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Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice
Chitin is a major molecular pattern for various fungi, and its fragments, chitin oligosaccharides, are known to induce various defense responses in plant cells. A plasma membrane glycoprotein, CEBiP (chitin elicitor binding protein) and a receptor kinase, CERK1 (chitin elicitor receptor kinase) (als...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996852/ https://www.ncbi.nlm.nih.gov/pubmed/21070404 http://dx.doi.org/10.1111/j.1365-313X.2010.04324.x |
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author | Shimizu, Takeo Nakano, Takuto Takamizawa, Daisuke Desaki, Yoshitake Ishii-Minami, Naoko Nishizawa, Yoko Minami, Eiichi Okada, Kazunori Yamane, Hisakazu Kaku, Hanae Shibuya, Naoto |
author_facet | Shimizu, Takeo Nakano, Takuto Takamizawa, Daisuke Desaki, Yoshitake Ishii-Minami, Naoko Nishizawa, Yoko Minami, Eiichi Okada, Kazunori Yamane, Hisakazu Kaku, Hanae Shibuya, Naoto |
author_sort | Shimizu, Takeo |
collection | PubMed |
description | Chitin is a major molecular pattern for various fungi, and its fragments, chitin oligosaccharides, are known to induce various defense responses in plant cells. A plasma membrane glycoprotein, CEBiP (chitin elicitor binding protein) and a receptor kinase, CERK1 (chitin elicitor receptor kinase) (also known as LysM-RLK1), were identified as critical components for chitin signaling in rice and Arabidopsis, respectively. However, it is not known whether each plant species requires both of these two types of molecules for chitin signaling, nor the relationships between these molecules in membrane signaling. We report here that rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown of OsCERK1 resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice. The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1. Blue native PAGE and chemical cross-linking experiments also suggested that a major portion of CEBiP exists as homo-oligomers even in the absence of chitin oligosaccharides. |
format | Text |
id | pubmed-2996852 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-29968522010-12-29 Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice Shimizu, Takeo Nakano, Takuto Takamizawa, Daisuke Desaki, Yoshitake Ishii-Minami, Naoko Nishizawa, Yoko Minami, Eiichi Okada, Kazunori Yamane, Hisakazu Kaku, Hanae Shibuya, Naoto Plant J Original Articles Chitin is a major molecular pattern for various fungi, and its fragments, chitin oligosaccharides, are known to induce various defense responses in plant cells. A plasma membrane glycoprotein, CEBiP (chitin elicitor binding protein) and a receptor kinase, CERK1 (chitin elicitor receptor kinase) (also known as LysM-RLK1), were identified as critical components for chitin signaling in rice and Arabidopsis, respectively. However, it is not known whether each plant species requires both of these two types of molecules for chitin signaling, nor the relationships between these molecules in membrane signaling. We report here that rice cells require a LysM receptor-like kinase, OsCERK1, in addition to CEBiP, for chitin signaling. Knockdown of OsCERK1 resulted in marked suppression of the defense responses induced by chitin oligosaccharides, indicating that OsCERK1 is essential for chitin signaling in rice. The results of a yeast two-hybrid assay indicated that both CEBiP and OsCERK1 have the potential to form hetero- or homo-oligomers. Immunoprecipitation using a membrane preparation from rice cells treated with chitin oligosaccharides suggested the ligand-induced formation of a receptor complex containing both CEBiP and OsCERK1. Blue native PAGE and chemical cross-linking experiments also suggested that a major portion of CEBiP exists as homo-oligomers even in the absence of chitin oligosaccharides. Blackwell Publishing Ltd 2010-10 2010-09-06 /pmc/articles/PMC2996852/ /pubmed/21070404 http://dx.doi.org/10.1111/j.1365-313X.2010.04324.x Text en Journal compilation © 2010 Blackwell Publishing Ltd and the Society for Experimental Biology http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation. |
spellingShingle | Original Articles Shimizu, Takeo Nakano, Takuto Takamizawa, Daisuke Desaki, Yoshitake Ishii-Minami, Naoko Nishizawa, Yoko Minami, Eiichi Okada, Kazunori Yamane, Hisakazu Kaku, Hanae Shibuya, Naoto Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title | Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title_full | Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title_fullStr | Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title_full_unstemmed | Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title_short | Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice |
title_sort | two lysm receptor molecules, cebip and oscerk1, cooperatively regulate chitin elicitor signaling in rice |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996852/ https://www.ncbi.nlm.nih.gov/pubmed/21070404 http://dx.doi.org/10.1111/j.1365-313X.2010.04324.x |
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