期刊
JOURNAL OF INFECTIOUS DISEASES
卷 204, 期 -, 页码 S904-S910出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/infdis/jir323
关键词
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资金
- National Institutes of Health [AI059536, U54 AI 057158]
- National Institutes of Health (Northeast Biodefense Center-Lipkin) [5F32AI084453]
- Northeast Center of Excellence for Biodefense
- Emerging Infectious Diseases Research Proteomics Core [U54 AI 057158]
The Ebola virus (EBOV) protein VP24 inhibits type I and II interferon (IFN) signaling by binding to NPI-1 subfamily karyopherin alpha (KPNA) nuclear import proteins, preventing their interaction with tyrosine-phosphorylated STAT1 (phospho-STAT1). This inhibits phospho-STAT1 nuclear import. A biochemical screen now identifies heterogenous nuclear ribonuclear protein complex C1/C2 (hnRNP C1/C2) nuclear import as an additional target of VP24. Co-immunoprecipitation studies demonstrate that hnRNP C1/C2 interacts with multiple KPNA family members, including KPNA1. Interaction with hnRNP C1/C2 occurs through the same KPNA1 C-terminal region (amino acids 424-457) that binds VP24 and phospho-STAT1. The ability of hnRNP C1/C2 to bind KPNA1 is diminished in the presence of VP24, and cells transiently expressing VP24 redistribute hnRNP C1/C2 from the nucleus to the cytoplasm. These data further define the mechanism of hnRNP C1/C2 nuclear import and demonstrate that the impact of EBOV VP24 on nuclear import extends beyond STAT1.
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