ArticleFrontiers in plant science2021
3D Domain Swapping Dimerization of the Receiver Domain of Cytokinin Receptor CRE1 From
Article in Frontiers in plant science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026Review
- ARR1 and AHP interactions in the multi-step phosphorelay system.Frontiers in plant science · 2025Article
- A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023Article
- Structures of permuted halves of a modern ribose-binding protein.Acta crystallographica. Section D, Structural biology · 2023Article
- QTL cluster analysis and marker development for kernel traits based on DArT markers in spring bread wheat (Frontiers in plant science · 2023Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytokinins are phytohormones regulating many biological processes that are vital to plants. CYTOKININ RESPONSE1 (CRE1), the main cytokinin receptor, has a modular architecture composed of a cytokinin-binding CHASE (Cyclases/Histidine kinases Associated Sensory Extracellular) domain, followed by a transmembrane fragment, an intracellular histidine kinase (HK) domain, and a receiver domain (REC). Perception of cytokinin signaling involves (i) a hormone molecule binding to the CHASE domain, (ii) CRE1 autophosphorylation at a conserved His residue in the HK domain, followed by a phosphorelay to (iii) a conserved Asp residue in the REC domain, (iv) a histidine-containing phosphotransfer protein (HPt), and (v) a response regulator (RR). This work focuses on the crystal structures of the REC domain of CRE1 from the model plant
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