CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
- Ayako Miya, Premkumar Albert, N. Shibuya
- BiologyProceedings of the National Academy of Sciences
- 4 December 2007
CERK1 is a plasma membrane protein containing three LysM motifs in the extracellular domain and an intracellular Ser/Thr kinase domain with autophosphorylation/myelin basic protein kinase activity, suggesting that CERK 1 plays a critical role in fungal MAMP perception in plants.
Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor.
- H. Kaku, Y. Nishizawa, N. Shibuya
- BiologyProceedings of the National Academy of Sciences…
- 18 July 2006
Chitin is a major component of fungal cell walls and serves as a molecular pattern for the recognition of potential pathogens in the innate immune systems of both plants and animals. In plants,…
Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice
- Takeo Shimizu, T. Nakano, N. Shibuya
- BiologyThe Plant Journal
- 6 September 2010
It is reported here that rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling, and the results of a yeast two-hybrid assay indicated that both CE biP and OsCerK1 have the potential to form hetero- or homo-oligomers.
Effector-Mediated Suppression of Chitin-Triggered Immunity by Magnaporthe oryzae Is Necessary for Rice Blast Disease[C][W]
- Thomas A. Mentlak, A. Kombrink, N. Talbot
- BiologyThe Plant Cell
- 1 January 2012
It is proposed that Slp1 sequesters chitin oligosaccharides to prevent PAMP-triggered immunity in rice, thereby facilitating rapid spread of the fungus within host tissue.
Conserved Fungal LysM Effector Ecp6 Prevents Chitin-Triggered Immunity in Plants
- R. de Jonge, H. Peter van Esse, B. Thomma
- 20 August 2010
It is shown that the LysM domain–containing effector protein Ecp6 of the fungal plant pathogen Cladosporium fulvum mediates virulence through perturbation of chitin-triggered host immunity.
Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization
- Masahiro Hayafune, R. Berisio, N. Shibuya
- Biology, ChemistryProceedings of the National Academy of Sciences
- 6 January 2014
The molecular basis of chitin recognition by the rice receptor, CEBiP (chitin-elicitor binding protein), and following receptor dimerization is shown based on the results of biochemical studies, epitope mapping by saturation transfer difference NMR spectroscopy and molecular modeling/docking studies.
The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence.
- N. Shibuya, I. Goldstein, W. Broekaert, M. Nsimba-Lubaki, B. Peeters, W. Peumans
- Chemistry, BiologyJournal of Biological Chemistry
- 5 February 1987
Oligosaccharide signalling for defence responses in plant
- N. Shibuya, E. Minami
- 1 November 2001
Higher plants have the ability to initiate various defence reactions such as the production of phytoalexins, antimicrobial proteins, reactive oxygen species, and reinforcement of cell walls when they are infected by pathogens such as fungi, bacteria and viruses but if these reactions occur too late or are suppressed, the infection process will proceed successfully.
The Arabidopsis CERK1‐associated kinase PBL27 connects chitin perception to MAPK activation
- Kenta Yamada, K. Yamaguchi, T. Kawasaki
- BiologyEMBO Journal
- 27 September 2016
A complete phospho‐signaling transduction pathway from PRR‐mediated pathogen recognition to MAPK activation in plants is identified and genetic evidence suggests that phosphorylation of MAPKKK5 by PBL27 is essential for chitin‐induced MAPKactivation in plants.
Selective regulation of the chitin-induced defense response by the Arabidopsis receptor-like cytoplasmic kinase PBL27.
- T. Shinya, K. Yamaguchi, N. Shibuya
- BiologyThe Plant Journal
- 1 July 2014
It is shown that PBL27, an Arabidopsis ortholog of OsRLCK185, is an immediate downstream component of the chitin receptor CERK1 and contributes to the regulation of chitIn-induced immunity in Arabidoptera.