期刊
MICROBES AND INFECTION
卷 12, 期 8-9, 页码 615-625出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.micinf.2010.04.005
关键词
Apoptosis; Capsid; HDM2; Importin; Phosphorylation; PKC
资金
- Biomedical Research Council, Singapore [BMRC/01/1/21/18/003]
- National University of Singapore, Singapore [R-182-000-055-112]
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-alpha 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-alpha. 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. (c) 2010 Elsevier Masson SAS. All rights reserved.
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