Stop and go signals at the stigma–pollen interface of the Brassicaceae

Nasrallah, June B.

doi:10.1093/plphys/kiad301

Cited by 13 publications

(6 citation statements)

References 130 publications

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“…Bra SRKs seem to preassemble into homodimers, which rearrange upon ligand binding to enhance Bra SRK dimerization, thus allowing rapid receptor activation (Giranton et al ., 2000; Naithani et al ., 2007; Shimosato et al ., 2007). In some species, S‐locus glycoproteins (SLGs), which are secreted and highly homologous to their corresponding SRK‐ECD, enhance SI by forming a receptor complex with SRKs, but without having direct ligand‐binding affinity (Takasaki et al ., 2000; Takayama et al ., 2001; Shimosato et al ., 2007; Nasrallah, 2023). The detailed molecular mechanism of how SLGs are involved in SI remains unclear.…”

Section: Discussionmentioning

confidence: 99%

“…The partial complementation of Alyr LORE in the lore‐ 1 phenotype by Alyr LORE (Fig. 3) in A. thaliana hints at additional components contributing to LORE receptor complex formation, which might be absent or diversified in A. lyrata , like SLG, which is absent from the S‐locus of A. lyrata (Nasrallah, 2023). These components might be recruited upon ligand binding to stabilize LORE homomers and partially rescue Alyr LORE homomerization in A. thaliana .…”

Section: Discussionmentioning

confidence: 99%

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LORE receptor homomerization is required for 3‐hydroxydecanoic acid‐induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

Eschrig,

Schäffer,

Shu

et al. 2024

New Phytologist

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Summary The S‐domain‐type receptor‐like kinase (SD‐RLK) LIPOOLIGOSACCHARIDE‐SPECIFIC REDUCED ELICITATION (LORE) from Arabidopsis thaliana is a pattern recognition receptor that senses medium‐chain 3‐hydroxy fatty acids, such as 3‐hydroxydecanoic acid (3‐OH‐C10:0), to activate pattern‐triggered immunity. Here, we show that LORE homomerization is required to activate 3‐OH‐C10:0‐induced immune signaling. Fluorescence lifetime imaging in Nicotiana benthamiana demonstrates that AtLORE homomerizes via the extracellular and transmembrane domains. Co‐expression of AtLORE truncations lacking the intracellular domain exerts a dominant negative effect on AtLORE signaling in both N. benthamiana and A. thaliana, highlighting that homomerization is essential for signaling. Screening for 3‐OH‐C10:0‐induced reactive oxygen species production revealed natural variation within the Arabidopsis genus. Arabidopsis lyrata and Arabidopsis halleri do not respond to 3‐OH‐C10:0, although both possess a putative LORE ortholog. Both LORE orthologs have defective extracellular domains that bind 3‐OH‐C10:0 to a similar level as AtLORE, but lack the ability to homomerize. Thus, ligand binding is independent of LORE homomerization. Analysis of AtLORE and AlyrLORE chimera suggests that the loss of AlyrLORE homomerization is caused by several amino acid polymorphisms across the extracellular domain. Our findings shed light on the activation mechanism of LORE and the loss of 3‐OH‐C10:0 perception within the Arabidopsis genus.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

LORE receptor homomerization is required for 3‐hydroxydecanoic acid‐induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

Eschrig,

Schäffer,

Shu

et al. 2024

New Phytologist

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“…BraSRKs seem to pre-assemble into homo-dimers, which rearrange upon ligand binding to enhance BraSRK dimerization, thus allowing rapid receptor activation (Giranton et al, 2000;Naithani et al, 2007;Shimosato et al, 2007). In some species, S-locus glycoproteins (SLGs), which are secreted and highly homologous to their corresponding SRK-ECD, enhance SI by forming a receptor complex with SRKs, but without having direct ligand binding affinity (Takasaki et al, 2000;Takayama et al, 2001;Shimosato et al, 2007;Nasrallah, 2023). The detailed molecular mechanism of how SLGs are involved in SI remains unclear.…”

Section: Discussionmentioning

confidence: 99%

“…The molecular mechanism of receptor activation upon ligand binding remains to be elucidated. The partial complementation of AlyrLORE in the lore-1 phenotype by AlyrLORE (Fig 3) in A. thaliana hints at additional components contributing to LORE receptor complex formation, which might be absent or diversified in A. lyrata, like SLG which is absent in the S-locus of A. lyrata(Nasrallah, 2023). These components might be recruited upon ligand binding to stabilize LORE homomers and partially rescue AlyrLORE homomerization in A. thaliana.…”

