Thanks!! Glad you find it useful!

Thank you!!

Many thanks to my co-authors
@yasukadota.bsky.social & @shirasulab.bsky.social , the editors, and the reviewers for their helpful suggestions that improved the manuscript.

We hope this review will be a useful resource for those interested in cell-surface receptors.

RLKs and RLCKs have undergone repeated diversification throughout plant evolution, contributing to their roles across a wide range of biological processes.

We propose several mechanisms through which new receptors and signaling pathways may evolve.

Receptor-like kinases represent one of the largest gene families in plants.

Together with receptor-like cytoplasmic kinases (RLCKs), they form a monophyletic clade, indicating a shared evolutionary origin of their kinase domains.

Upon ligand perception, cell-surface receptors associate with co-receptors and cytoplasmic kinases to activate distinct responses.

We summarize key receptor signaling pathways involved in immunity, symbiosis, development, phytohormone responses, reproduction, and abiotic stress.

The same classes of ligands can be perceived by distinct ectodomains.

We discuss and summarize representative solved receptor-ligand/receptor structures to provide mechanistic insights into how diverse ectodomains sense different molecules.

Diverse receptor ectodomains enable recognition of peptides, proteins, glycans, lipids, phytohormones, small molecules, and cell wall status.

We categorize cell-surface receptors based on the classes of ligands they perceive across different biological processes.

Plant cell surface receptors Plant cell surface receptors have evolved to perceive peptides, proteins, glycans, lipids, and small molecules through diverse ectodomains, integrating these inputs into distinct physiological output....

Cell-surface receptors play key roles across many biological processes.
In plants, these receptor families have undergone remarkable expansion. Here, we systematically review these receptors in
@theplantjournal.bsky.social

Happy to see this out!
onlinelibrary.wiley.com/doi/10.1111/...

Many thanks to the editors for the invitation. Free access tᴏ the article: authors.elsevier.com/a/1mIlz3PtAV...

Lastly, the cytosol𝗶c domain dictates signaling output. By swapping or engineering intracellular domains, receptor outputs can be modified or fine-tuned to activate different biological processes.

The juxta-membrane region is primarily responsible for receptor–receptor/co-receptor association. By modifying these regions, we can tune co-receptor preferences and, in turn, modify signaling oᴜtpᴜts.

The receptor ectodomain is primarily involved in ligand perception. By swapping ectodomains or modifying them in different ways, we can զuickly reprogram receptors to perceive new ligands.

Plant cell-surface receptors regulate diverse biological processes. They perceive a wide range of ligands via distinct ectodomainꜱ, then assemble into different receptor/co-receptor complexes to activate downstream responses.

A guide to designing cell-surface receptors in plants Cell-surface receptors perceive environmental cues and trigger appropriate responses. In plants, these receptors comprise ectodomain, juxta-membrane, …

We wrote a review on the mᴏdular properties of plant cell-surface receptors, and how this knowledge can be used to reprogram and engineer them:
www.sciencedirect.com/science/arti...

Thank you Mary!!

Thanks Nacho!

Thank youuuu Pingtao

Thank you Tatsuya!!

Thanks Adam!

I am very grateful to Michele & Marc, Takehiro & Dohmae-san, Markus, @yasukadota.bsky.social & @shirasulab.bsky.social for their support. Also big thanks to the reviewers and editors for improving our manuscript!

With this approach, we aim to characterize more PRRs against different pathogens & pests in the future.

To summarize, we reported the strategies to discover and engineer plant immune receptors.
As usual, we have uploaded the data, including RCM analysis, receptor & peptide sequences, raw data…etc etc on Zenodo
(zenodo.org/records/1546... )

Together with structural prediction, phylogenomics data, and lots of in-planta validations, we engineered synthetic SCORE that perceive CSPs from a range of plant pathogens and pests.

With the polymorphic CSP recognition specificity, we wonder if SCOREs can be engineered.
We predicted receptor-peptide structures to narrow down the region of interest.

They do!
Across the 22 SOCRE orthologs we tested, most exhibit unique recognition specificity towards different CSP peptides.

Bioinformatic analyses indicate that CSPs are very diverse across organisms (not just found in bacteria).
We wonder if SCORE orthologs across the flowering plant lineage can perceive different CSP peptides.

Unlike the previously identified PRR CORE, "181" exhibits a more selective recognition towards csp15 variants, so we named it “Selective CORE” (SCORE).
In addition, CORE and SCORE are not closely related; these receptors convergently evolved to perceive CSPs.

We screened for chimeric receptors activated by the plant pathogen Agrobacterium, and identified the receptor “181” from Pomelo.
Following biochemical analyses, we discovered that 181 perceives cold shock protein (CSP) peptides.

To characterize immune receptors (PRRs) in plants, we cluster PRRs into subgroups based on conservation of their inner LRR residues.
We obtained >1000s subgroups with this approach, and cloned ~210s into receptor chimeras for further characterization.