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  • 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

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Retrovirology20063 (Suppl 1) :S106

https://doi.org/10.1186/1742-4690-3-S1-S106

  • Published:

Keywords

  • Infectious Disease
  • Cancer Research
  • Molecular Recognition
  • Nuclear Export
  • Nuclear Import

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.

Authors’ Affiliations

(1)
Centre for Research in Infectious Diseases, Conway Institute, University College Dublin, Dublin, Ireland

Copyright

© Gu et al; licensee BioMed Central Ltd. 2006

This article is published under license to BioMed Central Ltd.

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