The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles
Open accessAbstract
Prion-like domains (PLDs) are low complexity sequences found in RNA binding proteins associated with the neurodegenerative disorder amyotrophic lateral sclerosis. Recently, PLDs have been implicated in mediating gene regulation via liquid-phase transitions that drive ribonucleoprotein granule assembly. In this paper, we report many PLDs in proteins associated with paraspeckles, subnuclear bodies that form around long noncoding RNA. We mapped the interactome network of paraspeckle proteins, finding enrichment of PLDs. We show that one protein, RBM14, connects key paraspeckle subcomplexes via interactions mediated by its PLD. We further show that the RBM14 PLD, as well as the PLD of another essential paraspeckle protein, FUS, is required to rescue paraspeckle formation in cells in which their endogenous counterpart has been knocked down. Similar to FUS, the RBM14 PLD also forms hydrogels with amyloid-like properties. These results suggest a role for PLD-mediated liquid-phase transitions in paraspeckle formation, highlighting this nuclear body as an excellent model system for understanding the perturbation of such processes in neurodegeneration.
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Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012
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
Self-citationIdentification and characterization of FUS/TLS as a new target of ATM
Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J. (2008) · Biochemical Journal · doi:10.1042/bj20081135 · Cited by 111
Cited by
Principles and Properties of Stress Granules
Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,728
Yamazaki, T., Souquere, S., Chujo, T., Kobelke, S., Chong, Y. S., Fox, A. H., Bond, C. S., Nakagawa, S., Pierron, G., & Hirose, T. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.019 · Cited by 594
Self-citationThe expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Paraspeckles: Where Long Noncoding RNA Meets Phase Separation
Fox, A. H., Nakagawa, S., Hirose, T., & Bond, C. S. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.12.001 · Cited by 441
Self-citationRNA-binding proteins with prion-like domains in health and disease
Harrison, A. F., & Shorter, J. (2017) · Biochemical Journal · doi:10.1042/bcj20160499 · Cited by 422
Metadata
- Authors
- Hennig, S., Kong, G., Mannen, T., Sadowska, A., Kobelke, S., Blythe, A., Knott, G. J., Iyer, K. S., Ho, D., Newcombe, E. A., Hosoki, K., Goshima, N., Kawaguchi, T., Hatters, D., Trinkle-Mulcahy, L., Hirose, T., Bond, C. S., & Fox, A. H.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2015-08-17
- Volume
- 210
- Issue
- 4
- Pages
- 529-539
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1901046087
- Cited by
- 336
- References
- 3
- FWCI
- 10.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles. https://app.cochat.ai/papers/10.1083/jcb.201504117
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- Hennig, S., Kong, G., Mannen, T., Sadowska, A., Kobelke, S., Blythe, A., Knott, G. J., Iyer, K. S., Ho, D., Newcombe, E. A., Hosoki, K., Goshima, N., Kawaguchi, T., Hatters, D., Trinkle-Mulcahy, L., Hirose, T., Bond, C. S., & Fox, A. H. (2015). Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles. Journal of Cell Biology. https://doi.org/10.1083/jcb.201504117
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
