A plant receptor protein interacts in an unusual way with the hormone it binds. The receptor cleaves the hormone, a fragment of which then binds covalently to the receptor and triggers a major receptor shape change. See Letter p.469
Notes
References
Yao, R. et al. Nature 536, 469–473 (2016).
de Saint Germain, A. et al. Nature Chem. Biol. http://dx.doi.org/10.1038/nchembio.2147 (2016).
Al-Babili, S. & Bouwmeester, H. J. Annu. Rev. Plant Biol. 66, 161–186 (2015).
Khosla, A. & Nelson, D. C. Curr. Opin. Plant Biol. 33, 57–63 (2016).
Hamiaux, C. et al. Curr. Biol. 22, 2032–2036 (2012).
Holmquist, M. Curr. Protein Pept. Sci. 1, 209–235 (2000).
Ueguchi-Tanaka, M. et al. Nature 437, 693–698 (2005).
Zhao, L.-H. et al. Cell Res. 23, 436–439 (2013).
Nakamura, H. et al. Nature Commun. 4, 2613 (2013).
Kagiyama, M. et al. Genes Cells 18, 147–160 (2013).
Zhao, L. H. et al. Cell Res. 25, 1219–1236 (2015).
Chevalier, F. et al. Plant Cell 26, 1134–1150 (2014).
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Snowden, K., Janssen, B. Signal locked in. Nature 536, 402–404 (2016). https://doi.org/10.1038/nature19418
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DOI: https://doi.org/10.1038/nature19418
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