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

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 (L...

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Autores principales: Bellande, Kevin, Bono, Jean-Jacques, Savelli, Bruno, Jamet, Elisabeth, Canut, Hervé
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485988/
https://www.ncbi.nlm.nih.gov/pubmed/28561754
http://dx.doi.org/10.3390/ijms18061164
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author Bellande, Kevin
Bono, Jean-Jacques
Savelli, Bruno
Jamet, Elisabeth
Canut, Hervé
author_facet Bellande, Kevin
Bono, Jean-Jacques
Savelli, Bruno
Jamet, Elisabeth
Canut, Hervé
author_sort Bellande, Kevin
collection PubMed
description 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.
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spelling pubmed-54859882017-06-29 Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside? Bellande, Kevin Bono, Jean-Jacques Savelli, Bruno Jamet, Elisabeth Canut, Hervé Int J Mol Sci Review 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. MDPI 2017-05-31 /pmc/articles/PMC5485988/ /pubmed/28561754 http://dx.doi.org/10.3390/ijms18061164 Text en © 2017 by the authors. 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/).
spellingShingle Review
Bellande, Kevin
Bono, Jean-Jacques
Savelli, Bruno
Jamet, Elisabeth
Canut, Hervé
Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title_full Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title_fullStr Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title_full_unstemmed Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title_short Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
title_sort plant lectins and lectin receptor-like kinases: how do they sense the outside?
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485988/
https://www.ncbi.nlm.nih.gov/pubmed/28561754
http://dx.doi.org/10.3390/ijms18061164
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