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Synchronized HIV assembly by tunable PIP(2) changes reveals PIP(2) 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)P(2). Using a novel chemical biology tool that allows rapidly tunable manipulation of PI(4,5)P(2) levels in living cells, we show that...
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| Publicado no: | eLife |
|---|---|
| Main Authors: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
eLife Sciences Publications, Ltd
2017
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5495570/ https://ncbi.nlm.nih.gov/pubmed/28574338 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.25287 |
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