For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
20
views
154
references
 Top references
cited by
50
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      438
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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 functions of LecPs; LecRLKs and LecRLPs referring to the biological processes they are involved in and to the ligands they recognize. Together; LecPs; LecRLKs and LecRLPs constitute versatile recognition systems at the cell surface contributing to the detection of symbionts and pathogens; and/or involved in monitoring of the cell wall structure and cell growth.

          Related collections

          Most cited references154

          • Record: found
          • Abstract: found
          • Article: not found

          CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis.

          Ayako Miya, Premkumar Albert, Tomonori Shinya … (2007)
          Chitin is a major component of fungal cell walls and serves as a microbe-associated molecular pattern (MAMP) for the detection of various potential pathogens in innate immune systems of both plants and animals. We recently showed that chitin elicitor-binding protein (CEBiP), plasma membrane glycoprotein with LysM motifs, functions as a cell surface receptor for chitin elicitor in rice. The predicted structure of CEBiP does not contain any intracellular domains, suggesting that an additional component(s) is required for signaling through the plasma membrane into the cytoplasm. Here, we identified a receptor-like kinase, designated CERK1, which is essential for chitin elicitor signaling in Arabidopsis. The KO mutants for CERK1 completely lost the ability to respond to the chitin elicitor, including MAPK activation, reactive oxygen species generation, and gene expression. Disease resistance of the KO mutant against an incompatible fungus, Alternaria brassicicola, was partly impaired. Complementation with the WT CERK1 gene showed cerk1 mutations were responsible for the mutant phenotypes. 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 CERK1 plays a critical role in fungal MAMP perception in plants.
          Article 0 comments Cited 382 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases.

            S.-H. Shiu, A Bleecker (2001)
            Plant receptor-like kinases (RLKs) are proteins with a predicted signal sequence, single transmembrane region, and cytoplasmic kinase domain. Receptor-like kinases belong to a large gene family with at least 610 members that represent nearly 2.5% of Arabidopsis protein coding genes. We have categorized members of this family into subfamilies based on both the identity of the extracellular domains and the phylogenetic relationships between the kinase domains of subfamily members. Surprisingly, this structurally defined group of genes is monophyletic with respect to kinase domains when compared with the other eukaryotic kinase families. In an extended analysis, animal receptor kinases, Raf kinases, plant RLKs, and animal receptor tyrosine kinases form a well supported group sharing a common origin within the superfamily of serine/threonine/tyrosine kinases. Among animal kinase sequences, Drosophila Pelle and related cytoplasmic kinases fall within the plant RLK clade, which we now define as the RLK/Pelle family. A survey of expressed sequence tag records for land plants reveals that mosses, ferns, conifers, and flowering plants have similar percentages of expressed sequence tags representing RLK/Pelle homologs, suggesting that the size of this gene family may have been close to the present-day level before the diversification of land plant lineages. The distribution pattern of four RLK subfamilies on Arabidopsis chromosomes indicates that the expansion of this gene family is partly a consequence of duplication and reshuffling of the Arabidopsis genome and of the generation of tandem repeats.
            Article 0 comments Cited 335 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases.

              Simona Radutoiu, Lene Madsen, Esben Madsen … (2003)
              Although most higher plants establish a symbiosis with arbuscular mycorrhizal fungi, symbiotic nitrogen fixation with rhizobia is a salient feature of legumes. Despite this host range difference, mycorrhizal and rhizobial invasion shares a common plant-specified genetic programme controlling the early host interaction. One feature distinguishing legumes is their ability to perceive rhizobial-specific signal molecules. We describe here two LysM-type serine/threonine receptor kinase genes, NFR1 and NFR5, enabling the model legume Lotus japonicus to recognize its bacterial microsymbiont Mesorhizobium loti. The extracellular domains of the two transmembrane kinases resemble LysM domains of peptidoglycan- and chitin-binding proteins, suggesting that they may be involved directly in perception of the rhizobial lipochitin-oligosaccharide signal. We show that NFR1 and NFR5 are required for the earliest physiological and cellular responses to this lipochitin-oligosaccharide signal, and demonstrate their role in the mechanism establishing susceptibility of the legume root for bacterial infection.
              Article 0 comments Cited 278 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Els Van Damme: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 31 May 2017
                Publication date Collection: June 2017
                Volume: 18
                Issue: 6
                Electronic Location Identifier: 1164
                Affiliations
                [1 ]Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 Chemin de Borde Rouge, Auzeville, BP 42617, 31326 Castanet-Tolosan, France; kevin.bellande@ 123456lrsv.ups-tlse.fr (K.B.); savelli@ 123456lrsv.ups-tlse.fr (B.S.); jamet@ 123456lrsv.ups-tlse.fr (E.J.)
                [2 ]LIPM, Université de Toulouse, INRA, CNRS, 31326 Castanet-Tolosan, France; Jean-Jacques.Bono@ 123456toulouse.inra.fr
                Author notes
                [* ]Correspondence: canut@ 123456lrsv.ups-tlse.fr ; Tel.: +33-534-32-38-59
                Article
                Publisher ID: ijms-18-01164
                DOI: 10.3390/ijms18061164
                PMC ID: 5485988
                PubMed ID: 28561754
                SO-VID: 68046040-4869-4100-934c-ccc5b7df0434
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 28 April 2017
                Date accepted : 28 May 2017
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: lectin,lectin receptor-like kinase,carbohydrate,cell wall,signalling,plant development,plant pathology
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: lectin, lectin receptor-like kinase, carbohydrate, cell wall, signalling, plant development, plant pathology

                Comments

                Comment on this article

                scite_

                Similar content438

                See all similar

                Cited by48

                See all cited by

                Most referenced authors2,046

                See all reference authors