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).
Highlights
The literature is filled with reports describing the overexpression of heat shock proteins (Hsps) in many types of cancer cells [1,2]
Additional to their up-regulated levels and broad molecular chaperone activities in stress conditions, small Hsps are described to have an incredible number of fundamental functions in unstressed human cells [5,27,83,234]
This activity can have several consequences: if the folding of the clients is not adapted to cellular conditions, small Hsps can participate in their refolding or degradation
Summary
The literature is filled with reports describing the overexpression of heat shock proteins (Hsps) in many types of cancer cells [1,2]. Small Hsps have been described to have an incredible number of crucial roles in normal unstressed cells as well as in pathological cells where they are usually expressed to high levels. These proteins are considered as important therapeutic targets, in cancer pathologies [5,6]. They display anti-apoptotic and tumorogenic properties and trigger host anti-cancer response inhibition, such as senescence [7,8,9,10,11,12,13]. We have reviewed the pro-oncogenic client proteins interacting with HspB1, HspB5 or HspB4 that can play crucial roles in human cancer pathologies
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