The FERONIA receptor kinase maintains cell-wall integrity during salt stress through Ca2+ signaling

Autor: Ming-Che Liu, Alexis Peaucelle, Heather N. Cartwright, Qiaohong Duan, José R. Dinneny, Ina Schmitz-Thom, Wei Feng, Leonie Steinhorst, Jörg Kudla, Daniel Kita, Robert Yvon, Vinh Doan, Jacob Maman, Alice Y. Cheung, Hen-Ming Wu
Přispěvatelé: Department of Plant Biology, Carnegie Institution for Science [Washington], University of Massachusetts System (UMASS), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Sainsbury Laboratory Cambridge University (SLCU), University of Cambridge [UK] (CAM), Institut für biologie und biotechnologie der pflanzen, Westfälische Wilhelms-Universität Münster (WWU), Department of Biology, Stanford University, Sainsbury Laboratory, Cambridge University, National Science Foundation (NSF) Plant Genome Research Program [IOS 1238202], NIH NIGMS [R01 GM123259-01], Carnegie Institution for Science Endowment, NSF [IOS-1146941, IOS-1147165, IOS-1645854], German Research Foundation [Ku 931/14-1], Howard Hughes Medical Institute, Simons Foundation, Dinneny, José R.
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Current Biology-CB
Current Biology-CB, Elsevier, 2018, 28 (5), pp.666-675 ; e1-e5. ⟨10.1016/j.cub.2018.01.023⟩
Current Biology 5 (28), 666-675 ; e1-e5. (2018)
Current biology : CB
ISSN: 0960-9822
1879-0445
DOI: 10.1016/j.cub.2018.01.023⟩
Popis: SUMMARY Cells maintain integrity despite changes in their mechanical properties elicited during growth and environmental stress. How cells sense their physical state and compensate for cell-wall damage is poorly understood, particularly in plants. Here we report that FERONIA (FER), a plasma-membrane-localized receptor kinase from Arabidopsis, is necessary for the recovery of root growth after exposure to high salinity, a widespread soil stress. The extracellular domain of FER displays tandem regions of homology with malectin, an animal protein known to bind diglucose in vitro and important for protein quality control in the endoplasmic reticulum. The presence of malectin-like domains in FER and related receptor kinases has led to widespread speculation that they interact with cell-wall polysaccharides and can potentially serve a wall-sensing function. Results reported here show that salinity causes softening of the cell wall and that FER is necessary to sense these defects. When this function is disrupted in the fer mutant, root cells explode dramatically during growth recovery. Similar defects are observed in the mur1 mutant, which disrupts pectin cross-linking. Furthermore, fer cell-wall integrity defects can be rescued by treatment with calcium and borate, which also facilitate pectin cross-linking. Sensing of these salinity-induced wall defects might therefore be a direct consequence of physical interaction between the extracellular domain of FER and pectin. FER-dependent signaling elicits cell-specific calcium transients that maintain cell-wall integrity during salt stress. These results reveal a novel extracellular toxicity of salinity, and identify FER as a sensor of damage to the pectin-associated wall.
In Brief For plant cells, growth requires maintenance of cell-wall integrity. Feng et al. show that salinity weakens the cell wall, which triggers FER-mediated calcium signaling to prevent root cells from bursting during growth under salt stress. The extracellular domain of FER physically interacts with pectin, indicating a potential sensing mechanism.
Databáze: OpenAIRE
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