crystallin is an important chaperone for cytoskeletal proteins in muscle cells. Decreases in the levels of αB-crystallin are specifically associated with a marked decrease in muscle mass (atrophy) in a rat hindlimb suspension model that mimics muscle and bone atrophy that occurs in space and increases with passive stretch. Moreover, immunofluorescence data show complete co-localization of αB-crystallin and the tubulin/microtubule system in myoblast cells. This association was further confirmed in biochemical experiments carried out in vitro showing that αB-crystallin acts as a chaperone for heat-denatured tubulin and prevents microtubule disassembly induced by calcium. Physical activity induces the constitutive expression of αB-crystallin, which helps to maintain the homeostasis of cytoskeleton dynamics in response to gravitational forces. This relationship between chaperone expression levels and regulation of cytoskeletal dynamics observed in slow anti-gravitational muscles as well as in mammalian striated muscles, such as those in the heart, diaphragm and tongue, may have been especially essential for human evolution in particular. Elucidation of the intrinsic properties of the tubulin/microtubule and chaperone αB-crystallin protein complex systems is expected to provide valuable information for high-pressure bioscience and gravity health science.

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“…17.2 ), from the cell cycle to genome stability, from apoptosis to proteostasis, from the cytoskeleton to metabolic enzymes. This explains their potential to integrate (Quinlan and Ellis 2013 ) and infl uence the proliferation, differentiation of individual cells and their integration into tissues and animal physiology. Equally, IF proteins are widely expressed and mutations in IF proteins are the cause of a broad range of diseases (Omary 2009 ).…”

Section: Fig 171 the Shsp-if Partnership -Seeing Is Believingmentioning

confidence: 98%

The Dynamic Duo of Small Heat Proteins and IFs Maintain Cell Homeostasis, Resist Cellular Stress and Enable Evolution in Cells and Tissues

Perng

Quinlan

2015

Heat Shock Proteins

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As with many proteins, their initial christening with a name corrals our thinking on their functions and roles. IFs were not named as heat shock proteins, but along with heat shock proteins, they continue to be expressed in response to heat shock. In this review we outline the case for exposing the identity of the "dynamic duo" as small heat shock proteins (sHSPs) and their IF (IF) partners in their battle to assuage stress. Together they maintain the homeostasis of and integrate key cellular processes within cells that allow potential evolutionary opportunity to be seized (Quinlan RA, Ellis RJ, Philos Trans R Soc Lond B Biol Sci 368:20130091, 2013). Both sHSPs and IFs form dynamic polymeric structures -nano-particles and intermediate (nano) fi laments respectively. Both have a wide range of interaction (client) proteins. IFs provide a convenient matrix to host small heat shock proteins and potentiate their role as chaperones, whilst IF function is sHSP-dependent. Together, it is their emerging capacity as integrators of both cell homeostasis and the stress response within and between tissues, however, which is the most exciting. This is because the dynamic duo co-operate on the two central chaperone activities -assisting protein assemblies and dealing with the consequences of protein damage. We propose that the sHSP-IF partnership is key to understanding the stress response, not least because it emphasizes the role of these protein chaperones in assisting the building, regulation and turnover of the IF protein assemblies as well as in diseases caused by their malfunction.

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Chaperones: needed for both the good times and the bad times

Cited by 26 publications

References 139 publications

Quantitative and integrated proteome and microRNA analysis of endothelial replicative senescence

Quantitative and integrated proteome and microRNA analysis of endothelial replicative senescence

Gravitational Effects on Human Physiology

The Dynamic Duo of Small Heat Proteins and IFs Maintain Cell Homeostasis, Resist Cellular Stress and Enable Evolution in Cells and Tissues

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