Abstract
Since its initial characterization, Hop (Hsp90/Hsp70 organizing protein), known as Sti1 in yeast (stress inducible) is mostly understood to serve as a bridge that facilitates transfer of substrate “client” proteins from Hsp70 to Hsp90. Recent work has shown that Sti1 regulates Hsp90 in a manner distinct from its role as a bridge to Hsp70. This second function of Sti1 seems to be to position Hsp90 for subsequent steps of the client maturation cycle, after the client has been transferred from Hsp70. Thus, Sti1/Hop occupies a central gatekeeper role in the Hsp90 reaction cycle, by first facilitating client access to Hsp90 and then promoting the next steps of the cycle.
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Abbreviations
- 3D:
-
Three dimensional
- AR:
-
Androgen receptor
- ATP:
-
Adenosine triphosphate
- cryoEM:
-
Cryoelectron microscopy
- DP:
-
Aspartate/proline-rich motif
- EM:
-
Electron microscopy
- FOA:
-
5′Fluoro-orotic acid
- GR:
-
Glucocorticoid receptor
- Hop:
-
Hsp90/Hsp70 organizing protein
- Hsp:
-
Heat shock protein
- MAP:
-
Mitogen-activated protein
- SdC:
-
Sti1-dependent carboxy-terminal proximal
- SdN:
-
Sti1-dependent amino-terminal proximal
- TPR:
-
Tetratricopeptide repeat
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Acknowledgements
We thank our National Institutes of Health colleagues for insightful discussions and help with the manuscript. This work was supported by the Intramural Program of the National Institutes of Health, National Institute of Diabetes and Digestive and Kidney diseases.
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Reidy, M. (2019). Sti1/Hop Plays a Pivotal Role in Hsp90 Regulation Beyond Bridging Hsp70. In: Asea, A., Kaur, P. (eds) Heat Shock Protein 90 in Human Diseases and Disorders. Heat Shock Proteins, vol 19. Springer, Cham. https://doi.org/10.1007/978-3-030-23158-3_17
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DOI: https://doi.org/10.1007/978-3-030-23158-3_17
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