G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA

Anaïs Aulas, Guillaume Caron, Christos G Gkogkas, Nguyen-Vi Mohamed, Laurie Destroismaisons, Nahum Sonenberg, Nicole Leclerc, J Alex Parker, Christine Vande Velde

Research output: Contribution to journalArticlepeer-review


G3BP1, a target of TDP-43, is required for normal stress granule (SG) assembly, but the functional consequences of failed SG assembly remain unknown. Here, using both transformed cell lines and primary neurons, we investigated the functional impact of this disruption in SG dynamics. While stress-induced translational repression and recruitment of key SG proteins was undisturbed, depletion of G3BP1 or its upstream regulator TDP-43 disturbed normal interactions between SGs and processing bodies (PBs). This was concomitant with decreased SG size, reduced SG-PB docking, and impaired preservation of polyadenylated mRNA. Reintroduction of G3BP1 alone was sufficient to rescue all of these phenotypes, indicating that G3BP1 is essential for normal SG-PB interactions and SG function.

Original languageEnglish
Pages (from-to)73-84
Number of pages12
JournalJournal of Cell Biology
Issue number1
Publication statusPublished - 6 Apr 2015


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