The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
RNA buffers the phase separation behavior of prion-like RNA binding proteins
Open accessAbstract
RNA and membraneless organelles: Membraneless compartments can form in cells through liquidliquid phase separation (see the Perspective by Polymenidou). But what prevents these cellular condensates from randomly fusing together? Using the RNA-binding protein (RBP) Whi3, Langdon et al. demonstrated that the secondary structure of different RNA components determines the distinct biophysical and biological properties of the two types of condensates that Whi3 forms. Several RBPs, such as FUS and TDP43, contain prion-like domains and are linked to neurodegenerative diseases. These RBPs are usually soluble in the nucleus but can form pathological aggregates in the cytoplasm. Maharana et al. showed that local RNA concentrations determine distinct phase separation behaviors in different subcellular locations. The higher RNA concentrations in the nucleus act as a buffer to prevent phase separation of RBPs; when mislocalized to the cytoplasm, lower RNA concentrations trigger aggregation. Science , this issue p. 922 , p. 918 ; see also p. 859
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Cites
Principles of Fluorescence Spectroscopy
(2006) · Springer eBooks · doi:10.1007/978-0-387-46312-4 · Cited by 19,339
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
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
Self-citationLiquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,152
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 3,282
Self-citationMolliex, A., Temirov, J., Lee, J., Coughlin, M., Kanagaraj, A. P., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,893
Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
Vance, C., Rogelj, B., Hortobágyi, T., De Vos, K. J., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B., Ruddy, D., Wright, P., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,564
Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J., Kasarskis, E. J., Munsat, T., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,553
Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,066
Clemson, C. M., Hutchinson, J. N., Sara, S. A., Ensminger, A. W., Fox, A. H., Chess, A., & Lawrence, J. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.026 · Cited by 1,445
Cited by
Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856
Self-citationWang, J., Choi, J.-M., Holehouse, A. S., Lee, H. O., Zhang, X., Jahnel, M., Maharana, S., Lemaitre, R., Pozniakovsky, A., Drechsel, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.006 · Cited by 2,076
Self-citationBiomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,160
Self-citationLiquid–Liquid Phase Separation in Disease
Alberti, S., & Dormann, D. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043527 · Cited by 868
Self-citationα‐Synuclein aggregation nucleates through liquid‐liquid phase separation
Ray, S., Singh, N., Kumar, R., Patel, K., Pandey, S., Datta, D., Mahato, J., Panigrahi, R., Navalkar, A., Mehra, S., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0465-9 · Cited by 863
Metadata
- Authors
- Maharana, S., Wang, J., Papadopoulos, D. K., Richter, D., Pozniakovsky, A., Poser, I., Bickle, M., Rizk, S., Guillén-Boixet, J., Franzmann, T. M., Jahnel, M., Marrone, L., Chang, Y.-T., Sterneckert, J., Tomancak, P., Hyman, A. A., & Alberti, S.
- Venue
- Science
- Published
- 2018-05-25
- Volume
- 360
- Issue
- 6391
- Pages
- 918-921
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2797600975
- Cited by
- 1,106
- References
- 54
- FWCI
- 37.20
- Type
- journal article
- Language
- en
- Open access
- green
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- Maharana, S., Wang, J., Papadopoulos, D. K., Richter, D., Pozniakovsky, A., Poser, I., Bickle, M., Rizk, S., Guillén-Boixet, J., Franzmann, T. M., Jahnel, M., Marrone, L., Chang, Y.-T., Sterneckert, J., Tomancak, P., Hyman, A. A., & Alberti, S. (2018). RNA buffers the phase separation behavior of prion-like RNA binding proteins. Science. https://doi.org/10.1126/science.aar7366
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