The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1
Abstract
Chitin is a fungal microbe-associated molecular pattern (MAMP) that is recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor in plants and mediates chitin-induced signaling through homodimerization and phosphorylation. However, the reported chitin binding affinity of AtCERK1 is quite low, suggesting another receptor with high chitin binding affinity might be present. Here, we propose that AtLYK5 is the primary chitin receptor in Arabidopsis. Mutations in AtLYK5 resulted in a significant reduction in the plant chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, only AtLYK4/AtLYK5-2 double mutants show a complete loss of chitin response. AtLYK5 interacts with AtCERK1 in a chitin-dependent manner. Chitin binding to AtLYK5 is indispensable for chitin-induced AtCERK1 phosphorylation. AtLYK5 binds chitin at a much higher affinity than AtCERK1. Furthermore, the data suggest that AtLYK5 is the primary plant receptor for chitin, forming a chitin inducible complex with AtCERK1 to induce plant innate immunity.
- Authors:
-
[1];
- Division of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States, Department of Biochemistry, University of Missouri, Columbia, United States
- Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, United States
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
- OSTI Identifier:
- 1181086
- Alternate Identifier(s):
- OSTI ID: 1227909; OSTI ID: 1240691
- Grant/Contract Number:
- FG02-08ER15309; FG02-02ER15309; AC02-06CH11357
- Resource Type:
- Published Article
- Journal Name:
- eLife
- Additional Journal Information:
- Journal Name: eLife Journal Volume: 3; Journal ID: ISSN 2050-084X
- Publisher:
- eLife Sciences Publications, Ltd.
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES
Citation Formats
Cao, Yangrong, Liang, Yan, Tanaka, Kiwamu, Nguyen, Cuong T., Jedrzejczak, Robert P., Joachimiak, Andrzej, and Stacey, Gary. The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1. United States: N. p., 2014.
Web. doi:10.7554/eLife.03766.
Cao, Yangrong, Liang, Yan, Tanaka, Kiwamu, Nguyen, Cuong T., Jedrzejczak, Robert P., Joachimiak, Andrzej, & Stacey, Gary. The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1. United States. https://doi.org/10.7554/eLife.03766
Cao, Yangrong, Liang, Yan, Tanaka, Kiwamu, Nguyen, Cuong T., Jedrzejczak, Robert P., Joachimiak, Andrzej, and Stacey, Gary. Thu .
"The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1". United States. https://doi.org/10.7554/eLife.03766.
@article{osti_1181086,
title = {The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1},
author = {Cao, Yangrong and Liang, Yan and Tanaka, Kiwamu and Nguyen, Cuong T. and Jedrzejczak, Robert P. and Joachimiak, Andrzej and Stacey, Gary},
abstractNote = {Chitin is a fungal microbe-associated molecular pattern (MAMP) that is recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor in plants and mediates chitin-induced signaling through homodimerization and phosphorylation. However, the reported chitin binding affinity of AtCERK1 is quite low, suggesting another receptor with high chitin binding affinity might be present. Here, we propose that AtLYK5 is the primary chitin receptor in Arabidopsis. Mutations in AtLYK5 resulted in a significant reduction in the plant chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, only AtLYK4/AtLYK5-2 double mutants show a complete loss of chitin response. AtLYK5 interacts with AtCERK1 in a chitin-dependent manner. Chitin binding to AtLYK5 is indispensable for chitin-induced AtCERK1 phosphorylation. AtLYK5 binds chitin at a much higher affinity than AtCERK1. Furthermore, the data suggest that AtLYK5 is the primary plant receptor for chitin, forming a chitin inducible complex with AtCERK1 to induce plant innate immunity.},
doi = {10.7554/eLife.03766},
journal = {eLife},
number = ,
volume = 3,
place = {United States},
year = {Thu Oct 23 00:00:00 EDT 2014},
month = {Thu Oct 23 00:00:00 EDT 2014}
}
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