Please use this identifier to cite or link to this item:
|Title:||West Nile virus capsid protein interaction with importin and HDM2 protein is regulated by protein kinase C-mediated phosphorylation|
|Authors:||Bhuvanakantham, R. |
|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|
|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.|
|Source Title:||Microbes and Infection|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 13, 2019
WEB OF SCIENCETM
checked on Jan 2, 2019
checked on Dec 30, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.