Abstract
Molecular chaperones are a functionally defined set of proteins which assist the structure formation of proteins in vivo. Without certain protective mechanisms, such as binding nascent polypeptide chains by molecular chaperones, cellular protein concentrations would lead to misfolding and aggregation. In the mammalian system, the molecular chaperones Hsp70 and Hsp90 are involved in the folding and maturation of key regulatory proteins, like steroid hormone receptors, transcription factors, and kinases, some of which are involved in cancer progression. Hsp70 and Hsp90 form a multichaperone complex, in which both are connected by a third protein called Hop. The connection of and the interplay between the two chaperone machineries is of crucial importance for cell viability. This review provides a detailed view of the Hsp70 and Hsp90 machineries, their cofactors and their mode of regulation. It summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction.
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Abbreviations
- TPR:
-
Tetratricopeptide repeat
- Hsp70:
-
Heat shock protein 70
- yHsp70:
-
Yeast heat shock protein 70
- Hsp90:
-
Heat shock protein 90
- yHsp90:
-
Yeast heat shock protein 90
- hHsp90:
-
Human heat shock protein 90
- SHR:
-
Steroid hormone receptor
- GA:
-
Geldanamycin
- GR:
-
Glucocorticoid receptor
- PR:
-
Progesterone receptor
- ER:
-
Endoplasmic reticulum
- DSG:
-
15-Deoxyspergualin
- GR-LBD:
-
Glucocorticoid receptor ligand binding domain
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Wegele, H., Müller, L., Buchner, J. (2004). Hsp70 and Hsp90—a relay team for protein folding. In: Reviews of Physiology, Biochemistry and Pharmacology. Reviews of Physiology, Biochemistry and Pharmacology, vol 151. Springer, Berlin, Heidelberg. https://doi.org/10.1007/s10254-003-0021-1
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