Chitin-induced and CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) phosphorylation-dependent endocytosis of Arabidopsis thaliana LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5)

Chitin-induced and CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) phosphorylation-dependent endocytosis of Arabidopsis thaliana LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5)

© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 215(2017), 1 vom: 17. Juli, Seite 382-396
1. Verfasser: Erwig, Jan (VerfasserIn)
Weitere Verfasser: Ghareeb, Hassan, Kopischke, Michaela, Hacke, Ronja, Matei, Alexandra, Petutschnig, Elena, Lipka, Volker
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Arabidopsis CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5) chitin endocytosis pattern recognition receptor (PRR) phosphorylation Arabidopsis Proteins Chitin mehr... 1398-61-4 LYK5 protein, Arabidopsis EC 2.7.- Protein Kinases CERK1 protein, Arabidopsis EC 2.7.11.1 Protein Serine-Threonine Kinases
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100 1 |a Erwig, Jan  |e verfasserin  |4 aut 
245 1 0 |a Chitin-induced and CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) phosphorylation-dependent endocytosis of Arabidopsis thaliana LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5) 
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520 |a To detect potential pathogens, plants perceive the fungal polysaccharide chitin through receptor complexes containing lysin motif receptor-like kinases (LysM-RLKs). To investigate the ligand-induced spatial dynamics of chitin receptor components, we studied the subcellular behaviour of two Arabidopsis thaliana LysM-RLKs involved in chitin signalling, CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) and LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5. We performed standard and quantitative confocal laser scanning microscopy on stably transformed A. thaliana plants expressing fluorescently tagged CERK1 and LYK5 from their native promoters. Microscopy approaches were complemented by biochemical analyses in plants and in vitro. Both CERK1 and LYK5 localized to the plasma membrane and showed constitutive endomembrane trafficking. After chitin treatment, however, CERK1 remained at the plasma membrane while LYK5 relocalized into mobile intracellular vesicles. Detailed analyses revealed that chitin perception transiently induced the internalization of LYK5 into late endocytic compartments. Plants that lacked CERK1 or expressed an enzymatically inactive CERK1 variant did not exhibit chitin-induced endocytosis of LYK5. CERK1 could phosphorylate LYK5 in vitro and chitin treatment induced CERK1-dependent phosphorylation of LYK5 in planta. Our results suggest that chitin-induced phosphorylation by CERK1 triggers LYK5 internalization. Thus, our work identifies phosphorylation as a key regulatory step in endocytosis of plant RLKs and also provides evidence for receptor complex dissociation after ligand perception 
650 4 |a Journal Article 
650 4 |a Arabidopsis 
650 4 |a CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) 
650 4 |a LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5) 
650 4 |a chitin 
650 4 |a endocytosis 
650 4 |a pattern recognition receptor (PRR) 
650 4 |a phosphorylation 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Chitin  |2 NLM 
650 7 |a 1398-61-4  |2 NLM 
650 7 |a LYK5 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
650 7 |a Protein Kinases  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
650 7 |a CERK1 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a Protein Serine-Threonine Kinases  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
700 1 |a Ghareeb, Hassan  |e verfasserin  |4 aut 
700 1 |a Kopischke, Michaela  |e verfasserin  |4 aut 
700 1 |a Hacke, Ronja  |e verfasserin  |4 aut 
700 1 |a Matei, Alexandra  |e verfasserin  |4 aut 
700 1 |a Petutschnig, Elena  |e verfasserin  |4 aut 
700 1 |a Lipka, Volker  |e verfasserin  |4 aut 
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773 1 8 |g volume:215  |g year:2017  |g number:1  |g day:17  |g month:07  |g pages:382-396 
856 4 0 |u http://dx.doi.org/10.1111/nph.14592  |3 Volltext 
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