The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein
Open accessAbstract
The multifunctional nucleocapsid (N) protein in SARS-CoV-2 binds the ~30 kb viral RNA genome to aid its packaging into the 80–90 nm membrane-enveloped virion. The N protein is composed of N-terminal RNA-binding and C-terminal dimerization domains that are flanked by three intrinsically disordered regions. Here we demonstrate that the N protein’s central disordered domain drives phase separation with RNA, and that phosphorylation of an adjacent serine/arginine rich region modulates the physical properties of the resulting condensates. In cells, N forms condensates that recruit the stress granule protein G3BP1, highlighting a potential role for N in G3BP1 sequestration and stress granule inhibition. The SARS-CoV-2 membrane (M) protein independently induces N protein phase separation, and three-component mixtures of N + M + RNA form condensates with mutually exclusive compartments containing N + M or N + RNA, including annular structures in which the M protein coats the outside of an N + RNA condensate. These findings support a model in which phase separation of the SARS-CoV-2 N protein contributes both to suppression of the G3BP1-dependent host immune response and to packaging genomic RNA during virion assembly.
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Metadata
- Authors
- Lu, S., Ye, Q., Singh, D., Cao, Y., Diedrich, J. K., Yates, J. R., Villa, E., Cleveland, D. W., & Corbett, K. D.
- Venue
- Nature Communications
- Published
- 2021-01-21
- Volume
- 12
- Issue
- 1
- Pages
- 502-502
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W3125800928
- Cited by
- 462
- References
- 103
- FWCI
- 27.91
- Type
- journal article
- Language
- en
- Open access
- gold
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- Lu, S., Ye, Q., Singh, D., Cao, Y., Diedrich, J. K., Yates, J. R., Villa, E., Cleveland, D. W., & Corbett, K. D. (2021). The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein. Nature Communications. https://doi.org/10.1038/s41467-020-20768-y
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