Synchronized HIV assembly by tunable PIP₂ changes reveals PIP₂ requirement for stable Gag anchoring.

ABSTRACT: 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 depletion of PI(4,5)P₂ completely prevents Gag PM targeting and assembly site formation. Unexpectedly, PI(4,5)P₂ depletion also caused loss of pre-assembled Gag lattices from the PM. Subsequent restoration of PM PI(4,5)P₂ reinduced assembly site formation even in the absence of new protein synthesis, indicating that the dissociated Gag molecules remained assembly competent. These results reveal an important role of PI(4,5)P₂ for HIV-

SUBMITTER: Mucksch F 

PROVIDER: S-EPMC5495570 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature