Please use this identifier to cite or link to this item: https://doi.org/10.3389/fonc.2018.00469
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dc.titleGears-in-motion: The interplay of WW and PPIase domains in PIN1
dc.contributor.authorLee, Y.M.
dc.contributor.authorLiou, Y.-C.
dc.date.accessioned2021-11-16T09:29:50Z
dc.date.available2021-11-16T09:29:50Z
dc.date.issued2018
dc.identifier.citationLee, Y.M., Liou, Y.-C. (2018). Gears-in-motion: The interplay of WW and PPIase domains in PIN1. Frontiers in Oncology 8 (OCT) : 469. ScholarBank@NUS Repository. https://doi.org/10.3389/fonc.2018.00469
dc.identifier.issn2234-943X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/206476
dc.description.abstractPin1 belongs to the family of the peptidyl-prolyl cis-trans isomerase (PPIase), which is a class of enzymes that catalyze the cis/trans isomerization of the Proline residue. Pin1 is unique and only catalyzes the phosphorylated Serine/Threonine-Proline (S/T-P) motifs of a subset of proteins. Since the discovery of Pin1 as a key protein in cell cycle regulation, it has been implicated in numerous diseases, ranging from cancer to neurodegenerative diseases. The main features of Pin1 lies in its two main domains: the WW (two conserved tryptophan) domain and the PPIase domain. Despite extensive studies trying to understand the mechanisms of Pin1 functions, how these two domains contribute to the biological roles of Pin1 in cellular signaling requires more investigations. The WW domain of Pin1 is known to have a higher affinity to its substrate than that of the PPIase domain. Yet, the WW domain seems to prefer the trans configuration of phosphorylated S/TP motif, while the PPIase catalyzes the cis to trans isomerasion. Such contradicting information has generated much confusion as to the actual mechanism of Pin1 function. In addition, dynamic allostery has been suggested to be important for Pin1 function. Henceforth, in this review, we will be looking at the progress made in understanding the function of Pin1, and how these understandings can aid us in overcoming the diseases implicated by Pin1 such as cancer during drug development. © 2018 Lee and Liou.
dc.publisherFrontiers Media S.A.
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2018
dc.subjectCancer target
dc.subjectDrug development
dc.subjectInterdomain communication
dc.subjectPeptidyl-prolyl cis/trans isomerase (PPIase)
dc.subjectPhosphorylation
dc.subjectPin1
dc.subjectWW domain
dc.typeReview
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.3389/fonc.2018.00469
dc.description.sourcetitleFrontiers in Oncology
dc.description.volume8
dc.description.issueOCT
dc.description.page469
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