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

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 me...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2017-01, Vol.355 (6322), p.280-284
Main Authors: Doblas, Verónica G., Smakowska-Luzan, Elwira, Fujita, Satoshi, Alassimone, Julien, Barberon, Marie, Madalinski, Mathias, Belkhadir, Youssef, Geldner, Niko
Format: Article
Language:English
Subjects:
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Binding
Diffusion
Diffusion barriers
Integrity
Kinases
Ligands
Lignin
Minerals
Mutants
Peptides
Peptides - metabolism
Plant protection
Plant roots
Plant Roots - genetics
Plant Roots - metabolism
Protein Binding
Protein Kinases - genetics
Protein Kinases - metabolism
Receptors
Roots
Strip
Sulfation
Sulfotransferases - genetics
Sulfotransferases - metabolism
T cell receptors
Waterproofing
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.aaj1562