- Oral presentation
- Open Access
The human I-mfa domain containing protein, HIC, interacts with HIV-1 Tat and Rev and sequesters them in the cytoplasm
Retrovirology volume 3, Article number: S106 (2006)
Tat and Rev are equally critical for HIV-1 replication and work in a sequential manner: first, transactivation of the HIV-1 LTR by Tat, followed by nuclear export of partially spliced and unspliced viral transcripts by Rev. Both functions require Tat and Rev to be imported to the nucleus, a process mediated by molecular recognition of their homologous arginine-rich NLS domains by importin-β.
Here, we report the interaction of the human I-mfa domain containing protein, HIC, with Tat and Rev resulting in the cytoplasmic redistribution of Tat and Rev with a concomitant reduction in their nuclear accumulation. We will discuss our data resulting from colocalisation studies and competitive in vitro nuclear import assays, which collectively support a model where HIC would mask Tat and Rev NLS domains, thereby impairing their nuclear import via rendering the NLS inaccessible to importin-β.
Functionally, this cytoplasmic sequestration could appear to represent a novel mechanism for the control of Tat and Rev activities and ultimately the regulation of HIV-1 replication.
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Gu, L., Gautier, V., Sheehy, N. et al. The human I-mfa domain containing protein, HIC, interacts with HIV-1 Tat and Rev and sequesters them in the cytoplasm. Retrovirology 3, S106 (2006). https://doi.org/10.1186/1742-4690-3-S1-S106
- Infectious Disease
- Cancer Research
- Molecular Recognition
- Nuclear Export
- Nuclear Import