The integrated LIM-peptidase domain of the CSA1-CHS3/DAR4 paired immune receptor detects changes in DA1 peptidase inhibitors in Arabidopsis

Gu, Benguo; Parkes, Toby; Rabanal, Fernando A.; Smith, Caroline; Lu, Fu-Hao; McKenzie, Neil; Dong, Hui; Weigel, Detlef; Jones, Jonathan D. G.; Çevik, Volkan; Bevan, Michael W.

doi:10.1016/j.chom.2023.04.009

Cited by 3 publications

(3 citation statements)

References 51 publications

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“…Fourth, the E3 ligases BB ( 30 ) and DA2, which ubiquitinate DA1, are characterized by a high turnover. Fifth, DAR3 inhibits the activity of DA1 to repress endoreduplication ( 89 ). Last, by directly deubiquitinating DA2 and hereby limiting its ubiquitination activity toward DA1, UBP12 and UBP13 further limit the ubiquitination of DA1 and its related proteins ( Fig.…”

Section: Discussionmentioning

confidence: 99%

A dynamic ubiquitination balance of cell proliferation and endoreduplication regulators determines plant organ size

Chen,

Vermeersch,

Van Leene

et al. 2024

Sci. Adv.

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Ubiquitination plays a crucial role throughout plant growth and development. The E3 ligase DA2 has been reported to activate the peptidase DA1 by ubiquitination, hereby limiting cell proliferation. However, the molecular mechanisms that regulate DA2 remain elusive. Here, we demonstrate that DA2 has a very high turnover and auto-ubiquitinates with K48-linkage polyubiquitin chains, which is counteracted by two deubiquitinating enzymes, UBIQUITIN-SPECIFIC PROTEASE 12 (UBP12) and UBP13. Unexpectedly, we found that auto-ubiquitination of DA2 does not influence its stability but determines its E3 ligase activity. We also demonstrate that impairing the protease activity of DA1 abolishes the growth-reducing effect of DA2. Last, we show that synthetic, constitutively activated DA1-ubiquitin fusion proteins overrule this complex balance of ubiquitination and deubiquitination and strongly restrict growth and promote endoreduplication. Our findings highlight a nonproteolytic function of K48-linked polyubiquitination and reveal a mechanism by which DA2 auto-ubiquitination levels, in concert with UBP12 and UBP13, precisely monitor the activity of DA1 and fine-tune plant organ size.

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Section: Discussionmentioning

confidence: 99%

A dynamic ubiquitination balance of cell proliferation and endoreduplication regulators determines plant organ size

Chen,

Vermeersch,

Van Leene

et al. 2024

Sci. Adv.

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“…Such pairs make up ~10% of the NLR repertoire in Arabidopsis genomes (33). Each pair consists of a specialized "sensor" for effector perception and an "executor" for immune activation (34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44). To date, postactivation oligomerization and requirements for the oligomerization of paired NLRs are still elusive.…”

mentioning

confidence: 99%

“…CHS3 is the proposed sensor NLR, and CSA1 is the proposed executor NLR in this pair ( 33 , 43 ). The clade 1 sensor CHS3 proteins contain a putative effector-binding integrated decoy domain (ID) ( 44 ), which is lacking in clades 2 and 3 ( 33 , 43 ) (fig. S1A).…”

mentioning

confidence: 99%

Paired plant immune CHS3-CSA1 receptor alleles form distinct hetero-oligomeric complexes

Yang,

Furzer,

Fensterle

et al. 2024

Science

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Plant intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) analyzed to date oligomerize and form resistosomes upon activation to initiate immune responses. Some NLRs are encoded in tightly linked co-regulated head-to-head genes whose products function together as pairs. We uncover the oligomerization requirements for different Arabidopsis paired CHS3-CSA1 alleles. These pairs form resting-state heterodimers that oligomerize into complexes distinct from NLRs analyzed previously. Oligomerization requires both conserved and allele-specific features of the respective CHS3 and CSA1 Toll-like interleukin-1 receptor (TIR) domains. The receptor kinases BAK1 and BIRs inhibit CHS3-CSA1 pair oligomerization to maintain the CHS3-CSA1 heterodimer in an inactive state. Our study reveals that paired NLRs hetero-oligomerize and likely form a distinctive “dimer of heterodimers” and that structural heterogeneity is expected even among alleles of closely related paired NLRs.

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NLR receptors in plant immunity: making sense of the alphabet soup

Contreras,

Lüdke,

Pai

et al. 2023

EMBO Reports

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Plants coordinately use cell‐surface and intracellular immune receptors to perceive pathogens and mount an immune response. Intracellular events of pathogen recognition are largely mediated by immune receptors of the nucleotide binding and leucine rich‐repeat (NLR) classes. Upon pathogen perception, NLRs trigger a potent broad‐spectrum immune reaction, usually accompanied by a form of programmed cell death termed the hypersensitive response. Some plant NLRs act as multifunctional singleton receptors which combine pathogen detection and immune signaling. However, NLRs can also function in higher order pairs and networks of functionally specialized interconnected receptors. In this article, we cover the basic aspects of plant NLR biology with an emphasis on NLR networks. We highlight some of the recent advances in NLR structure, function, and activation and discuss emerging topics such as modulator NLRs, pathogen suppression of NLRs, and NLR bioengineering. Multi‐disciplinary approaches are required to disentangle how these NLR immune receptor pairs and networks function and evolve. Answering these questions holds the potential to deepen our understanding of the plant immune system and unlock a new era of disease resistance breeding.

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The integrated LIM-peptidase domain of the CSA1-CHS3/DAR4 paired immune receptor detects changes in DA1 peptidase inhibitors in Arabidopsis

Cited by 3 publications

References 51 publications

A dynamic ubiquitination balance of cell proliferation and endoreduplication regulators determines plant organ size

A dynamic ubiquitination balance of cell proliferation and endoreduplication regulators determines plant organ size

Paired plant immune CHS3-CSA1 receptor alleles form distinct hetero-oligomeric complexes

NLR receptors in plant immunity: making sense of the alphabet soup

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