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Cancers 2014, 6(1), 333-365; doi:10.3390/cancers6010333

HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins

Apoptosis, Cancer and Development Laboratory, Lyon Cancer Research Center, INSERM U1052-CNRS UMR5286, Claude Bernard University Lyon 1, Lyon 69008, France
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Received: 11 November 2013 / Revised: 3 January 2014 / Accepted: 17 January 2014 / Published: 7 February 2014
(This article belongs to the Special Issue Heat Shock Proteins in Cancer: Chaperones of Tumorigenesis)
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Abstract

Human small heat shock proteins are molecular chaperones that regulate fundamental cellular processes in normal unstressed cells as well as in many cancer cells where they are over-expressed. These proteins are characterized by cell physiology dependent changes in their oligomerization and phosphorylation status. These structural changes allow them to interact with many different client proteins that subsequently display modified activity and/or half-life. Nowdays, the protein interactomes of small Hsps are under intense investigations and will represent, when completed, key parameters to elaborate therapeutic strategies aimed at modulating the functions of these chaperones. Here, we have analyzed the potential pro-cancerous roles of several client proteins that have been described so far to interact with HspB1 (Hsp27) and its close members HspB5 (αB-crystallin) and HspB4 (αA-crystallin). View Full-Text
Keywords: human small Hsps; HspB1; HspB5; HspB4; Hsp27; alphaA-crystallin; alphaB-crystallin; clients; cancer human small Hsps; HspB1; HspB5; HspB4; Hsp27; alphaA-crystallin; alphaB-crystallin; clients; cancer
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Arrigo, A.-P.; Gibert, B. HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins. Cancers 2014, 6, 333-365.

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