期刊
ACS CHEMICAL BIOLOGY
卷 9, 期 8, 页码 1698-1705出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb500256u
关键词
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资金
- W. H. Goodwin and A. Goodwin
- Commonwealth Cancer Foundation for Research
- Experimental Therapeutics Center of Memorial Sloan-Kettering Cancer Center (MSKCC)
- Hirshberg Foundation for Pancreatic Cancer
- Department of Defense [W81XWH-10-1-0490]
- Clinical and Translation Science Center at Weill Cornell Medical College [UL1RR024996]
- Susan G. Komen for the Cure
- Breast Cancer Research Fund
- NIH [R01 CA119001, R01 CA172546, LLS 6330-11, CA158728, R01 CA155226]
- NCI Cancer Center Support Grant [P30 CA08748]
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.
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