2017
DOI: 10.3390/ijms18061164
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Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?

Abstract: Lectins are fundamental to plant life and have important roles in cell-to-cell communication; development and defence strategies. At the cell surface; lectins are present both as soluble proteins (LecPs) and as chimeric proteins: lectins are then the extracellular domains of receptor-like kinases (LecRLKs) and receptor-like proteins (LecRLPs). In this review; we first describe the domain architectures of proteins harbouring G-type; L-type; LysM and malectin carbohydrate-binding domains. We then focus on the fu… Show more

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Cited by 120 publications
(152 citation statements)
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References 188 publications
(264 reference statements)
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“…Nevertheless, neither RGD peptides nor eATP are the expected ligands for this L-LecRLK. Instead, cell wall-derived molecules or glycoproteins have been suggested to be the bona fide ligands based on in silico modelling of LecRKI.9 ED (Bellande et al, 2017). These data suggest that LecRKI.9 and/or other L-Lec-RLKs might be implicated in the perception of as-yet-unknown cell wall-derived DAMPs.…”
Section: Lectin-like (Lec)-prrs: a Diverse Set Of Plant Receptors Shamentioning
confidence: 99%
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“…Nevertheless, neither RGD peptides nor eATP are the expected ligands for this L-LecRLK. Instead, cell wall-derived molecules or glycoproteins have been suggested to be the bona fide ligands based on in silico modelling of LecRKI.9 ED (Bellande et al, 2017). These data suggest that LecRKI.9 and/or other L-Lec-RLKs might be implicated in the perception of as-yet-unknown cell wall-derived DAMPs.…”
Section: Lectin-like (Lec)-prrs: a Diverse Set Of Plant Receptors Shamentioning
confidence: 99%
“…LysM domains are widespread in eukaryotic and prokaryotic proteins, and are typically implicated in the recognition of N-acetylglucosamine (GlcNAc)-containing glycans (Buist et al, 2008;Bellande et al, 2017). LysM-PRRs have been described in various plant species as receptors for MAMPs such as chitin and PGN, both in symbiotic and pathogenic interactions (Zipfel and Oldroyd, 2017).…”
Section: Lysm-prrs: a Few Receptors Perceiving A Diverse Set Of Carbomentioning
confidence: 99%
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“…Arabidopsis (Pegadaraju et al, 2007). However, no barley PAD4 (MLOC_1340) or 341 PAD4-related genes were up-regulated during the barley-M. persicae interaction 342 defence (Bellande et al, 2017). PP2 is a lectin highly abundant in the phloem and 348 accumulates in damaged phloem sieve pores to form protective plugs (Read & Northcote, 1983).…”
mentioning
confidence: 99%