Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2 The sections in this article are Introduction The Hsp 90 Family in vivo Evolutionary Relationships within the Hsp 90 Gene Family In Vivo Functions of Hsp 90 Regulation of Hsp 90 Expression and Posttranscriptional Activation Chemical Inhibition of Hsp 90 Identification of Natural Hsp 90 Substrates In Vitro Investigation of the Chaperone Hsp 90 Hsp 90: A Special Kind of ATPase The ATPase Cycle of Hsp 90 Interaction of Hsp 90 with Model Substrate Proteins Investigating Hsp 90 Substrate Interactions Using Native Substrates Partner Proteins: Does Complexity Lead to Specificity? Hop , p 23, and PPIases: The Chaperone Cycle of Hsp 90 Hop / Sti 1: Interactions Mediated by TPR Domains p 23/ Sba 1: Nucleotide‐specific Interaction with Hsp 90 Large PPIases: Conferring Specificity to Substrate Localization? Pp5: Facilitating Dephosphorylation Cdc 37: Building Complexes with Kinases Tom 70: Chaperoning Mitochondrial Import CHIP and Sgt 1: Multiple Connections to Protein Degradation Aha 1 and Hch 1: Just Stimulating the ATPase? Cns 1, Sgt 2, and Xap 2: Is a TPR Enough to Become an Hsp 90 Partner? Conclusion Acknowledgements
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