LYK4 is a component of a tripartite chitin receptor complex in Arabidopsis thaliana

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 70(2019), 19 vom: 15. Okt., Seite 5507-5516
1. Verfasser: Xue, De-Xing (VerfasserIn)
Weitere Verfasser: Li, Chun-Lian, Xie, Zhi-Ping, Staehelin, Christian
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana chitin signaling plant defense protein-protein interactions receptor complex receptor-like kinase Arabidopsis Proteins Chitin mehr... 1398-61-4 AT2G23770 protein, Arabidopsis EC 2.7.11.1 Protein Serine-Threonine Kinases
Beschreibung
Zusammenfassung:© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
LysM receptor-like kinases (LYKs) of Arabidopsis thaliana (namely LYK1, LYK4 and LYK5) play a major role in chitin perception and immunity against pathogenic fungi. Chitin-induced heterodimerization of LYK1 and LYK5 has been previously reported, but protein interaction partners of LYK4 have not yet been identified. In this study, by analysing mutants we confirmed a role of LYK4 in chitin perception, and found that the ectodomain of LYK4 homodimerizes and also interacts with the ectodomain of LYK5 in vitro. Pull-down experiments with proteins expressed in protoplasts indicated LYK4-LYK4 and LY4-LYK5 interactions in planta. When protoplasts were treated with chitoheptaose or chitin, a protein complex was immunoprecipitated that appeared to be composed of LYK1, LYK4, and LYK5. Similar experiments with proteins expressed in lyk mutant plants suggested that elicitor treatment induced a physical interaction between LYK1 and LYK5 but not between LYK1 and LYK4. Bimolecular fluorescence complementation experiments substantiated these findings. Overall, our data suggest that LYK4 functions as a LYK5-associated co-receptor or scaffold protein that enhances chitin-induced signaling in Arabidopsis
Beschreibung:Date Completed 10.08.2020
Date Revised 04.12.2021
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erz313