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| http://purl.uniprot.org/citations/25360769 | http://www.w3.org/2000/01/rdf-schema#comment | "Hepatitis B virus (HBV) core protein (HBc) can shuttle between nucleus and cytoplasm. Cytoplasm-predominant HBc is clinically associated with severe liver inflammation. Previously, we found that HBc arginine-rich domain (ARD) can associate with a host factor NXF1 (TAP) by coimmunoprecipitation. It is well known that NXF1-p15 heterodimer can serve as a major export receptor of nuclear mRNA as a ribonucleoprotein complex (RNP). In the NXF1-p15 pathway, TREX (transcription/export) complex plays an important role in coupling nuclear pre-mRNA processing with mRNA export in mammalian cells. Here, we tested the hypothesis whether HBc and HBV specific RNA can be exported via the TREX and NXF1-p15 mediated pathway. We demonstrated here that HBc can physically and specifically associate with TREX components, and the NXF1-p15 export receptor by coimmunoprecipitation. Accumulation of HBc protein in the nucleus can be induced by the interference with TREX and NXF1-p15 mediated RNA export machinery. HBV transcripts encodes a non-spliced 3.5 kb pregenomic RNA (pgRNA) which can serve as a template for reverse transcription. Cytoplasmic HBV pgRNA appeared to be reduced by siRNA treatment specific for the NXF1-p15 complex by quantitative RT-qPCR and Northern blot analyses. This result suggests that the pgRNA was also exported via the NXF1-p15 machinery. We entertain the hypothesis that HBc protein can be exported as an RNP cargo via the mRNA export pathway by hijacking the TREX and NXF1-p15 complex. In our current and previous studies, HBc is not required for pgRNA accumulation in the cytoplasm. Furthermore, HBc ARD can mediate nuclear export of a chimeric protein containing HBc ARD in a pgRNA-independent manner. Taken together, it suggests that while both pgRNA and HBc protein exports are dependent on NXF1-p15, they are using the same export machinery in a manner independent of each other."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0106683"xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/author | "Shih C."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/author | "Yang C.C."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/author | "Li H.C."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/author | "Huang E.Y."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/author | "Su P.Y."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/pages | "e106683"xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/title | "Nuclear export of human hepatitis B virus core protein and pregenomic RNA depends on the cellular NXF1-p15 machinery."xsd:string |
| http://purl.uniprot.org/citations/25360769 | http://purl.uniprot.org/core/volume | "9"xsd:string |
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