The universe of Hsp90
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions. Among the ATP-dependent chaperones, heat shock proteins (Hsp90) proteins play a special role. While Hsp90s can interact with unfolded and...
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2012-02-01
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Online Access: | https://doi.org/10.1515/bmc.2011.054 |
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doaj-a5103423736f465580760e0cd4767a092021-09-05T20:42:37ZengDe GruyterBiomolecular Concepts1868-50211868-503X2012-02-0131799710.1515/bmc.2011.054The universe of Hsp90Stankiewicz Marta0Mayer Matthias P.1Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH-Alliance, Im Neuenheimer Feld 282, D-69120 Heidelberg, GermanyZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH-Alliance, Im Neuenheimer Feld 282, D-69120 Heidelberg, GermanyMolecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions. Among the ATP-dependent chaperones, heat shock proteins (Hsp90) proteins play a special role. While Hsp90s can interact with unfolded and misfolded proteins, their main (and in eukaryotic cells essential) function appears to involve interactions with a limited number of protein clients at late steps of maturation or in “alter-native” conformations for regulating their stability and activity. Because Hsp90 clients are hubs of diverse signaling networks and participate in nearly every cellular function, Hsp90s interconnect many regulatory circuits and link them to environmental impacts. The availability and activity of Hsp90 may thus influence complex physiological and pathophysiological processes, such as differentiation, development, aging, cancer, neurodegeneration, and infectious diseases. Furthermore, through homeostatic effects on differentiation and development, Hsp90s act as capacitors of phenotypic evolution. In this review, we discuss recent insights in the structure and chaperone cycle of Hsp90s, the mechanisms underlying Hsp90 binding to clients, and potential reasons why client proteins specifically require the assistance of Hsp90s. Moreover, the current views on Hsp90-cochaperone interactions and regulation of Hsp90 proteins via posttranslational modifications are summarized. The second half of this article is devoted to the role of Hsp90 proteins in health and disease, aging, and evolution.https://doi.org/10.1515/bmc.2011.054agingchaperonesevolutionprotein foldingregulation by cochaperonesregulation by posttranslational modifications |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Stankiewicz Marta Mayer Matthias P. |
spellingShingle |
Stankiewicz Marta Mayer Matthias P. The universe of Hsp90 Biomolecular Concepts aging chaperones evolution protein folding regulation by cochaperones regulation by posttranslational modifications |
author_facet |
Stankiewicz Marta Mayer Matthias P. |
author_sort |
Stankiewicz Marta |
title |
The universe of Hsp90 |
title_short |
The universe of Hsp90 |
title_full |
The universe of Hsp90 |
title_fullStr |
The universe of Hsp90 |
title_full_unstemmed |
The universe of Hsp90 |
title_sort |
universe of hsp90 |
publisher |
De Gruyter |
series |
Biomolecular Concepts |
issn |
1868-5021 1868-503X |
publishDate |
2012-02-01 |
description |
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions. Among the ATP-dependent chaperones, heat shock proteins (Hsp90) proteins play a special role. While Hsp90s can interact with unfolded and misfolded proteins, their main (and in eukaryotic cells essential) function appears to involve interactions with a limited number of protein clients at late steps of maturation or in “alter-native” conformations for regulating their stability and activity. Because Hsp90 clients are hubs of diverse signaling networks and participate in nearly every cellular function, Hsp90s interconnect many regulatory circuits and link them to environmental impacts. The availability and activity of Hsp90 may thus influence complex physiological and pathophysiological processes, such as differentiation, development, aging, cancer, neurodegeneration, and infectious diseases. Furthermore, through homeostatic effects on differentiation and development, Hsp90s act as capacitors of phenotypic evolution. In this review, we discuss recent insights in the structure and chaperone cycle of Hsp90s, the mechanisms underlying Hsp90 binding to clients, and potential reasons why client proteins specifically require the assistance of Hsp90s. Moreover, the current views on Hsp90-cochaperone interactions and regulation of Hsp90 proteins via posttranslational modifications are summarized. The second half of this article is devoted to the role of Hsp90 proteins in health and disease, aging, and evolution. |
topic |
aging chaperones evolution protein folding regulation by cochaperones regulation by posttranslational modifications |
url |
https://doi.org/10.1515/bmc.2011.054 |
work_keys_str_mv |
AT stankiewiczmarta theuniverseofhsp90 AT mayermatthiasp theuniverseofhsp90 AT stankiewiczmarta universeofhsp90 AT mayermatthiasp universeofhsp90 |
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