Please use this identifier to cite or link to this item: https://doi.org/10.1128/JVI.79.17.11476-11486.2005
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dc.titleThe severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation
dc.contributor.authorSurjit, M.
dc.contributor.authorKumar, R.
dc.contributor.authorMishra, R.N.
dc.contributor.authorReddy, M.K.
dc.contributor.authorChow, V.T.K.
dc.contributor.authorLal, S.K.
dc.date.accessioned2016-11-17T08:38:52Z
dc.date.available2016-11-17T08:38:52Z
dc.date.issued2005-09
dc.identifier.citationSurjit, M., Kumar, R., Mishra, R.N., Reddy, M.K., Chow, V.T.K., Lal, S.K. (2005-09). The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation. Journal of Virology 79 (17) : 11476-11486. ScholarBank@NUS Repository. https://doi.org/10.1128/JVI.79.17.11476-11486.2005
dc.identifier.issn0022538X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/130582
dc.description.abstractThe severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid (N) protein is one of the four structural proteins of the virus and is predicted to be a 46-kDa phosphoprotein. Our in silico analysis predicted N to be heavily phosphorylated at multiple residues. Experimentally, we have shown in this report that the N protein of the SARS-CoV gets serine-phosphorylated by multiple kinases, in both the cytoplasm and the nucleus. The phosphoprotein is stable and localizes in the cytoplasm and coprecipitates with the membrane fraction. Also, using specific inhibitors of phosphorylation and an in vitro phosphorylation assay, we show that the nucleocapsid protein is a substrate of cyclin-dependent kinase (CDK), glycogen synthase kinase, mitogen-activated protein kinase, and casein kinase II. Further, we show that the phosphorylated protein is translocated to the cytoplasm by binding to 14-3-3 (tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein). 14-3-3 proteins are a family of highly conserved, ubiquitously expressed eukaryotic proteins that function primarily as adapters that modulate interactions between components of various cellular signaling and cell cycle regulatory pathways through phosphorylation-dependent protein-protein interactions. Coincidentally, the N protein was also found to downregulate the expression of the theta isoform of 14-3-3 (14-3-3θ), leading to the accumulation of phosphorylated N protein in the nucleus, in the absence of growth factors. Using short interfering RNA specific to 14-3-3θ we have inhibited its expression to show accumulation of phosphorylated N protein in the nucleus. Thus, the data presented here provide a possible mechanism for phosphorylation-dependent nucleocytoplasmic shuttling of the N protein. This 14-3-3-mediated transport of the phosphorylated N protein and its possible implications in interfering with the cellular machinery are discussed. Copyright © 2005, American Society for Microbiology. All Rights Reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1128/JVI.79.17.11476-11486.2005
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1128/JVI.79.17.11476-11486.2005
dc.description.sourcetitleJournal of Virology
dc.description.volume79
dc.description.issue17
dc.description.page11476-11486
dc.description.codenJOVIA
dc.identifier.isiut000231303900062
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