- Title
- Hsp90 co-chaperones as drug targets in cancer: current perspectives
- Creator
- Edkins, Adrienne L
- Date
- 2016
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/66347
- Identifier
- vital:28938
- Identifier
- https://doi.org/10.1007/7355_2015_99
- Description
- publisher version
- Description
- Hsp90 is a molecular chaperone that regulates the function of numerous oncogenic transcription factors and signalling intermediates in the cell. Inhibition of Hsp90 is sufficient to induce the proteosomal degradation of many of these proteins, and as such, the Hsp90 chaperone has been regarded as a promising drug target. The appropriate functioning of the Hsp90 chaperone is dependent on its ATPase activity and interactions with a cohort of non-substrate accessory proteins known as co-chaperones. Co-chaperones associate with Hsp90 at all stages of the chaperone cycle and regulate a range of Hsp90 functions, including ATP hydrolysis and client protein binding and release. Given the ability of co-chaperones to organise the function of the Hsp90 molecular machine, these proteins are now regarded as potential drug targets. Herein the role of selected Hsp90 co-chaperones Hop, Cdc37, p23 and Aha1 as possible drug targets is discussed with a focus on cancer.
- Description
- This work is based on the research supported by the South African Research Chairs Initiative of the Department of Science and Technology and National Research Foundation of South Africa (Grant No 98566), the Cancer Association of South Africa (CANSA), Medical Research Council South Africa (MRC-SA) and Rhodes University. The views expressed are those of the authors and should not be attributed to the DST, NRF, CANSA, MRC-SA or Rhodes University. We apologize if we have inadvertently missed any important contributions to the field.
- Format
- Publisher
- Springer International Publishing Switzerland
- Language
- English
- Relation
- Topics in Medicinal Chemistry, Edkins A.L. (2016) Hsp90 Co-chaperones as Drug Targets in Cancer: Current Perspectives. In: McAlpine S., Edkins A. (eds) Heat Shock Protein Inhibitors. Topics in Medicinal Chemistry, vol 19. Springer, Cham, Topics in Medicinal Chemistry volume 19 number 21 54 2016 978-3-319-32607-8
- Rights
- Springer International Publishing Switzerland
- Rights
- Use of this resource is governed by the terms and conditions of the National Library of South Africa Copyright Act (http://www.nlsa.ac.za/downloads/Copyright Act.pdf)
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