G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
Brigham and Women's Hospital · Harvard University · +3 more institutions
Abstract
Mammalian stress granules (SGs) contain stalled translation preinitiation complexes that are assembled into discrete granules by specific RNA-binding proteins such as G3BP. We now show that cells lacking both G3BP1 and G3BP2 cannot form SGs in response to eukaryotic initiation factor 2α phosphorylation or eIF4A inhibition, but are still SG-competent when challenged with severe heat or osmotic stress. Rescue experiments using G3BP1 mutants show that phosphomimetic G3BP1-S149E fails to rescue SG formation, whereas G3BP1-F33W, a mutant unable to bind G3BP partner proteins Caprin1 or USP10, rescues SG formation. Caprin1/USP10 binding to G3BP is mutually exclusive: Caprin binding promotes, but USP10 binding…
Citation impact
- FWCI
- 28.03
- Percentile
- 100%
- References
- 66
Authors
11- NKNancy KedershaCorresponding
Brigham and Women's Hospital, Harvard University
- MDMarc D. Panas
Brigham and Women's Hospital, Harvard University
- CAChristopher A. Achorn
Brigham and Women's Hospital, Harvard University
- SMShawn M. Lyons
Brigham and Women's Hospital, Harvard University
- STSarah Tisdale
Brigham and Women's Hospital, Harvard University
Topics & keywords
- Stress granule
- Cell biology
- eIF4A
- Phosphorylation
- Eukaryotic Small Ribosomal Subunit
- Eukaryotic translation
- Eukaryotic initiation factor
- Binding site