Journal
MOLECULAR CELL
Volume 79, Issue 6, Pages 978-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2020.08.004
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Funding
- NIH [T-32-GM007315, R01 GM122803]
- AACR prostate cancer research fellowship
- NCI-SPORE Career Enhancement Award
- University of Michigan Comprehensive Cancer Center/Biointerfaces Institute research grant
- NCI Prostate SPORE [P50 CA186786]
- NSF MRI-ID grant [DBI-0959823]
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Processing bodies (PBs) and stress granules (SGs) are prominent examples of subcellular, membraneless compartments that are observed under physiological and stress conditions, respectively. We observe that the trimeric PB protein DCP1A rapidly (within similar to 10 s) phase-separates in mammalian cells during hyperosmotic stress and dissolves upon isosmotic rescue (over similar to 100 s) with minimal effect on cell viability even after multiple cycles of osmotic perturbation. Strikingly, this rapid intracellular hyperosmotic phase separation (HOPS) correlates with the degree of cell volume compression, distinct from SG assembly, and is exhibited broadly by homo-multimeric (valency >= 2) proteins across several cell types. Notably, HOPS sequesters pre-mRNA cleavage factor components from actively transcribing genomic loci, providing a mechanism for hyperosmolarity-induced global impairment of transcription termination. Our data suggest that the multimeric proteome rapidly responds to changes in hydration and molecular crowding, revealing an unexpected mode of globally programmed phase separation and sequestration.
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