The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
Open accessAbstract
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 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 inhibits, SG formation. G3BP interacts with 40S ribosomal subunits through its RGG motif, which is also required for G3BP-mediated SG formation. We propose that G3BP mediates the condensation of SGs by shifting between two different states that are controlled by binding to Caprin1 or USP10.
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1 retracted
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RetractedA Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
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Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation
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Intrinsically unstructured proteins
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Cited by
G3BP1 is a tunable switch that triggers phase separation to assemble stress granules
Yang, P., Mathieu, C., Kolaitis, R.-M., Zhang, P., Messing, J., Yurtsever, U., Yang, Z., Wu, J., Li, Y., Pan, Q., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.046 · Cited by 1,249
A framework for understanding the functions of biomolecular condensates across scales
Lyon, A. S., Peeples, W. B., & Rosen, M. K. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00303-z · Cited by 895
Stress granules and neurodegeneration
Wolozin, B., & Ivanov, P. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 810
Self-citationCompeting Protein-RNA Interaction Networks Control Multiphase Intracellular Organization
Sanders, D. W., Kedersha, N., Lee, D. S. W., Strom, A. R., Drake, V., Riback, J. A., Bracha, D., Eeftens, J. M., Iwanicki, A., Wang, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.050 · Cited by 773
Self-citationKim, T. H., Tsang, B., Vernon, R. M., Sonenberg, N., Kay, L. E., & Forman-Kay, J. D. (2019) · Science · doi:10.1126/science.aax4240 · Cited by 341
Metadata
- Authors
- Kedersha, N., Panas, M. D., Achorn, C. A., Lyons, S., Tisdale, S., Hickman, T., Thomas, M., Lieberman, J., McInerney, G. M., Ivanov, P., & Anderson, P.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2016-03-28
- Volume
- 212
- Issue
- 7
- Pages
- 845-60
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2311204218
- Cited by
- 659
- References
- 65
- FWCI
- 20.92
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kedersha, N., Panas, M. D., Achorn, C. A., Lyons, S., Tisdale, S., Hickman, T., Thomas, M., Lieberman, J., McInerney, G. M., Ivanov, P., & Anderson, P. (2016). G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits. Journal of Cell Biology. https://doi.org/10.1083/jcb.201508028
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