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Macromolecular tool box to elucidate CLAVATA3/EMBRYO SURROUNDING REGION-RELATED-RLK binding, signaling, and downstream effects.
Narasimhan, Madhumitha; Jahnke, Nina; Kallert, Felix; Bahafid, Elmehdi; Böhmer, Franziska; Hartmann, Laura; Simon, Rüdiger.
Afiliación
  • Narasimhan M; Institute for Developmental Genetics, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Jahnke N; Institute of Organic Chemistry and Macromolecular Chemistry, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Kallert F; Institute of Organic Chemistry and Macromolecular Chemistry, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Bahafid E; Institute for Developmental Genetics, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Böhmer F; Institute of Organic Chemistry and Macromolecular Chemistry, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Hartmann L; Institute of Organic Chemistry and Macromolecular Chemistry, Heinrich Heine University, Universitätstraße 1, D-40225 Düsseldorf, North Rhine Westphalia, Germany.
  • Simon R; Institute of Macromolecular Chemistry, University Freiburg, Stefan-Meier-Straße 31, D-79104 Freiburg, Germany.
J Exp Bot ; 75(17): 5438-5456, 2024 Sep 11.
Article en En | MEDLINE | ID: mdl-38717932
ABSTRACT
Plant peptides communicate by binding to a large family of receptor-like kinases (RLKs), and they share a conserved binding mechanism, which may account for their promiscuous interaction with several RLKs. In order to understand the in vivo binding specificity of the CLAVATA3/EMBRYO SURROUNDING REGION-RELATED peptide family in Arabidopsis, we have developed a novel set of CLAVATA3 (CLV3)-based peptide tools. After carefully evaluating the CLE peptide binding characteristics, using solid phase synthesis process, we modified the CLV3 peptide and attached a fluorophore and a photoactivable side group. We observed that the labeled CLV3 shows binding specificity within the CLAVATA1 clade of RLKs while avoiding the distantly related PEP RECEPTOR clade, thus resolving the contradictory results obtained previously by many in vitro methods. Furthermore, we observed that the RLK-bound CLV3 undergoes clathrin-mediated endocytosis and is trafficked to the vacuole via ARA7 (a Rab GTPase)-labeled endosomes. Additionally, modifying CLV3 for light-controlled activation enabled spatial and temporal control over CLE signaling. Hence, our CLV3 macromolecular toolbox can be used to study rapid cell specific down-stream effects. Given the conserved binding properties, in the future our toolbox can also be used as a template to modify other CLE peptides.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: J Exp Bot Asunto de la revista: BOTANICA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: J Exp Bot Asunto de la revista: BOTANICA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido