The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Open accessAbstract
SUMMARY The multifunctional, stress-inducible, molecular chaperone HSP70 has important roles in aiding protein folding and maintaining protein homeostasis. HSP70 expression is elevated in many cancers, contributing to tumor cell survival and resistance to therapy. We have determined that a small molecule called 2-Phenylethynesulfonamide (PES) interacts selectively with HSP70, and leads to a disruption of the association between HSP70 and several of its co-chaperones and substrate proteins. Treatment of cultured tumor cells with PES promotes cell death that is associated with protein aggregation, impaired autophagy, and inhibition of lysosomal function. Moreover, this small molecule is able to suppress tumor development and enhance survival in a mouse model of Myc-induced lymphomagenesis. The data demonstrate that PES disrupts actions of HSP70 in multiple cell signaling pathways offering an opportunity to better understand the diverse functions of this molecular chaperone, and also to aid in the development of new cancer therapies.
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Cites
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Self-citation
Cited by
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Autophagy-Dependent Anticancer Immune Responses Induced by Chemotherapeutic Agents in Mice
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Histone deacetylase 10 promotes autophagy-mediated cell survival
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Metadata
- Authors
- Leu, J. I.-J., Pimkina, J., Frank, A., Murphy, M. E., & George, D. L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 36
- Issue
- 1
- Pages
- 15-27
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2001569984
- Cited by
- 441
- References
- 66
- FWCI
- 11.16
- Type
- journal article
- Language
- en
- Open access
- bronze
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