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Crystal structures of Arabidopsis and Physcomitrella CR4 reveal the molecular architecture of CRINKLY4 receptor kinases

View ORCID ProfileSatohiro Okuda, View ORCID ProfileLudwig A. Hothorn, View ORCID ProfileMichael Hothorn
doi: https://doi.org/10.1101/2020.08.10.245050
Satohiro Okuda
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
*Department of Biological Science, School of Science, University of Tokyo, 113-0033 Tokyo, Japan
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Ludwig A. Hothorn
2Institute of Biostatistics, Leibniz University, 30167 Hannover, Germany
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Michael Hothorn
1Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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  • For correspondence: michael.hothorn@unige.ch
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Abstract

Plant-unique receptor kinases harbor conserved cytoplasmic kinase domains and sequence-diverse ectodomains. Here we report crystal structures of CRINKLY4-type ectodomains from Arabidopsis ACR4 and Physcomitrella patens PpCR4 at 1.95 Å and 2.70 Å resolution, respectively. Monomeric CRINKLY4 ectodomains harbor a N-terminal WD40 domain and a cysteine-rich domain (CRD) connected by a short linker. The WD40 domain forms a seven-bladed β-propeller with the N-terminal strand buried in its center. Each propeller blade is stabilized by a disulfide bond. The CRD forms a β-sandwich structure stabilized by six disulfide bonds and shares low structural homology with tumor necrosis factor receptor domains. Quantitative binding assays reveal that ACR4 is not a direct receptor for the peptide hormone CLE40. An ACR4 variant lacking the entire CRD can rescue the known acr4-2 mutant phenotype, as can expression of PpCR4. Together, an evolutionary conserved signaling function for CRINKLY4 receptor kinases is encoded in its WD40 domain.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • ↵# retired.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted August 10, 2020.
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Crystal structures of Arabidopsis and Physcomitrella CR4 reveal the molecular architecture of CRINKLY4 receptor kinases
Satohiro Okuda, Ludwig A. Hothorn, Michael Hothorn
bioRxiv 2020.08.10.245050; doi: https://doi.org/10.1101/2020.08.10.245050
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Crystal structures of Arabidopsis and Physcomitrella CR4 reveal the molecular architecture of CRINKLY4 receptor kinases
Satohiro Okuda, Ludwig A. Hothorn, Michael Hothorn
bioRxiv 2020.08.10.245050; doi: https://doi.org/10.1101/2020.08.10.245050

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