title: The Nicotiana attenuata LECTIN RECEPTOR KINASE 1 is involved in the perception of insect feeding.
abstract: The Nicotiana attenuata LECTIN RECEPTOR KINASE 1 (LecRK1) has been recently identified as a component of the mechanism used by plants to suppress the Manduca sexta-triggered accumulation of salicylic acid (SA). The suppression of the SA burst by LecRK1 allows for the unfettered induction of jasmonic acid (JA)-mediated defense responses against M. sexta herbivory. LecRK1 contains a multi-domain extracellular region composed of a G-type Lectin domain and a PAN-AP domain separated by a variable sequence with low similarity to an EGF domain. The LecRK1 intracellular region is composed of a single domain structure with predicted Ser/Thr protein kinase activity. The multi-domain structure of the extracellular region of LecRK1 adds a level of complexity in terms of the potential ligands that this receptor protein could recognize.
authors: Max Planck Institute of Chemical Ecology, Department of Molecular Ecology, Jena, Germany. gbonaventure@ice.mpg.de
authors: Gustavo
authors: G
authors: Bonaventure
mesh_terms: D000818:Animals; D003517:Cyclopentanes / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D060434:Herbivory; D008024:Ligands; D018402:Manduca / Q000502:physiology*; D054883:Oxylipins / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D014026:Nicotiana / Q000201:enzymology* / Q000235:genetics
chemical_list: D003517:Cyclopentanes; D008024:Ligands; D054883:Oxylipins; D010940:Plant Proteins; C011006:jasmonic acid; D017346:Protein Serine-Threonine Kinases