Abstract
Hsp90 is an essential and ubiquitous molecular chaperone that is required for the proper folding of a set of client proteins at a late stage in their folding process. In eukaryotes, cytoplasmic Hsp90 is absolutely essential for cell viability under all growth conditions. The functional cycle of the Hsp90 system requires a cohort of cochaperones and cofactors that regulate the activity of this chaperone. Hence, Hsp90 function is highly complex; in order to understand that complexity, several groups have attempted to map out the interaction network of this chaperone in yeast and mammalian systems using the latest available proteomic and genomic tools. Interaction networks emerging from these large scale efforts clearly demonstrate that Hsp90 plays a central role effecting multiple pathways and cellular processes. In yeast Saccharomyces cerevisiae, Hsp90 was shown to interact directly or indirectly with at least 10% of the yeast ORFs. The systematic application of large scale approaches to map out the Hsp90 chaperone network should allow the determination of the mechanisms employed by this chaperone system to maintain protein homeostasis in the cell.
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© 2007 Landes Bioscience and Springer Science+Business Media
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Zhao, R., Houry, W.A. (2007). Molecular Interaction Network of the Hsp90 Chaperone System. In: Csermely, P., VÃgh, L. (eds) Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology, vol 594. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39975-1_3
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DOI: https://doi.org/10.1007/978-0-387-39975-1_3
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