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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.
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  • 2020-01-23
Published in:
  • Proceedings of the National Academy of Sciences of the United States of America. - 2020
Arabidopsis
coreceptor
peptide hormone
receptor kinase
root development
Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Kinetics
Ligands
Peptides
Plant Growth Regulators
Protein Binding
Protein Kinases
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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  • English
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hybrid
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https://sonar.ch/global/documents/232805
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