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Updated: Mar 1, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
Kevin Bellande1, Jean-Jacques Bono2, Bruno Savelli3
1Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 Chemin de Borde Rouge, Auzeville, BP 42617, 31326 Castanet-Tolosan, France. kevin.bellande@lrsv.ups-tlse.fr.
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.
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