Apoptosis, Cancer and Development Laboratory, Lyon Cancer Research Center, INSERM U1052-CNRS UMR5286, Claude Bernard University Lyon 1, Lyon 69008, France.
Cancers (Basel). 2014 Feb 7;6(1):333-65. doi: 10.3390/cancers6010333.
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).
人类小分子热休克蛋白是分子伴侣，它们在正常未受应激的细胞以及许多癌细胞中调节基本的细胞过程，在这些癌细胞中它们被过度表达。这些蛋白质的特点是其寡聚化和磷酸化状态随细胞生理学而变化。这些结构变化使它们能够与许多不同的客户蛋白相互作用，随后这些客户蛋白表现出修饰的活性和/或半衰期。如今，小分子 Hsp 的蛋白质相互作用组正在进行深入研究，当完成后，这些研究将成为制定旨在调节这些伴侣蛋白功能的治疗策略的关键参数。在这里，我们分析了迄今为止已描述与 HspB1（Hsp27）及其密切成员 HspB5（αB-晶体蛋白）和 HspB4（αA-晶体蛋白）相互作用的几种客户蛋白的潜在致癌作用。
