Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2
| Autor: | Satoshi Fujita, Andrea Moretti, Niko Geldner, Alexandre Pfister, Michael Hothorn, Ulrich Hohmann, Benjamin Brandt, Yan Ma, Satohiro Okuda, Verónica G. Doblas |
|---|---|
| Přispěvatelé: | Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva [Switzerland]-University of Geneva [Switzerland], Department of Plant Molecular Biology, University of Lausanne (UNIL), Swiss National Science Foundation (SNSF)European Commission31003A_17623731CP30_18021331003A_156261310030E_176090European Research Council (ERC)European Commission616228-ENDOFUNHuman Frontier Science Program Organization postdoctoral fellowship LT000567/2016-LMinistry of Education, Culture, Sports, Science and Technology, Japan (MEXT)Japan Society for the Promotion of Science Howard Hughes Medical Institute |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
Tyrosylprotein sulfotransferase root development Sequence analysis Arabidopsis Plant Biology Peptide Peptide binding Ligands 01 natural sciences 03 medical and health sciences [SPI]Engineering Sciences [physics] Plant Growth Regulators Cell surface receptor receptor kinase Amino Acid Sequence Arabidopsis/chemistry Arabidopsis/enzymology Arabidopsis/genetics Arabidopsis/metabolism Arabidopsis Proteins/chemistry Arabidopsis Proteins/genetics Arabidopsis Proteins/metabolism Kinetics Peptides/chemistry Peptides/metabolism Plant Growth Regulators/chemistry Plant Growth Regulators/metabolism Protein Binding Protein Kinases/chemistry Protein Kinases/genetics Protein Kinases/metabolism coreceptor peptide hormone Gene 030304 developmental biology chemistry.chemical_classification 0303 health sciences Multidisciplinary Kinase Arabidopsis Proteins Receptor kinase food and beverages Biological Sciences Peptide hormone Root development Amino acid 3. Good health Cell biology ddc:580 Biochemistry chemistry Ectodomain Peptides Protein Kinases Coreceptor Function (biology) 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, 117 (5), pp.2693-2703. ⟨10.1073/pnas.1911553117⟩ Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 5, pp. 2693-2703 Proceedings of the National Academy of Sciences, Vol. 117, No 5 (2020) pp. 2693-2703 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1911553117⟩ |
| Popis: | Significance Plants have evolved unique membrane receptor kinases with extracellular leucine-rich repeat domains that regulate diverse developmental processes and that form the first layer of the plant immune system. Here it is shown that 2 sequence-related receptor kinases and their shape-complementary coreceptors selectively sense members of a small family of secreted peptide hormones to control formation of an important diffusion barrier in the plant root. 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. |
| Databáze: | OpenAIRE |
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