Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.tibs.2011.07.001
Title: Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Authors: Liou, Y.-C. 
Zhou, X.Z.
Lu, K.P.
Issue Date: Oct-2011
Citation: Liou, Y.-C., Zhou, X.Z., Lu, K.P. (2011-10). Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins. Trends in Biochemical Sciences 36 (10) : 501-514. ScholarBank@NUS Repository. https://doi.org/10.1016/j.tibs.2011.07.001
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. © 2011 Elsevier Ltd.
Source Title: Trends in Biochemical Sciences
URI: http://scholarbank.nus.edu.sg/handle/10635/102515
ISSN: 09680004
DOI: 10.1016/j.tibs.2011.07.001
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