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Trends Biochem Sci. 2011 Oct;36(10):501-14. doi: 10.1016/j.tibs.2011.07.001. Epub 2011 Aug 17.

Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins.

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1
Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543. dbslyc@nus.edu.sg

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.

PMID:
21852138
PMCID:
PMC3185210
DOI:
10.1016/j.tibs.2011.07.001
[Indexed for MEDLINE]
Free PMC Article

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