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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Detalles Bibliográficos
Autores principales: Mücksch, Frauke, Laketa, Vibor, Müller, Barbara, Schultz, Carsten, Kräusslich, Hans-Georg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Cell Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495570/
https://www.ncbi.nlm.nih.gov/pubmed/28574338
http://dx.doi.org/10.7554/eLife.25287

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495570/
https://www.ncbi.nlm.nih.gov/pubmed/28574338
http://dx.doi.org/10.7554/eLife.25287

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