Scientific article
Open access

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

Published inProceedings of the National Academy of Sciences, vol. 117, no. 5, p. 2693-2703
Publication date2020

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.

  • Arabidopsis
  • Receptor kinase
  • Peptide hormone
  • Root development
  • Coreceptor
Research group
Citation (ISO format)
OKUDA, Satohiro et al. Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2. In: Proceedings of the National Academy of Sciences, 2020, vol. 117, n° 5, p. 2693–2703. doi: 10.1073/pnas.1911553117
Main files (1)
Article (Published version)
ISSN of the journal0027-8424

Technical informations

Creation02/06/2020 12:05:00 PM
First validation02/06/2020 12:05:00 PM
Update time03/15/2023 9:07:21 PM
Status update03/15/2023 9:07:21 PM
Last indexation10/19/2023 12:07:36 PM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack