Zoekopdracht:
faculteit: "FNWI" en publicatiejaar: "2011"
| Auteurs | T. Maekawa, W. Cheng, L.N. Spiridon, A. Töller, E. Lukasik, Y. Saijo, P. Liu, Q.H. Shen, M.A. Micluta, I.E. Somssich, F.L.W. Takken, A.J. Petrescu, J. Chai, P. Schulze-Lefert | | Titel | Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death |
| Tijdschrift | CELL Host & Microbe |
| Jaargang | 9 |
| Jaar | 2011 |
| Nummer | 3 |
| Pagina's | 187-199 |
| ISSN | 19313128 |
| Faculteit | Faculteit der Natuurwetenschappen, Wiskunde en Informatica |
| Instituut/afd. | FNWI: Swammerdam Institute for Life Sciences (SILS) |
| Samenvatting | Plants and animals have evolved structurally related innate immune sensors, designated NLRs, to detect intracellular nonself molecules. NLRs are modular, consisting of N-terminal coiled-coil (CC) or TOLL/interleukin-1 receptor (TIR) domains, a central nucleotide-binding (NB) domain, and C-terminal leucine-rich repeats (LRRs). The polymorphic barley mildew A (MLA) locus encodes CC-containing allelic immune receptors recognizing effectors of the pathogenic powdery mildew fungus. We report the crystal structure of an MLA receptor's invariant CC domain, which reveals a rod-shaped homodimer. MLA receptors also self-associate in vivo, but self-association appears to be independent of effector-triggered receptor activation. MLA CC mutants that fail to self-interact impair in planta cell death activity triggered by the CC domain alone and by an autoactive full-length MLA receptor that mimics its ATP-bound state. Thus, CC domain-dependent dimerization of the immune sensor defines a minimal functional unit and implies a role for the dimeric CC module in downstream immune signaling. |
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