Journal
CELL
Volume 180, Issue 3, Pages 411-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2019.12.031
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Funding
- NSF SCR training grant [T32GM08759]
- Banting Postdoctoral Fellowship
- NIH [GM045443]
- Howard Hughes Medical Institute
- BioFrontiers Institute Advanced Light Microscopy Core Facility (NIST-CU cooperative agreement) [70NANB15H226]
- BioFrontiers Institute Advanced Light Microscopy Core Facility (NIH) [1S10RR026680-01A1]
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Stress granules are condensates of non-translating mRNAs and proteins involved in the stress response and neurodegenerative diseases. Stress granules form in part through intermolecular RNA-RNA interactions, and to better understand how RNA-based condensation occurs, we demonstrate that RNA is effectively recruited to the surfaces of RNA or RNP condensates in vitro. We demonstrate that, through ATP-dependent RNA binding, the DEAD-box protein eIF4A reduces RNA condensation in vitro and limits stress granule formation in cells. This defines a function for eIF4A to limit intermolecular RNA-RNA interactions in cells. These results establish an important role for eIF4A, and potentially other DEAD-box proteins, as ATP-dependent RNA chaperones that limit the condensation of RNA, analogous to the function of proteins like HSP70 in combatting protein aggregates.
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