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

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Science  20 Jan 2017:
Vol. 355, Issue 6322, pp. 280-284
DOI: 10.1126/science.aaj1562

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Keeping roots water-tight

The Casparian strip provides a waterproofing function to plant roots, protecting them against unregulated influxes of water and minerals. The integrity of the Casparian strip depends on a receptor-like kinase. Doblas et al. and Nakayama et al. now identify the peptide ligands in the core of the root (the stele) that help regulate Casparian strip formation. The receptor is expressed on the outward-facing surface of the root endodermal cells that surround the stele. When the endodermal layer is sealed by the Casparian strip, the peptide ligands cannot reach their receptors. When the endodermal layer is breached, whether by damage or during development, the peptides reach their receptors and activate signaling that encourages lignin deposition, shoring up the strips.

Science, this issue p. 280, p. 284


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.

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