Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0042642
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dc.titleBinding of translationally controlled tumour protein to the N-terminal domain of HDM2 is inhibited by Nutlin-3
dc.contributor.authorFunston, G.
dc.contributor.authorGoh, W.
dc.contributor.authorWei, S.J.
dc.contributor.authorTng, Q.S.
dc.contributor.authorBrown, C.
dc.contributor.authorJiah Tong, L.
dc.contributor.authorVerma, C.
dc.contributor.authorLane, D.
dc.contributor.authorGhadessy, F.
dc.date.accessioned2014-10-27T08:22:47Z
dc.date.available2014-10-27T08:22:47Z
dc.date.issued2012-08-13
dc.identifier.citationFunston, G., Goh, W., Wei, S.J., Tng, Q.S., Brown, C., Jiah Tong, L., Verma, C., Lane, D., Ghadessy, F. (2012-08-13). Binding of translationally controlled tumour protein to the N-terminal domain of HDM2 is inhibited by Nutlin-3. PLoS ONE 7 (8) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0042642
dc.identifier.issn19326203
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100165
dc.description.abstractTranslationally Controlled Tumour Protein (TCTP), a highly conserved protein present in all eukaryotic organisms, has a number of intracellular and extracellular functions including an anti-apoptotic role. TCTP was recently shown to interact with both p53 and HDM2, inhibiting auto-ubiquitination of the latter and thereby promoting p53 degradation. In this study, we further investigated the interaction between TCTP and HDM2, mapping the reciprocal binding sites of TCTP and HDM2. TCTP primarily interacts with the N-terminal, p53-binding region of HDM2 through its highly basic domain 2. Furthermore, we discovered that Nutlin-3, a small molecule known to promote apoptosis and cell cycle arrest by blocking binding between HDM2 and p53, has a similar inhibitory effect on the interaction of HDM2 and TCTP. This result may provide an additional explanation of how Nutlin-derived compounds currently in clinical trials function to promote apoptosis in cancer cells. © 2012 Funston et al.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1371/journal.pone.0042642
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1371/journal.pone.0042642
dc.description.sourcetitlePLoS ONE
dc.description.volume7
dc.description.issue8
dc.description.page-
dc.identifier.isiut000307500100020
dc.published.statePublished
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