Lectin Receptor-like Kinase Signaling during Engineered Ectomycorrhiza Colonization

• Published in: Cells (Basel, Switzerland) Vol. 12; no. 7; p. 1082
• Main Authors: Shrestha, Him, Yao, Tao, Qiao, Zhenzhen, Muchero, Wellington, Hettich, Robert L, Chen, Jin-Gui, Abraham, Paul E
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 04.04.2023; MDPI
• Subjects: Analysis; BASIC BIOLOGICAL SCIENCES; Cell cycle; Colonization; Communication; Cytoskeleton; Disease susceptibility; ectomycorrhiza colonization; Ectomycorrhizas; Endocytosis; Genetic engineering; Host plants; Intracellular signalling; lectin receptor-like kinase; Lectins; Lectins - metabolism; MAP kinase; Methods; Molecular mechanics; Mycorrhizae - metabolism; Peptides; phosphoproteomics; Phosphorylation; Plant Growth Regulators - metabolism; Plant Roots - metabolism; plant–microbe interaction; Plasmids; Populus trichocarpa; Proteasomes; Protein kinase G; Protein kinases; Proteins; Proteomics; Software; Susceptibility; Symbiosis; Symbiosis - physiology; Transgenic plants; United States; Germany; phosphoproteomics; ectomycorrhiza colonization; plant–microbe interaction; lectin receptor-like kinase; symbiosis
• ISSN: 2073-4409; 2073-4409
• DOI: 10.3390/cells12071082

Mutualistic association can improve a plant's health and productivity. G-type lectin receptor-like kinase (PtLecRLK1) is a susceptibility factor in that permits root colonization by a beneficial fungus, . Engineering PtLecRLK1 also permits root colonization in non-host plants similar to . The intracellular signaling reprogramed by PtLecRLK1 upon recognition of to allow for the development and maintenance of symbiosis is yet to be determined. In this study, phosphoproteomics was utilized to identify phosphorylation-based relevant signaling pathways associated with recognition of in transgenic switchgrass roots. Our finding shows that in transgenic plants modifies the chitin-triggered plant defense and MAPK signaling along with a significant adjustment in phytohormone signaling, ROS balance, endocytosis, cytoskeleton movement, and proteasomal degradation in order to facilitate the establishment and maintenance of colonization. Moreover, protein-protein interaction data implicate a cGMP-dependent protein kinase as a potential substrate of .