title: Arabidopsis NDR1 is an integrin-like protein with a role in fluid loss and plasma membrane-cell wall adhesion.
abstract: Arabidopsis (Arabidopsis thaliana) NON-RACE-SPECIFIC DISEASE RESISTANCE1 (NDR1), a plasma membrane-localized protein, plays an essential role in resistance mediated by the coiled-coil-nucleotide-binding site-leucine-rich repeat class of resistance (R) proteins, which includes RESISTANCE TO PSEUDOMONAS SYRINGAE2 (RPS2), RESISTANCE TO PSEUDOMONAS SYRINGAE PV MACULICOLA1, and RPS5. Infection with Pseudomonas syringae pv tomato DC3000 expressing the bacterial effector proteins AvrRpt2, AvrB, and AvrPphB activates resistance by the aforementioned R proteins. Whereas the genetic requirement for NDR1 in plant disease resistance signaling has been detailed, our study focuses on determining a global, physiological role for NDR1. Through the use of homology modeling and structure threading, NDR1 was predicted to have a high degree of structural similarity to Arabidopsis LATE EMBRYOGENESIS ABUNDANT14, a protein implicated in abiotic stress responses. Specific protein motifs also point to a degree of homology with mammalian integrins, well-characterized proteins involved in adhesion and signaling. This structural homology led us to examine a physiological role for NDR1 in preventing fluid loss and maintaining cell integrity through plasma membrane-cell wall adhesions. Our results show a substantial alteration in induced (i.e. pathogen-inoculated) electrolyte leakage and a compromised pathogen-associated molecular pattern-triggered immune response in ndr1-1 mutant plants. As an extension of these analyses, using a combination of genetic and cell biology-based approaches, we have identified a role for NDR1 in mediating plasma membrane-cell wall adhesions. Taken together, our data point to a broad role for NDR1 both in mediating primary cellular functions in Arabidopsis through maintaining the integrity of the cell wall-plasma membrane connection and as a key signaling component of these responses during pathogen infection.
authors.affiliation: Graduate Program in Genetics, Michigan State University, East Lansing, Michigan 48824, USA.
authors.forename: Caleb
authors.initials: C
authors.lastname: Knepper
authors.forename: Elizabeth A
authors.initials: EA
authors.lastname: Savory
authors.forename: Brad
authors.initials: B
authors.lastname: Day
mesh_terms: D017360:Arabidopsis / Q000166:cytology / Q000235:genetics* / Q000276:immunology / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D002448:Cell Adhesion; D002462:Cell Membrane / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D060467:Disease Resistance; D004573:Electrolytes; D016023:Integrins; D008958:Models, Molecular; D046912:Multiprotein Complexes; D009154:Mutation; D010935:Plant Diseases / Q000276:immunology* / Q000382:microbiology; D018515:Plant Leaves; D044224:Pseudomonas syringae / Q000502:physiology; D018749:RNA, Plant / Q000235:genetics; D015398:Signal Transduction; D013312:Stress, Physiological; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D004573:Electrolytes; D016023:Integrins; D046912:Multiprotein Complexes; C109369:NDR1 protein, Arabidopsis; D018749:RNA, Plant; D014157:Transcription Factors