Synchronized HIV assembly by tunable PIP2 changes reveals PIP2 requirement for stable Gag anchoring
HIV-1 assembles at the plasma membrane (PM) of infected cells. PM association of the main structural protein Gag depends on its myristoylated MA domain and PM PI(4,5)P2. Using a novel chemical biology tool that allows rapidly tunable manipulation of PI(4,5)P2 levels in living cells, we show that dep...
Main Authors: | , , , , |
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Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2017-06-01
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Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/25287 |