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  • Title: Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins.
    Author: Liou YC, Zhou XZ, Lu KP.
    Journal: Trends Biochem Sci; 2011 Oct; 36(10):501-14. PubMed ID: 21852138.
    Abstract:
    Pin1 is a highly conserved enzyme that only isomerizes specific phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Such conformational changes represent a novel and tightly controlled signaling mechanism regulating a spectrum of protein activities in physiology and disease; often through phosphorylation-dependent, ubiquitin-mediated proteasomal degradation. In this review, we summarize recent advances in elucidating the role and regulation of Pin1 in controlling protein stability. We also propose a mechanism by which Pin1 functions as a molecular switch to control the fates of phosphoproteins. We finally stress the need to develop tools to visualize directly Pin1-catalyzed protein conformational changes as a way to determine their roles in the development and treatment of human diseases.
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