Characterization of HIV-1 Vpr Nuclear Import: Analysis of Signals and Pathways
| العنوان: | Characterization of HIV-1 Vpr Nuclear Import: Analysis of Signals and Pathways |
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| المؤلفون: | Yonchu Jenkins, Karsten Weis, Warner C. Greene, Michele McEntee |
| المصدر: | The Journal of Cell Biology The Journal of cell biology, vol 143, iss 4 |
| بيانات النشر: | Rockefeller University Press, 1998. |
| سنة النشر: | 1998 |
| مصطلحات موضوعية: | viruses, Nuclear Localization Signals, medicine.disease_cause, Medical and Health Sciences, Competitive, Nuclear protein, Nuclear pore, Hydrolysis, Nuclear Proteins, virus diseases, vpr Gene Products, Human Immunodeficiency Virus, Biological Sciences, Cell biology, medicine.anatomical_structure, Lac Operon, Biochemistry, Karyopherins, Guanosine Triphosphate, Human Immunodeficiency Virus, Signal Transduction, vpr Gene Products, Nuclear Envelope, preintegration complex, Viral protein, Virus Integration, Vpr, Biology, Transfection, Binding, Competitive, nuclear pore complex, medicine, Gene Products, Humans, NLS, Gene Products, vpr, HIV, Cell Biology, Binding, nuclear import, Peptide Fragments, Cell nucleus, ran GTP-Binding Protein, Hela Cells, HIV-1, Nuclear transport, Nuclear localization sequence, Developmental Biology, HeLa Cells, Regular Articles |
| الوصف: | While the Vpr protein of HIV-1 has been implicated in import of the viral preintegration complex across the nuclear pore complex (NPC) of nondividing cellular hosts, the mechanism by which Vpr enters the nucleus remains unknown. We now demonstrate that Vpr contains two discrete nuclear targeting signals that use two different import pathways, both of which are distinct from the classical nuclear localization signal (NLS)- and the M9-dependent pathways. Vpr import does not appear to require Ran-mediated GTP hydrolysis and persists under conditions of low energy. Competition experiments further suggest that Vpr directly engages the NPC at two discrete sites. These sites appear to form distal components of a common import pathway used by NLS- and M9-containing proteins. Together, our data suggest that Vpr bypasses many of the soluble receptors involved in import of cellular cargoes. Rather, this viral protein appears to directly access the NPC, a property that may help to ensure the capacity of HIV to replicate in nondividing cellular hosts. |
| وصف الملف: | application/pdf |
| تدمد: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.143.4.875 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c87362f61138c80f0b55331cbe0551b2 https://doi.org/10.1083/jcb.143.4.875 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....c87362f61138c80f0b55331cbe0551b2 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15408140 00219525 |
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| DOI: | 10.1083/jcb.143.4.875 |