Title
Affinity-purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer
Publication Date
1-1-2014
Document Type
Article
Abstract
Heat shock protein 70 (Hsp70) is a family of proteins with key roles in regulating malignancy. Cancer cells rely on Hsp70 to inhibit apoptosis, regulate senescence and autophagy, and maintain the stability of numerous onco-proteins. Despite these important biological functions in cancer, robust chemical tools that enable the analysis of the Hsp70-regulated proteome in a tumor-by-tumor manner are yet unavailable. Here we take advantage of a recently reported Hsp70 ligand to design and develop an affinity purification chemical toolset for potential use in the investigation of the endogenous Hsp70-interacting proteome in cancer. We demonstrate that these tools lock Hsp70 in complex with onco-client proteins and effectively isolate Hsp70 complexes for identification through biochemical techniques. Using these tools we provide proof-of-concept analyses that glimpse into the complex roles played by Hsp70 in maintaining a multitude of cell-specific malignancy-driving proteins.
Comments
Rodina A, Taldone T, Kang Y, Patel PD, Koren J, Yan P, DaGama Gomes EM, Yang C, Patel MR, Shrestha L, et al. Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer. ACS Chem Biol 2014 08/15;9(8):1698-705.