title: Lectin receptor kinases participate in protein-protein interactions to mediate plasma membrane-cell wall adhesions in Arabidopsis.
abstract: Interactions between plant cell walls and plasma membranes are essential for cells to function properly, but the molecules that mediate the structural continuity between wall and membrane are unknown. Some of these interactions, which are visualized upon tissue plasmolysis in Arabidopsis (Arabidopsis thaliana), are disrupted by the RGD (arginine-glycine-aspartic acid) tripeptide sequence, a characteristic cell adhesion motif in mammals. In planta induced-O (IPI-O) is an RGD-containing protein from the plant pathogen Phytophthora infestans that can disrupt cell wall-plasma membrane adhesions through its RGD motif. To identify peptide sequences that specifically bind the RGD motif of the IPI-O protein and potentially play a role in receptor recognition, we screened a heptamer peptide library displayed in a filamentous phage and selected two peptides acting as inhibitors of the plasma membrane RGD-binding activity of Arabidopsis. Moreover, the two peptides also disrupted cell wall-plasma membrane adhesions. Sequence comparison of the RGD-binding peptides with the Arabidopsis proteome revealed 12 proteins containing amino acid sequences in their extracellular domains common with the two RGD-binding peptides. Eight belong to the receptor-like kinase family, four of which have a lectin-like extracellular domain. The lectin domain of one of these, At5g60300, recognized the RGD motif both in peptides and proteins. These results imply that lectin receptor kinases are involved in protein-protein interactions with RGD-containing proteins as potential ligands, and play a structural and signaling role at the plant cell surfaces.
authors.affiliation: Surfaces Cellulaires et Signalisation chez les Végétaux, Unité Mixte de Recherche 5546 Centre National de la Recherche Scientifique-Université Paul Sabatier, 31326 Castanet Tolosan, France.
authors.forename: Anne
authors.initials: A
authors.lastname: Gouget
authors.forename: Virginie
authors.initials: V
authors.lastname: Senchou
authors.forename: Francine
authors.initials: F
authors.lastname: Govers
authors.forename: Arnaud
authors.initials: A
authors.lastname: Sanson
authors.forename: Annick
authors.initials: A
authors.lastname: Barre
authors.forename: Pierre
authors.initials: P
authors.lastname: Rougé
authors.forename: Rafael
authors.initials: R
authors.lastname: Pont-Lezica
authors.forename: Hervé
authors.initials: H
authors.lastname: Canut
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism*; D002448:Cell Adhesion; D002462:Cell Membrane / Q000201:enzymology* / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism*; D007887:Fabaceae / Q000235:genetics; D005656:Fungal Proteins / Q000378:metabolism; D037102:Lectins / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019151:Peptide Library; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; D005656:Fungal Proteins; C112546:IpiO1 protein, Phytophthora infestans; D037102:Lectins; D008024:Ligands; D019151:Peptide Library; C099543:ATHLECRK protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases