Ministry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Yangzhou, Jiangsu, China.
Arch Virol. 2013 Dec;158(12):2589-95. doi: 10.1007/s00705-013-1769-5. Epub 2013 Jun 27.
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.
新城疫病毒（NDV）基质（M）蛋白已被证明是一种核质穿梭蛋白。先前的研究表明，M 蛋白通过双部分核定位信号定位在细胞核中。在这里，我们报告说，M 蛋白向细胞质穿梭的能力是由三个核输出信号序列（NESs）介导的。使用莱普霉素 B（LMB），一种 CRM1 的特异性抑制剂，我们发现这三个 NES 的核输出对 LMB不敏感，因此与 CRM1 无关。此外，这些 NES 的失活导致 M 蛋白在核内积累。我们的结果强调了这些 NES 对 NDV M 蛋白核输出的重要性。
