ORCID Profile
0000-0002-0255-3886
Current Organisations
Murdoch University
,
Institut Sophia Agrobiotech
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Publisher: Elsevier BV
Date: 02-2019
Publisher: Elsevier BV
Date: 02-2020
Publisher: Elsevier BV
Date: 05-2021
Publisher: Elsevier BV
Date: 05-2014
Publisher: Elsevier BV
Date: 05-2015
DOI: 10.1016/J.CELL.2015.04.024
Abstract: Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.
Publisher: EDP Sciences
Date: 2017
DOI: 10.1051/REES/2017022
Publisher: IEEE
Date: 02-2010
Publisher: Elsevier BV
Date: 02-2016
Publisher: IOP Publishing
Date: 06-2018
Publisher: American Association for the Advancement of Science (AAAS)
Date: 18-04-2014
Abstract: Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of Arabidopsis receptors, Williams et al. (p. 299 see the Perspective by Nishimura and Dangl ) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest the molecular mechanisms may translate broadly.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Simon Saucet.