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Science. 2017 Jan 20;355(6322):280-284. doi: 10.1126/science.aaj1562.

Root diffusion barrier control by a vasculature-derived peptide binding to the SGN3 receptor.

Author information

1
Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
2
Gregor Mendel Institute, Austrian Academy of Sciences, Vienna Biocenter, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
3
Protein Chemistry Core Facility, Research Institute of Molecular Pathology, Vienna Biocenter 1A, 1030 Vienna, Austria.
4
Gregor Mendel Institute, Austrian Academy of Sciences, Vienna Biocenter, Dr. Bohr-Gasse 3, 1030 Vienna, Austria. youssef.belkhadir@gmi.oeaw.ac.at niko.geldner@unil.ch.
5
Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland. youssef.belkhadir@gmi.oeaw.ac.at niko.geldner@unil.ch.

Abstract

The root endodermis forms its extracellular diffusion barrier by developing ringlike impregnations called Casparian strips. A factor responsible for their establishment is the SCHENGEN3/GASSHO1 (SGN3/GSO1) receptor-like kinase. Its loss of function causes discontinuous Casparian strips. SGN3 also mediates endodermal overlignification of other Casparian strip mutants. Yet, without ligand, SGN3 function remained elusive. Here we report that schengen2 (sgn2) is defective in an enzyme sulfating peptide ligands. On the basis of this observation, we identified two stele-expressed peptides (CASPARIAN STRIP INTEGRITY FACTORS, CIF1/2) that complement sgn2 at nanomolar concentrations and induce Casparian strip mislocalization as well as overlignification-all of which depend on SGN3. Direct peptide binding to recombinant SGN3 identifies these peptides as SGN3 ligands. We speculate that CIF1/2-SGN3 is part of a barrier surveillance system, evolved to guarantee effective sealing of the supracellular Casparian strip network.

PMID:
28104888
DOI:
10.1126/science.aaj1562
[Indexed for MEDLINE]

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