Pharmacological Targeting of the Hsp70 Chaperone

Title: Pharmacological Targeting of the Hsp70 Chaperone

Volume: 9 Issue: 15

Author(s): Srikanth Patury, Yoshinari Miyata and Jason E. Gestwicki

Affiliation:

Keywords: Proteostasis, flavonoids, dihydropyrimidines, spergualin, sulfoglycolipids, geranylgeranyl acetone, protein folding, ATPase, protein-protein interactions

Abstract: The molecular chaperone, heat shock protein 70 (Hsp70), acts at multiple steps in a proteins life cycle, including during the processes of folding, trafficking, remodeling and degradation. To accomplish these various tasks, the activity of Hsp70 is shaped by a host of co-chaperones, which bind to the core chaperone and influence its functions. Genetic studies have strongly linked Hsp70 and its co-chaperones to numerous diseases, including cancer, neurodegeneration and microbial pathogenesis, yet the potential of this chaperone as a therapeutic target remains largely underexplored. Here, we review the current state of Hsp70 as a drug target, with a special emphasis on the important challenges and opportunities imposed by its co-chaperones, protein-protein interactions and allostery.

Cite this article as:

Patury Srikanth, Miyata Yoshinari and Gestwicki E. Jason, Pharmacological Targeting of the Hsp70 Chaperone, Current Topics in Medicinal Chemistry 2009; 9 (15) . https://dx.doi.org/10.2174/156802609789895674