The cytoplasmic tail of HIV-1 gp160 contains regions that associate with cellular membranes
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Updated: Aug 8, 2026

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
Published on: March 8, 2012
O K Haffar1, D J Dowbenko, P W Berman
1Department of Developmental Biology, Genentech, Inc., South San Francisco, California 94080.
Abstract:
The HIV-1 envelope glycoprotein gp160 associates with cellular membranes via a discrete transmembrane domain. Unlike other retroviral envelope proteins, however, gp160 also forms a secondary association with the lipid bilayer mediated by one or more regions located in the cytoplasmic tail. We have expressed the full cytoplasmic tail sequence of gp160, as a fusion protein with the HSV-1 glycoprotein D signal sequence, transiently in a human embryonic kidney cell line. Our results show that in the absence of any defined transmembrane domain or stop transfer sequence, the protein corresponding to the cytoplasmic tail of HIV-1 gp160 formed stable interactions with cellular membranes that mediated its export to the cell surface.
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