Please use this identifier to cite or link to this item: https://doi.org/10.1128/MCB.01159-10
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dc.titleImportin beta plays an essential role in the regulation of the LysRS-Ap4A pathway in immunologically activated mast cells
dc.contributor.authorCarmi-Levy, I.
dc.contributor.authorMotzik, A.
dc.contributor.authorOfir-Birin, Y.
dc.contributor.authorYagil, Z.
dc.contributor.authorYang, C.M.
dc.contributor.authorKemeny, D.M.
dc.contributor.authorHan, J.M.
dc.contributor.authorKim, S.
dc.contributor.authorKay, G.
dc.contributor.authorNechushtan, H.
dc.contributor.authorSuzuki, R.
dc.contributor.authorRivera, J.
dc.contributor.authorRazin, E.
dc.date.accessioned2016-09-06T08:19:08Z
dc.date.available2016-09-06T08:19:08Z
dc.date.issued2011-05
dc.identifier.citationCarmi-Levy, I., Motzik, A., Ofir-Birin, Y., Yagil, Z., Yang, C.M., Kemeny, D.M., Han, J.M., Kim, S., Kay, G., Nechushtan, H., Suzuki, R., Rivera, J., Razin, E. (2011-05). Importin beta plays an essential role in the regulation of the LysRS-Ap4A pathway in immunologically activated mast cells. Molecular and Cellular Biology 31 (10) : 2111-2121. ScholarBank@NUS Repository. https://doi.org/10.1128/MCB.01159-10
dc.identifier.issn02707306
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/126728
dc.description.abstractWe recently reported that diadenosine tetraphosphate hydrolase (Ap4A hydrolase) plays a critical role in gene expression via regulation of intracellular Ap4A levels. This enzyme serves as a component of our newly described lysyl tRNA synthetase (LysRS)-Ap4A biochemical pathway that is triggered upon immunological challenge. Here we explored the mechanism of this enzyme's translocation into the nucleus and found its immunologically dependent association with importin beta. Silencing of importin beta prevented Ap4A hydrolase nuclear translocation and affected the local concentration of Ap4A, which led to an increase in microphthalmia transcription factor (MITF) transcriptional activity. Furthermore, immunological activation of mast cells resulted in dephosphorylation of Ap4A hydrolase, which changed the hydrolytic activity of the enzyme. © 2011, American Society for Microbiology.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1128/MCB.01159-10
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1128/MCB.01159-10
dc.description.sourcetitleMolecular and Cellular Biology
dc.description.volume31
dc.description.issue10
dc.description.page2111-2121
dc.description.codenMCEBD
dc.identifier.isiut000289936600016
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