Journal
ARCHIVES OF VIROLOGY
Volume 158, Issue 12, Pages 2589-2595Publisher
SPRINGER WIEN
DOI: 10.1007/s00705-013-1769-5
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Funding
- Earmarked Fund for Modern Agro-Industry Technology Research System [nycytx-41-G07]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT0978]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- Chinese Special Fund for Agro-Scientific Research in the Public Interest [201303033]
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The Newcastle disease virus (NDV) matrix (M) protein has been demonstrated to be a nuclear-cytoplasmic trafficking protein. Previous studies have shown that the M protein localizes in the nucleus through a bipartite nuclear localization signal. Here, we report that the ability of the M protein to shuttle to the cytoplasm is mediated by three nuclear export signal sequences (NESs). Using leptomycin B (LMB), a specific inhibitor of CRM1, we found that the nuclear export of the three NESs was LMB insensitive and thus was CRM1 independent. In addition, inactivation of these NESs led to nuclear accumulation of the M protein. Our results highlight the significance of these NESs to the nuclear export of the NDV M protein.
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