Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.

Okuda S; Fujita S; Moretti A; Hohmann U; Doblas VG; Ma Y; Pfister A; Brandt B; Geldner N; Hothorn M

doi:10.1073/pnas.1911553117

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Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.

Okuda S Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland.
Fujita S Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Moretti A Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland.
Hohmann U Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland.
Doblas VG Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Ma Y Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Pfister A Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Brandt B Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland.
Geldner N Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland Niko.Geldner@unil.ch michael.hothorn@unige.ch.
Hothorn M Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland; Niko.Geldner@unil.ch michael.hothorn@unige.ch.

2020-01-23

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Proceedings of the National Academy of Sciences of the United States of America. - 2020

English Plants use leucine-rich repeat receptor kinases (LRR-RKs) to sense sequence diverse peptide hormones at the cell surface. A 3.0-Å crystal structure of the LRR-RK GSO1/SGN3 regulating Casparian strip formation in the endodermis reveals a large spiral-shaped ectodomain. The domain provides a binding platform for 21 amino acid CIF peptide ligands, which are tyrosine sulfated by the tyrosylprotein sulfotransferase TPST/SGN2. GSO1/SGN3 harbors a binding pocket for sulfotyrosine and makes extended backbone interactions with CIF2. Quantitative biochemical comparisons reveal that GSO1/SGN3-CIF2 represents one of the strongest receptor-ligand pairs known in plants. Multiple missense mutations are required to block CIF2 binding in vitro and GSO1/SGN3 function in vivo. Using structure-guided sequence analysis we uncover previously uncharacterized CIF peptides conserved among higher plants. Quantitative binding assays with known and novel CIFs suggest that the homologous LRR-RKs GSO1/SGN3 and GSO2 have evolved unique peptide binding properties to control different developmental processes. A quantitative biochemical interaction screen, a CIF peptide antagonist and genetic analyses together implicate SERK proteins as essential coreceptor kinases required for GSO1/SGN3 and GSO2 receptor activation. Our work provides a mechanistic framework for the recognition of sequence-divergent peptide hormones in plants.

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