Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.121368
DC FieldValue
dc.titlePin1 acts as a negative regulator of the G2/M transition by interacting with the Aurora-A-Bora complex
dc.contributor.authorLee, Y.-C.
dc.contributor.authorQue, J.
dc.contributor.authorChen, Y.-C.
dc.contributor.authorLin, J.-T.
dc.contributor.authorLiou, Y.-C.
dc.contributor.authorLiao, P.-C.
dc.contributor.authorLiu, Y.-P.
dc.contributor.authorLee, K.-H.
dc.contributor.authorLin, L.-C.
dc.contributor.authorHsiao, M.
dc.contributor.authorHung, L.Y.
dc.contributor.authorHuang, C.-Y.
dc.contributor.authorLu, P.-J.
dc.date.accessioned2014-10-27T08:36:49Z
dc.date.available2014-10-27T08:36:49Z
dc.date.issued2013-11-01
dc.identifier.citationLee, Y.-C., Que, J., Chen, Y.-C., Lin, J.-T., Liou, Y.-C., Liao, P.-C., Liu, Y.-P., Lee, K.-H., Lin, L.-C., Hsiao, M., Hung, L.Y., Huang, C.-Y., Lu, P.-J. (2013-11-01). Pin1 acts as a negative regulator of the G2/M transition by interacting with the Aurora-A-Bora complex. Journal of Cell Science 126 (21) : 4862-4872. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.121368
dc.identifier.issn00219533
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101402
dc.description.abstractPin1 was the first prolyl isomerase identified that is involved in cell division. The mechanism by which Pin1 acts as a negative regulator of mitotic activity in G2 phase remains unclear. Here, we found that Aurora A can interact with and phosphorylate Pin1 at Ser16, which suppresses the G2/M function of Pin1 by disrupting its binding ability and mitotic entry. Our results also show that phosphorylation of Bora at Ser274 and Ser278 is crucial for binding of Pin1. Through the interaction, Pin1 can alter the cytoplasmic translocation of Bora and promote premature degradation by β-TrCP, which results in a delay in mitotic entry. Together with the results that Pin1 protein levels do not significantly fluctuate during cell-cycle progression and Aurora A suppresses Pin1 G2/M function, our data demonstrate that a gain of Pin1 function can override the Aurora-A-mediated functional suppression of Pin1. Collectively, these results highlight the physiological significance of Aurora-A-mediated Pin1 Ser16 phosphorylation for mitotic entry and the suppression of Pin1 is functionally linked to the regulation of mitotic entry through the Aurora-A-Bora complex. © 2013. Published by The Company of Biologists Ltd.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1242/jcs.121368
dc.sourceScopus
dc.subjectAurora a
dc.subjectBora
dc.subjectG2/M negative regulator
dc.subjectPin1
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1242/jcs.121368
dc.description.sourcetitleJournal of Cell Science
dc.description.volume126
dc.description.issue21
dc.description.page4862-4872
dc.description.codenJNCSA
dc.identifier.isiut000326392500008
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

24
checked on Sep 25, 2020

WEB OF SCIENCETM
Citations

24
checked on Sep 25, 2020

Page view(s)

59
checked on Sep 19, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.