Structural basis for assembly and function of a heterodimeric plant immune receptor

Simon J. Williams*, Kee Hoon Sohn, Li Wan, Maud Bernoux, Panagiotis F. Sarris, Cecile Segonzac, Thomas Ve, Yan Ma, Simon B. Saucet, Daniel J. Ericsson, Lachlan W. Casey, Thierry Lonhienne, Donald J. Winzor, Xiaoxiao Zhang, Anne Coerdt, Jane E. Parker, Peter N. Dodds, Bostjan Kobe, Jonathan D.G. Jones

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

267 Citations (Scopus)


Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll-interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling.

Original languageEnglish
Pages (from-to)299-303
Number of pages5
Issue number6181
Publication statusPublished - 2014
Externally publishedYes


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