Hsp90 Activation and Cell Cycle Regulation

摘要: The widely-expressed molecular chaperone heat shock protein 90 (Hsp90) regulates several important cellular processes via its' repertoire of 'client' proteins. Signal transduction pathways controlled by Hsp90 contribute to all major components the malignant phenotype, so inhibitors are under investigation as anticancer agents. Since is also expressed at high levels in many normal tissues, it was unclear why such 17-allylamino-geldanamycin (17-AAG) have selective antitumor activity animals and well tolerated clinically. Recent findings indicate that largely latent unstressed cells, but tumor becomes completely utilized during progression, resulting an activation-dependent conformational shift radically increases 17-AAG binding affinity cancer cells. In this article, implications discovery discussed, with particular reference cell cycle regulation consequences inducing arrest inhibitors.