Affinity Purification Probes of Potential Use To Investigate the Endogenous Hsp70 Interactome in Cancer
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- 作者：Anna Rodina ; Tony Taldone ; Yanlong Kang ; Pallav D. Patel ; John Koren ; III ; Pengrong Yan ; Erica M. DaGama Gomes ; Chenghua Yang ; Maulik R. Patel ; Liza Shrestha ; Stefan O. Ochiana ; Cristina Santarossa ; Ronnie Maharaj ; Alexander Gozman ; Marc B. Cox ; Hediye Erdjument-Bromage ; Ronald C. Hendrickson ; Leandro Cerchietti ; Ari Melnick ; Monica L. Guzman ; Gabriela Chiosis
- 刊名：ACS Chemical Biology
- 出版年：2014
- 出版时间：August 15, 2014
- 年：2014
- 卷：9
- 期：8
- 页码：1698-1705
- 全文大小：468K
- ISSN：1554-8937
文摘
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.