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

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 Arabidops...

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Published in:	The New phytologist Vol. 215; no. 1; pp. 382 - 396
Main Authors:	Erwig, Jan, Ghareeb, Hassan, Kopischke, Michaela, Hacke, Ronja, Matei, Alexandra, Petutschnig, Elena, Lipka, Volker
Format:	Journal Article
Language:	English
Published:	England New Phytologist Trust 01-07-2017 Wiley Subscription Services, Inc
Subjects:	Arabidopsis Arabidopsis - cytology Arabidopsis - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - physiology Arabidopsis thaliana Chitin Chitin - metabolism CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) Confocal microscopy Endocytosis Fungi Internalization Kinases Ligands LYSIN MOTIF‐CONTAINING RECEPTOR‐LIKE KINASE5 (LYK5) Microscopy Pathogens pattern recognition receptor (PRR) Perception Phosphorylation Promoters Protein Kinases - metabolism Protein-Serine-Threonine Kinases - metabolism Protein-Serine-Threonine Kinases - physiology Spatial discrimination Arabidopsis endocytosis LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5) pattern recognition receptor (PRR) phosphorylation CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) chitin
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0028-646X 1469-8137
DOI:	10.1111/nph.14592