期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 479, 期 3, 页码 429-433出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.09.043
关键词
Paramyxovirus; Nuclear transport; Nipah virus; W protein; Importin; Exportin
资金
- National Health and Medical Research Council Australia [1003244, 1079211]
- Australian Research Council [DP110101749, DP150102569]
- Meigunyah Trust Grimwade Fellowship
- Senior Principal Research Fellowship [1002486]
- Postgraduate Scholarship [1017904]
- National Health and Medical Research Council of Australia [1079211] Funding Source: NHMRC
Paramyxoviruses replicate in the cytoplasm with no obvious requirement to interact with the nucleus. Nevertheless, the W protein of the highly lethal bat-borne paramyxovirus Nipah virus (NiV) is known to undergo specific targeting to the nucleus, mediated by a single nuclear localisation signal (NLS) within the C-terminal domain. Here, we report for the first time that additional sites modulate nucleocytoplasmic localisation of W. We show that the N-terminal domain interacts with importin alpha 1 and contributes to nuclear accumulation of W, indicative of a novel N-terminal NLS. We also find that W undergoes exportin-1 mediated nuclear export, dependent on a leucine at position 174. Together, these data enable significant revision of the generally accepted model of W trafficking, with implications for understanding of the mechanisms of NiV immune evasion. (C) 2016 Elsevier Inc. All rights reserved.
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