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Article: PIN1 in Cell Cycle Control and Cancer

TitlePIN1 in Cell Cycle Control and Cancer
Authors
KeywordsCell cycle
Checkpoint
Isomerization
Phosphorylation
PIN1
Issue Date2018
PublisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/pharmacology
Citation
Frontiers in Pharmacology, 2018, v. 9, p. article no. 1367 How to Cite?
AbstractCell cycle progression is tightly controlled by many cell cycle-regulatory proteins that are in turn regulated by a family of cyclin-dependent kinases (CDKs) through protein phosphorylation. The peptidyl-prolyl cis/trans isomerase PIN1 provides a further post-phosphorylation modification and functional regulation of these CDK-phosphorylated proteins. PIN1 specifically binds the phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif of its target proteins and catalyzes the cis/trans isomerization on the pSer/Thr-Pro peptide bonds. Through this phosphorylation-dependent prolyl isomerization, PIN1 fine-tunes the functions of various cell cycle-regulatory proteins including retinoblastoma protein (Rb), cyclin D1, cyclin E, p27, Cdc25C, and Wee1. In this review, we discussed the essential roles of PIN1 in regulating cell cycle progression through modulating the functions of these cell cycle-regulatory proteins. Furthermore, the mechanisms underlying PIN1 overexpression in cancers were also explored. Finally, we examined and summarized the therapeutic potential of PIN1 inhibitors in cancer therapy.
Persistent Identifierhttp://hdl.handle.net/10722/275735
ISSN
2017 Impact Factor: 3.831
2015 SCImago Journal Rankings: 1.845
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorCheng, CW-
dc.contributor.authorTse, E-
dc.date.accessioned2019-09-10T02:48:38Z-
dc.date.available2019-09-10T02:48:38Z-
dc.date.issued2018-
dc.identifier.citationFrontiers in Pharmacology, 2018, v. 9, p. article no. 1367-
dc.identifier.issn1663-9812-
dc.identifier.urihttp://hdl.handle.net/10722/275735-
dc.description.abstractCell cycle progression is tightly controlled by many cell cycle-regulatory proteins that are in turn regulated by a family of cyclin-dependent kinases (CDKs) through protein phosphorylation. The peptidyl-prolyl cis/trans isomerase PIN1 provides a further post-phosphorylation modification and functional regulation of these CDK-phosphorylated proteins. PIN1 specifically binds the phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif of its target proteins and catalyzes the cis/trans isomerization on the pSer/Thr-Pro peptide bonds. Through this phosphorylation-dependent prolyl isomerization, PIN1 fine-tunes the functions of various cell cycle-regulatory proteins including retinoblastoma protein (Rb), cyclin D1, cyclin E, p27, Cdc25C, and Wee1. In this review, we discussed the essential roles of PIN1 in regulating cell cycle progression through modulating the functions of these cell cycle-regulatory proteins. Furthermore, the mechanisms underlying PIN1 overexpression in cancers were also explored. Finally, we examined and summarized the therapeutic potential of PIN1 inhibitors in cancer therapy.-
dc.languageeng-
dc.publisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/pharmacology-
dc.relation.ispartofFrontiers in Pharmacology-
dc.rightsThis Document is Protected by copyright and was first published by Frontiers. All rights reserved. It is reproduced with permission.-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectCell cycle-
dc.subjectCheckpoint-
dc.subjectIsomerization-
dc.subjectPhosphorylation-
dc.subjectPIN1-
dc.titlePIN1 in Cell Cycle Control and Cancer-
dc.typeArticle-
dc.identifier.emailCheng, CW: timwai@hku.hk-
dc.identifier.emailTse, E: ewctse@hku.hk-
dc.identifier.authorityTse, E=rp00471-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3389/fphar.2018.01367-
dc.identifier.pmid30534074-
dc.identifier.pmcidPMC6275231-
dc.identifier.scopuseid_2-s2.0-85057858994-
dc.identifier.hkuros303716-
dc.identifier.volume9-
dc.identifier.spagearticle no. 1367-
dc.identifier.epagearticle no. 1367-
dc.publisher.placeSwitzerland-

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