Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer Journal Article
| Authors: | Rodina, A.; Taldone, T.; Kang, Y.; Patel, P. D.; Koren, J.; Yan, P.; DaGama Gomes, E. M.; Yang, C.; Patel, M. R.; Shrestha, L.; Ochiana, S. O.; Santarossa, C.; Maharaj, R.; Gozman, A.; Cox, M. B.; Erdjument-Bromage, H.; Hendrickson, R. C.; Cerchietti, L.; Melnick, A.; Guzman, M. L.; Chiosis, G. |
| Article Title: | Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer |
| 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. © 2014 American Chemical Society. |
| Journal Title: | ACS Chemical Biology |
| Volume: | 9 |
| Issue: | 8 |
| ISSN: | 1554-8929 |
| Publisher: | American Chemical Society |
| Date Published: | 2014-08-15 |
| Start Page: | 1698 |
| End Page: | 1705 |
| Language: | English |
| DOI: | 10.1021/cb500256u |
| PROVIDER: | scopus |
| PMCID: | PMC4134716 |
| PUBMED: | 24934503 |
| DOI/URL: | |
| Notes: | Export Date: 2 September 2014 -- CODEN: ACBCC -- Source: Scopus |
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