title: Receptor kinase signaling pathways in plant-microbe interactions.
abstract: Plant receptor-like kinases (RLKs) function in diverse signaling pathways, including the responses to microbial signals in symbiosis and defense. This versatility is achieved with a common overall structure: an extracytoplasmic domain (ectodomain) and an intracellular protein kinase domain involved in downstream signal transduction. Various surfaces of the leucine-rich repeat (LRR) ectodomain superstructure are utilized for interaction with the cognate ligand in both plant and animal receptors. RLKs with lysin-motif (LysM) ectodomains confer recognitional specificity toward N-acetylglucosamine-containing signaling molecules, such as chitin, peptidoglycan (PGN), and rhizobial nodulation factor (NF), that induce immune or symbiotic responses. Signaling downstream of RLKs does not follow a single pattern; instead, the detailed analysis of brassinosteroid (BR) signaling, innate immunity, and symbiosis revealed at least three largely nonoverlapping pathways. In this review, we focus on RLKs involved in plant-microbe interactions and contrast the signaling pathways leading to symbiosis and defense.
authors.affiliation: Genetics, Faculty of Biology, University of Munich (LMU), 82152 Martinsried, Germany. meritxellantolin@lrz.uni-muenchen.de
authors.forename: Meritxell
authors.initials: M
authors.lastname: Antolín-Llovera
authors.forename: Martina K
authors.initials: MK
authors.lastname: Ried
authors.forename: Andreas
authors.initials: A
authors.lastname: Binder
authors.forename: Martin
authors.initials: M
authors.lastname: Parniske
mesh_terms: D057865:Plant Immunity; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D010944:Plants / Q000276:immunology / Q000378:metabolism* / Q000382:microbiology; D011494:Protein Kinases / Q000378:metabolism / Q000502:physiology*; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D013559:Symbiosis
chemical_list: D010940:Plant Proteins; D011494:Protein Kinases