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Article

Three mutations repurpose a plant karrikin receptor to a strigolactone receptor.

Proceedings of the National Academy of Sciences of the United States of America - 27 Jul 2021

Arellano-Saab Amir, Bunsick Michael, Al Galib Hasan, Zhao Wenda, Schuetz Stefan, Bradley James Michael, Xu Zhenhua, Adityani Claresta, Subha Asrinus, McKay Hayley, de Saint Germain Alexandre, Boyer François-Didier, McErlean Christopher S P, Toh Shigeo, McCourt Peter, Stogios Peter J, Lumba Shelley

Abstract excerpt

Uncovering the basis of small-molecule hormone receptors' evolution is paramount to a complete understanding of how protein structure drives function. In plants, hormone receptors for strigolactones are well suited to evolutionary inquiries because closely related homologs have different ligand preferences. More importantly, because of facile plant transgenic systems, receptors can be swapped and quickly assessed...

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Identifiers

PMID: 34301902
DOI: 10.1073/pnas.2103175118
PMCID: PMC8325247

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Three mutations repurpose a plant karrikin receptor to a strigolactone receptor.PMID 34301902Read ↗

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Mechanistic basis for enhanced strigolactone sensitivity in KAI2 triple mutant.Semantic proximity Read ↗

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KAI2- and MAX2-mediated responses to karrikins and strigolactones are largely independent of HY5 in Arabidopsis seedlings.Semantic proximity Read ↗

Dominant-Negative KAI2d Paralogs Putatively Attenuate Strigolactone Responses in Root Parasitic Plants.Semantic proximity Read ↗

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