Work

Contributions of Co-Chaperones and Post-Translational Modifications Towards Hsp90 Drug Sensitivity

Year: 2013

Type: article

Abstract: Hsp90 is a molecular chaperone and important driver of stabilization and activation of several oncogenic proteins that are involved in the malignant transformation of tumor cells. Therefore, it is not surprising that Hsp90 has been reported to be a promising target for the treatment of several neoplasias, such as non-small-cell lung cancer and HER2-positive breast cancer. Hsp90 chaperone function depends on its ability to bind and hydrolyze ATP and Hsp90 inhibitors have been shown to compete with nucleotides for binding to Hsp90. Multiple factors, such as co-chaperones and post-translational modification, are involved in regulating Hsp90 ATPase activity. Here, the impact of post-translational modifications and co-chaperones on the efficacy of Hsp90 inhibitors are reviewed.

Source: Future Medicinal Chemistry

DOI: 10.4155/fmc.13.88

Authors: Annerleim Walton-Diaz, Sahar Khan, Dimitra Bourboulia, Jane B Trepel, Len Neckers, Mehdi Mollapour

Institutions: National Cancer Institute, Center for Cancer Research, SUNY Upstate Medical University

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funder: National Institutes of Health