Please use this identifier to cite or link to this item:
https://doi.org/10.1016/j.micinf.2010.04.005
DC Field | Value | |
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dc.title | West Nile virus capsid protein interaction with importin and HDM2 protein is regulated by protein kinase C-mediated phosphorylation | |
dc.contributor.author | Bhuvanakantham, R. | |
dc.contributor.author | Cheong, Y.K. | |
dc.contributor.author | Ng, M.-L. | |
dc.date.accessioned | 2011-07-26T06:54:21Z | |
dc.date.available | 2011-07-26T06:54:21Z | |
dc.date.issued | 2010 | |
dc.identifier.citation | Bhuvanakantham, R., Cheong, Y.K., Ng, M.-L. (2010). West Nile virus capsid protein interaction with importin and HDM2 protein is regulated by protein kinase C-mediated phosphorylation. Microbes and Infection 12 (8-9) : 615-625. ScholarBank@NUS Repository. https://doi.org/10.1016/j.micinf.2010.04.005 | |
dc.identifier.issn | 12864579 | |
dc.identifier.issn | 1769714X | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/24767 | |
dc.description.abstract | West Nile virus (WNV) capsid (C) protein was shown to enter the nucleus via importin-mediated pathway and induce apoptosis although the precise regulatory mechanisms for such events have remained elusive. In this study, it was shown that WNV C protein was phosphorylated by protein kinase C (PKC). PKC-mediated phosphorylation influenced nuclear trafficking of C protein by modulating the efficiency of C protein-importin-α binding. Combination of bio-informatics, site-directed mutagenesis, co-immunoprecipitation, immuno-fluorescence and mammalian two-hybrid analyses showed that phosphorylation at amino acid residues residing near (Ser83) or within (Ser99 and Thr100) the bipartite nuclear localization motif of WNV C protein was essential for efficient interaction between C protein and importin-α. In addition, phosphorylation of WNV C protein by PKC was shown to enhance its binding to HDM2 and could subsequently induce p53-dependent apoptosis. Collectively, this study highlighted that phosphorylation is an important post-translational modification required to execute the functions of C protein. © 2010 Elsevier Masson SAS. All rights reserved. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.micinf.2010.04.005 | |
dc.source | Scopus | |
dc.subject | Apoptosis | |
dc.subject | Capsid | |
dc.subject | HDM2 | |
dc.subject | Importin | |
dc.subject | Phosphorylation | |
dc.subject | PKC | |
dc.type | Article | |
dc.contributor.department | MICROBIOLOGY | |
dc.description.doi | 10.1016/j.micinf.2010.04.005 | |
dc.description.sourcetitle | Microbes and Infection | |
dc.description.volume | 12 | |
dc.description.issue | 8-9 | |
dc.description.page | 615-625 | |
dc.identifier.isiut | 000280780100004 | |
Appears in Collections: | Staff Publications |
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