The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
Open accessAbstract
In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade initiated by cytosolic calcium concentration elevation. Members of the OSCA family in Arabidopsis thaliana , identified as the hyperosmolality-gated calcium-permeable channels, have been suggested to play a key role during the initial phase of hyperosmotic stress response. Here, we report the atomic structure of Arabidopsis OSCA1.2 determined by single-particle cryo-electron microscopy. It contains 11 transmembrane helices and forms a homodimer. It is in an inactivated state, and the pore-lining residues are clearly identified. Its cytosolic domain contains a RNA recognition motif and two unique long helices. The linker between these two helices forms an anchor in the lipid bilayer and may be essential to osmosensing. The structure of AtOSCA1.2 serves as a platform for the study of the mechanism underlying osmotic stress responses and mechanosensing.
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Citations
Cites
Piezo1 and Piezo2 Are Essential Components of Distinct Mechanically Activated Cation Channels
Coste, B., Mathur, J., Schmidt, M., Earley, T. J., Ranade, S., Petrus, M. J., Dubin, A. E., & Patapoutian, A. (2010) · Science · doi:10.1126/science.1193270 · Cited by 3,316
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Structure of the mechanically activated ion channel Piezo1
Saotome, K., Murthy, S. E., Kefauver, J. M., Whitwam, T., Patapoutian, A., & Ward, A. B. (2018) · Nature · doi:10.1038/nature25453 · Cited by 649
Structure-based membrane dome mechanism for Piezo mechanosensitivity
Guo, Y. R., & MacKinnon, R. (2017) · eLife · doi:10.7554/elife.33660 · Cited by 446
Cryo-EM structures of the TMEM16A calcium-activated chloride channel
Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., et al. (2017) · Nature · doi:10.1038/nature25024 · Cited by 333
Kurusu, T., Nishikawa, D., Yamazaki, Y., Gotoh, M., Nakano, M., Hamada, H., Yamanaka, T., Iida, K., Nakagawa, Y., Saji, H., et al. (2012) · BMC Plant Biology · doi:10.1186/1471-2229-12-11 · Cited by 130
Cited by
How Plants Sense and Respond to Stressful Environments
Lamers, J., van der Meer, T., & Testerink, C. (2020) · Plant Physiology · doi:10.1104/pp.19.01464 · Cited by 512
Davis, M. J., Earley, S., Li, Y.-S., & Chien, S. (2023) · Physiological Reviews · doi:10.1152/physrev.00053.2021 · Cited by 273
Jojoa-Cruz, S., Burendei, B., Lee, W.-H., & Ward, A. B. (2024) · Structure · doi:10.1016/j.str.2023.11.009 · Cited by 20
Giese, A. P. J., Weng, W.-H., Kindt, K. S., Chang, H. H. V., Montgomery, J. S., Ratzan, E. M., Beirl, A. J., Rivera, R. A., Lotthammer, J. M., Walujkar, S., et al. (2023) · doi:10.1101/2023.05.26.542533 · Cited by 8
Lin, Y., Zhou, Z., Han, Y., Cheng, D., Wang, H. J., Ju, L. A., Zhang, Y., Cox, C. D., & Corry, B. (2026) · Nature Communications · doi:10.1038/s41467-026-68919-x · Cited by 7
Metadata
- Authors
- Liu, X., Wang, J., & Sun, L.
- Venue
- Nature Communications
- Published
- 2018-11-29
- Volume
- 9
- Issue
- 1
- Pages
- 5060-5060
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2901407004
- Cited by
- 178
- References
- 6
- FWCI
- 4.71
- Type
- journal article
- Language
- en
- Open access
- gold
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