ArticlePlant signaling & behavior2013
OsLYP4 and OsLYP6 play critical roles in rice defense signal transduction.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 26 citations in OpenAlex.
- Mining of disease-resistance genes inFrontiers in genetics · 2024Article
- The grapevine LysM receptor-like kinase VvLYK5-1 recognizes chitin oligomers through its association with VvLYK1-1.Frontiers in plant science · 2023Article
- Bulked segregant transcriptome analysis in pea identifies key expression markers for resistance to Peyronellaea pinodes.Scientific reports · 2022Article
- Genome-wide analysis of LysM gene family members and their expression in response toFrontiers in plant science · 2022Article
- Lysin Motif (LysM) Proteins: Interlinking Manipulation of Plant Immunity and Fungi.International journal of molecular sciences · 2021Review
- Tomato LysM Receptor-Like Kinase SlLYK12 Is Involved in Arbuscular Mycorrhizal Symbiosis.Frontiers in plant science · 2018Article
- From Chaos to Harmony: Responses and Signaling upon Microbial Pattern Recognition.Annual review of phytopathology · 2017Review
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant innate immunity relies on successful detection of trespassing pathogens through recognizing their microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) at the cell surface. We recently reported two rice lysin motif (LysM)-containing proteins, OsLYP4 and OsLYP6, as dual functional PRRs sensing bacterial peptidoglycan (PGN) and fungal chitin. Here we further demonstrated the important roles of OsLYP4 and OsLYP6 in rice defense signaling, as silencing of either LYP impaired the defense marker gene activation induced by either bacterial pathogen Xanthomonas oryzaecola or fungal pathogen Magnaporthe oryzae. Moreover, we found that OsLYP4 and OsLYP6 could form homo- and hetero-dimers, and could interact with CEBiP, suggesting an unexpected complexity of chitin perception in rice.
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