Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 36, Issue 10, Pages 501-514Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2011.07.001
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Funding
- BMRC [09/1/21119/604, SSCC-09-020]
- MOE, Singapore [MOE2009-T2-2-111]
- NIH [R01CA122434, R01GM058556, AG017870]
- Alliance for Lupus Research grant
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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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