Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function

Author(s): Lei Wang, Li Li, Kai Gu, Xiao-Li Xu, Yuan Sun, Qi-Dong You*.

Journal Name: Current Drug Targets

Volume 18 , Issue 13 , 2017

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Graphical Abstract:


Background & Objective: The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins. In recent years, many Hsp90 inhibitors have entered into the clinical trials while all of them target ATPase showing similar binding capacity and kinds of side-effects so that none have reached to the market. During the regulation progress, numerous protein- protein interactions (PPI) such as Hsp90 and client proteins or cochaperones are involved. With the Hsp90-cochaperones PPI networks being more and more clear, many cancerous proteins have been reported to be tightly correlated to Hsp90-cochaperones PPI. Among them, Hsp90-Cdc37 PPI has been widely reported to associate with numerous protein kinases, making it a novel target for the treatment of cancers.

Results and Conclusion: In this paper, we briefly review the strategies and modulators targeting Hsp90-Cdc37 complex including direct and indirect regulation mechanism. Through these discussions we expect to present inspirations for new insights into an alternative way to inhibit Hsp90 chaperone function.

Keywords: Hsp90/Cdc37, protein-protein interaction, PPI inhibitors, targeting strategies, protein kinases.

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Article Details

Year: 2017
Page: [1572 - 1585]
Pages: 14
DOI: 10.2174/1389450117666160527125522
Price: $65

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