Small heat shock proteins (sHsps) regulate a large number of fundamental cellular processes and are involved in many pathological diseases. They share complex oligomerization and phosphorylation properties allowing them to interact and modulate the activity of many client proteins. Here, the up-to date protein interactome of the ten human sHsps is presented as an illustration of their multiple cellular functions. In addition of forming homo-oligomers, some of these proteins interact whith each other and form hetero-oligomeric complexes that could bear new protein targets recognition abilities. Here, novel informations are presented on how the formation of HspB1/HspB5 complex can stimulate the activity of the oxidoresistance promoting enzyme glucose 6-phosphate dehydrogenase through its interaction with newly formed highly phosphorylated HspB1 homo-oligomers.
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| http://dx.doi.org/10.1016/j.febslet.2013.05.011 | DOI Listing |
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