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confidence: 96%

LORE receptor homomerization is required for 3-hydroxydecanoic acid-induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

Eschrig

Schaeffer

Illig

et al. 2021

Preprint

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Perception and processing of various internal and external signals is essential for all living organisms. Plants have an expanded and diversified repertoire of cell surface-localized receptor-like kinases (RLKs) that transduce signals across the plasma membrane. RLKs often assemble into higher-order receptor complexes with co-receptors, regulators and scaffolds to convert extracellular stimuli into cellular responses. To date, the only S-domain-RLK from Arabidopsis thaliana with a known ligand and function is AtLORE, a pattern recognition receptor that senses bacterial 3-hydroxy fatty acids of medium chain length, such as 3-hydroxy decanoic acid (3-OH-C10:0), to activate pattern-triggered immunity. Here we show that AtLORE forms receptor homomers, which is essential for 3-OH-C10:0-induced immune signaling. AtLORE homomerization is mediated by the transmembrane and extracellular domain. We show natural variation in the perception of 3-OH-C10:0 within the Brassicaceae family. Arabidopsis lyrata and Arabidopsis halleri do not respond to 3-OH-C10:0, although they possess a putative LORE orthologue. We found that LORE orthologues of these 3-OH-C10:0 nonresponsive species have defective extracellular domains that can bind the 3-OH-C10:0 ligand but lack the ability to homomerize. Our findings shed light on the activation mechanisms of AtLORE and explain natural variation of 3-OH-C10:0 perception within the Brassicaceae family.

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“…SRK, which is located on the plasma membrane of the papilla cells, specifically binds to its cognate SP11 that is released from the pollen surface. This triggers the self-phosphorylation of the kinase domain inside the cell, which results in the rejection of fertilization [22][23][24][25][26] . The alleles of SLG, SRK, and SP11 are tightly linked at the S-locus and are transmitted to the progeny as a single set called S haplotype 18,27 .…”

Section: Introductionmentioning

confidence: 99%

Comprehensive computational analysis of the molecular mechanism of self-incompatibility in Brassicaceae using improved structure prediction

Sawa

Moriwaki

Jiang

et al. 2023

Preprint

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Plants employ self-incompatibility (SI) to promote cross-fertilization. In Brassicaceae, this process is regulated by the complex formation of the pistil determinantSreceptor kinase (SRK) and the pollen determinantS-locus protein 11 (SP11, also known asS-locus cysteine-rich protein, SCR). In our previous study, we demonstrated that only the SRK ectodomain (eSRK) and SP11 pairs derived from the sameShaplotype exhibit high binding free energy based on the crystal structures of two eSRK–SP11 complexes inBrassica rapaS8andS9haplotypes and nine computationally predicted complex models. However, predicting the eSRK–SP11 complex structures for the other 100+ S haplotypes and genera remains difficult because of the SP11 polymorphism in sequence and structure. Although protein structure prediction using AlphaFold2 exhibits considerably high accuracy for most protein monomers and complexes, 46% of predicted SP11 structures we tested showed per-residue mean pLDDT < 75. Here, we demonstrate that the use of curated multiple sequence alignment (MSA) for cysteine-rich proteins significantly improves the model accuracy for SP11 and eSRK–SP11 complexes. Additionally, we calculated the binding free energies of the predicted eSRK–SP11 complexes using molecular dynamics (MD) simulations and observed that some Arabidopsis haplotypes formed a binding mode that was critically different from that ofB. rapaS8andS9. Thus, these computational results provide insights into the haplotype-specific eSRK–SP11 binding modes in Brassicaceae and could be adopted as a general method for obtaining more accurate models for other cysteine-rich proteins.

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Stop and go signals at the stigma–pollen interface of the Brassicaceae

Cited by 13 publications

References 130 publications

LORE receptor homomerization is required for 3‐hydroxydecanoic acid‐induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

LORE receptor homomerization is required for 3‐hydroxydecanoic acid‐induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

LORE receptor homomerization is required for 3-hydroxydecanoic acid-induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

Comprehensive computational analysis of the molecular mechanism of self-incompatibility in Brassicaceae using improved structure prediction

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