<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Okuda S</dc:creator>
  <dc:creator>Fujita S</dc:creator>
  <dc:creator>Moretti A</dc:creator>
  <dc:creator>Hohmann U</dc:creator>
  <dc:creator>Doblas VG</dc:creator>
  <dc:creator>Ma Y</dc:creator>
  <dc:creator>Pfister A</dc:creator>
  <dc:creator>Brandt B</dc:creator>
  <dc:creator>Geldner N</dc:creator>
  <dc:creator>Hothorn M</dc:creator>
  <dc:date>2020</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">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.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/232805</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1911553117</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/31964818</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Proceedings of the National Academy of Sciences of the United States of America. - 2020</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Arabidopsis</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">coreceptor</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">peptide hormone</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">receptor kinase</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">root development</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Amino Acid Sequence</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Arabidopsis</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Arabidopsis Proteins</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Kinetics</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Ligands</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Peptides</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Plant Growth Regulators</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Protein Binding</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Protein Kinases</dc:subject>
  <dc:title xmlns:ns15="xml" ns15:lang="en">Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>