title: Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways.
abstract: Accumulating evidence indicates that plant disease-resistance (R) proteins assemble in hetero-multimeric protein complexes in the absence of pathogens. Such complexes might enable the indirect recognition of pathogen effector molecules during attempted pathogen invasion. RAR1 and SGT1 are required for the function of most known R proteins. They interact with each other and with diverse protein complexes, which might explain their multi-functionality. The promiscuous behavior of RAR1 and SGT1 might be crucial for the formation and activation of R protein-containing recognition complexes as well as for regulating downstream signaling processes.
authors.affiliation: The Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich, UK NR4 7UH. ken.shirasu@sainsbury-laboratory.ac.uk
authors.forename: Ken
authors.initials: K
authors.lastname: Shirasu
authors.forename: Paul
authors.initials: P
authors.lastname: Schulze-Lefert
mesh_terms: D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D010940:Plant Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D010944:Plants / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D011485:Protein Binding; D015398:Signal Transduction
chemical_list: D010940:Plant Proteins