Origins and Immunity Networking Functions of EDS1 Family Proteins

Dmitry Lapin, Deepak D. Bhandari, Jane E. Parker*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The EDS1 family of structurally unique lipase-like proteins EDS1, SAG101, and PAD4 evolved in seed plants, on top of existing phytohormone and nucleotide-binding-leucine-rich-repeat (NLR) networks, to regulate immunity pathways against host-adapted biotrophic pathogens. Exclusive heterodimers between EDS1 and SAG101 or PAD4 create essential surfaces for resistance signaling. Phylogenomic information, together with functional studies in Arabidopsis and tobacco, identify a coevolved module between the EDS1-SAG101 heterodimer and coiled-coil (CC) HET-S and LOP-B (CC binf HELO einf ) domain helper NLRs that is recruited by intracellular Toll-interleukin1-receptor (TIR) domain NLR receptors to confer host cell death and pathogen immunity. EDS1-PAD4 heterodimers have a different and broader activity in basal immunity that transcriptionally reinforces local and systemic defenses triggered by various NLRs. Here, we consider EDS1 family protein functions across seed plant lineages in the context of networking with receptor and helper NLRs and downstream resistance machineries. The different modes of action and pathway connectivities of EDS1 family members go some way to explaining their central role in biotic stress resilience.

Original languageEnglish
Pages (from-to)253-276
Number of pages24
JournalAnnual Review of Phytopathology
Volume58
DOIs
Publication statusPublished - 25 Aug 2020
Externally publishedYes

Bibliographical note

Funding Information:
We thank Shigeyuki Betsuyaku (Ryukoku University, Japan) for providing the original image in Figure 3a. We thank Murray Grant (University of Warwick, UK), Ksenia Krasileva (UC Berkeley, USA), Jijie Chai, and Paul Schulze-Lefert (MPIPZ Cologne) for helpful discussions and ideas. This work was supported by the Max Planck Society and Deutsche Forschungsgemeinschaft (DFG; German Research Foundation) under Germany’s Excellence Strategy CEPLAS (EXC-2048/1, Project 390686111), CRC 1403 project B08 reference 414786233 ( J.E.P. and D.L.), CRC 680 project B10 ( J.E.P. and D.L.), and CRC 670 project TP19 ( J.E.P. and D.D.B.).

Publisher Copyright:
© 2020 Annual Reviews Inc.. All rights reserved.

Funding

We thank Shigeyuki Betsuyaku (Ryukoku University, Japan) for providing the original image in Figure 3a. We thank Murray Grant (University of Warwick, UK), Ksenia Krasileva (UC Berkeley, USA), Jijie Chai, and Paul Schulze-Lefert (MPIPZ Cologne) for helpful discussions and ideas. This work was supported by the Max Planck Society and Deutsche Forschungsgemeinschaft (DFG; German Research Foundation) under Germany’s Excellence Strategy CEPLAS (EXC-2048/1, Project 390686111), CRC 1403 project B08 reference 414786233 ( J.E.P. and D.L.), CRC 680 project B10 ( J.E.P. and D.L.), and CRC 670 project TP19 ( J.E.P. and D.D.B.).

Keywords

  • salicylic acid
  • cell death
  • TIR domain
  • PAD4
  • SAG101
  • NLR

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