Some like it hot: the structure and function of small heat-shock proteins

Haslbeck, Martin; Franzmann, Titus M.; Weinfurtner, Daniel; Büchner, Johannes

doi:10.1038/nsmb993

Cited by 744 publications

(750 citation statements)

References 68 publications

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“…In an ATP independent process, an aspect that is remarkably different from other chaperones (except TF), small HSPs induce changes in the physiochemical properties of misfolded polypeptides in the aggregates. This presumably facilitates the disaggregation machinery to effectively separate and unfold the individual polypeptides in the aggregates (Haslbeck, 2002;Haslbeck et al, 2005;Mogk et al, 2003).…”

Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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Section: Ii441 Chaperone Mediated Refolding and Disaggregationmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…Small HSPs (sHSPs) comprise the most widespread but also the most poorly conserved family of molecular chaperones. sHSPs share characteristic features, including a conserved -crystallin domain, formation of large oligomers, induction by stress conditions and chaperone activity (Haslbeck et al, 2005;Sun and MacRae, 2005). It is generally accepted that HSPs protect organisms from the detrimental effects of heat and possibly other stressors, including various chemicals, heavy metals, cold, oxidative stress, osmotic stress and desiccation (Kregel, 2002;Lindquist, 1986;Somero, 1995).…”

Section: Introductionmentioning

confidence: 99%

Natural annual cycle of heat shock protein expression in land snails: desertversusMediterranean species ofSphincterochila

Arad

Mizrahi

Goldenberg

et al. 2010

Journal of Experimental Biology

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SUMMARYLand snails are subject to daily and seasonal variations in temperature and in water availability, and have evolved annual cycles of activity and aestivation as part of their survival strategy. We tested in the field whether adaptation to different habitats affects the endogenous levels of heat shock proteins (HSPs) in two closely related Sphincterochila snail species, a desiccation-resistant desert species, Sphincterochila zonata, and a Mediterranean-type, desiccation-sensitive species, S. cariosa. We examined HSP levels in various tissues of snails during aestivation and after resumption of activity. Our study shows that, during aestivation, S. cariosa had higher standing stocks of Hsp70 in the foot and the hepatopancreas, and of small HSPs (sHSPs) in all the examined tissues, whereas S. zonata had higher stocks of Hsp70 in the kidney and of Hsp90 in the kidney and in the hepatopancreas. Arousal induced a general upregulation of HSPs, except for Hsp90, the expression of which in the foot was higher during aestivation. We suggest that the stress protein machinery is upregulated during arousal in anticipation of possible oxidative stress ensuing from the accelerating metabolic rate and the exit from the deep hypometabolic state. Our findings support the concept that, in land snails, aestivation and activity represent two distinct physiological states, and suggest that land snails use HSPs as important components of the aestivation mechanism, and as part of their survival strategy during and after arousal. Our study also indicates that adaptation to different habitats results in the development of distinct strategies of HSP expression with likely consequences for the ecology and distribution of land snails. Supplementary material available online at

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“…Irrespective of the final destination of unfolded proteins, sHsps can act as a first line of defence against the threat of unfolded proteins, capable of sensing very subtle changes in the stability of proteins (McHaourab et al 2009). Considering the presence of multiple sHsp genes in almost all organisms (Haslbeck et al 2005), their implication in a variety of different diseases (Sun and MacRae 2005), and their dramatic upregulation into the most abundant proteins upon stress (Beck et al 2009), it is obvious that sHsps play an important role in maintaining proteostasis in the cell.…”

Section: Introductionmentioning

confidence: 99%

Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry

Lambert

Rutsdottir

Hussein

et al. 2013

Cell Stress and Chaperones

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Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and little is known about what parts of the small heat-shock proteins interact with substrates and what parts of a partially unfolded substrate protein interact with the small heat-shock proteins. The transient nature of the interactions that prevent substrate aggregation rationalize probing this interaction by crosslinking mass spectrometry. Here, we used a workflow with lysine-specific crosslinking and offline nano-liquid chromatography matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry to explore the interaction between the plant small heat-shock protein Hsp21 and a thermosensitive model substrate protein, malate dehydrogenase. The identified crosslinks point at an interaction between the disordered N-terminal region of Hsp21 and the C-terminal presumably unfolding part of the substrate protein.

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Some like it hot: the structure and function of small heat-shock proteins

Cited by 744 publications

References 68 publications

Firefly luciferase mutants as sensors of proteome stress

Firefly luciferase mutants as sensors of proteome stress

Natural annual cycle of heat shock protein expression in land snails: desertversusMediterranean species ofSphincterochila

Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry

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