Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M109.022814
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dc.titlePin1 catalyzes conformational changes of Thr-187 in p27Kip1 and mediates its stability through a polyubiquitination process
dc.contributor.authorZhou, W.
dc.contributor.authorYang, Q.
dc.contributor.authorLow, C.B.
dc.contributor.authorKarthik, B.C.
dc.contributor.authorWang, Y.
dc.contributor.authorRyo, A.
dc.contributor.authorYao, S.Q.
dc.contributor.authorYang, D.
dc.contributor.authorLiou, Y.-C.
dc.date.accessioned2014-10-16T08:37:10Z
dc.date.available2014-10-16T08:37:10Z
dc.date.issued2009-09-04
dc.identifier.citationZhou, W., Yang, Q., Low, C.B., Karthik, B.C., Wang, Y., Ryo, A., Yao, S.Q., Yang, D., Liou, Y.-C. (2009-09-04). Pin1 catalyzes conformational changes of Thr-187 in p27Kip1 and mediates its stability through a polyubiquitination process. Journal of Biological Chemistry 284 (36) : 23980-23988. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M109.022814
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/94535
dc.description.abstractThe cis-trans peptidylprolyl isomerase Pin1 plays a critical role in regulating a subset of phosphoproteins by catalyzing conformational changes on the phosphorylated Ser/Thr-Pro motifs. The phosphorylation-directed ubiquitination is one of the major mechanisms to regulate the abundance of p27Kip1. In this study, we demonstrate that Pin1 catalyzes the cis-trans conformational changes of p27Kip1 and further mediates its stability through the polyubiquitination mechanism. Our results show that the phosphorylated Thr-187-Pro motif in p27Kip1 is a key Pin1-binding site. In addition, NMR analyses show that this phosphorylated Thr-187-Pro site undergoes conformational change catalyzed by Pin1. Moreover, in Pin1 knock-out mouse embryonic fibroblasts, p27Kip1 has a shorter lifetime and displays a higher degree of polyubiquitination than in Pin1 wild-type mouse embryonic fibroblasts, suggesting that Pin1 plays a critical role in regulating p27Kip1 degradation. Additionally, Pin1 dramatically reduces the interaction between p27Kip1 and Cks1, possibly via isomerizing the cis-trans conformation of p27Kip1. Our study thus reveals a novel regulatory mechanism for p27Kip1 stability and sheds new light on the biological function of Pin1 as a general regulator of protein stability. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M109.022814
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1074/jbc.M109.022814
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume284
dc.description.issue36
dc.description.page23980-23988
dc.description.codenJBCHA
dc.identifier.isiut000269380200012
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