Functional modulation of DBC2 by the Hsp90 chaperone machine

Abstract

Scope and Method of Study: This study involved looking at various mechanistic associations of the tumor suppressor DBC2 with the Hsp90 chaperone machine. Along with aspects of functional relationships of co-chaperone and inhibitors of the Hsp90 Chaperone machine. Techniques that were used in this study include: In vitro coupled transcription/translation, Immunoprecipitation, LC-MS/MS, Tyrosine kinase assay, and Surface plasmon resonance.

Findings and Conclusions: The tumor suppressor DBC2 was shown to be a client protein of the Hsp90 chaperone machine. The Hsp90 chaperone machine was identified to modulate the GTP binding of DBC2 as well as the associating protein complexes. This allowed for the detection of the protein complexes that are associated with DBC2 in resistant (HeLa) and sensitive (MCF-7) cell lines.

Additionally, this allowed for the identification of a novel Cdc37 null In vitro system in WGL. Along with the observations for direct interaction of Hsp90 with novel small molecule inhibitors