Date Published:
04/2004

Publication Type:
Journal Article

Authors:

K. Hsu
J. Seharaseyon
P. Dong
S. Bour
E. Marban

Secondary:
Molecular Cell

Volume:
14

Pagination:
259-67

Issue:
2

URL:
https://pubmed.ncbi.nlm.nih.gov/

Keywords:
beta-Transducin Repeat-Containing Proteins;Blotting;Consensus Sequence;Conserved Sequence;External;Gene Expression Regulation;Genes;Human Immunodeficiency Virus Proteins;Hydrogen-Ion Concentration;Ion Channels;Patch-Clamp;Viral;Western

Abstract:
<p>Sequence analysis predicted significant structural homology between the HIV-1 accessory protein Vpu and the N-terminal region of TASK-1, a mammalian background K(+) channel. If the homology resulted from molecular piracy during HIV-1 evolution, these two proteins may have important functional interactions. Here we demonstrate that TASK and Vpu physically interact in cultured cells and in AIDS lymphoid tissues. The functional consequences were potentially destructive for both components: Vpu abolished TASK-1 current, while overexpressing TASK led to a marked impairment of Vpu's ability to enhance viral particle release. Further, the first 40 amino acids of TASK-1 (part of the homology to Vpu) were capable of enhancing HIV-1 particle release. This virus-host interaction may influence HIV-1/AIDS progression, as well as electrical signaling in infected host tissues.</p>