The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Modulation of RNA Condensation by the DEAD-Box Protein eIF4A
Open accessAbstract
SUMMARY 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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1 retracted
RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules
Tourrière, H., Chebli, K., Zekri, L., Courselaud, B., Blanchard, J. M., Bertrand, E., & Tazi, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212128 · Cited by 834
RetractedFiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,100
ImageJ2: ImageJ for the next generation of scientific image data
Rueden, C. T., Schindelin, J., Hiner, M. C., DeZonia, B. E., Walter, A. E., Arena, E. T., & Eliceiri, K. W. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1934-z · Cited by 5,980
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,152
Baker Brachmann, C., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., & Boeke, J. D. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980130)14:2<115::aid-yea204>3.0.co;2-2 · Cited by 3,401
Molecular theory of capillarity
Rowlinson, J. S., & Widom, B. (1982) · Cited by 2,854
Molecular Theory of Capillarity
Rickayzen, G. (1983) · Physics Bulletin · doi:10.1088/0031-9112/34/10/030 · Cited by 2,642
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Coexisting Liquid Phases Underlie Nucleolar Subcompartments
Feric, M., Vaidya, N., Harmon, T. S., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R. W., Pappu, R. V., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,945
Cited by
LNCcation: lncRNA localization and function
Bridges, M. C., Daulagala, A. C., & Kourtidis, A. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202009045 · Cited by 1,556
Competing 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
Integrated lncRNA function upon genomic and epigenomic regulation
Herman, A. B., Tsitsipatis, D., & Gorospe, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.027 · Cited by 747
Capillary forces generated by biomolecular condensates
Gouveia, B., Kim, Y., Shaevitz, J. W., Petry, S., Stone, H. A., & Brangwynne, C. P. (2022) · Nature · doi:10.1038/s41586-022-05138-6 · Cited by 270
Liquid–liquid phase separation underpins the formation of replication factories in rotaviruses
Geiger, F., Acker, J., Papa, G., Wang, X., Arter, W. E., Saar, K. L., Erkamp, N. A., Qi, R., Bravo, J. P., Strauss, S., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021107711 · Cited by 130
Metadata
- Authors
- Tauber, D., Tauber, G., Khong, A., Van Treeck, B., Pelletier, J., & Parker, R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-02
- Volume
- 180
- Issue
- 3
- Pages
- 411-426.e16
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W3000736974
- Cited by
- 281
- References
- 94
- FWCI
- 11.69
- Type
- journal article
- Language
- en
- Open access
- bronze
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