ArticleScientific reports2021
Characterization of CHARK, an unusual cytokinin receptor of rice.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- The cytokinin histidine kinase receptors regulate nodulation, shoot and root development inFrontiers in plant science · 2026Article
- How meristems shape plant architecture in cereals-Cereal Stem Cell Systems (CSCS) Consortium.The Plant cell · 2025Review
- Non-Canonical Inter-Protein Interactions of Key Proteins Belonging to Cytokinin Signaling Pathways.Plants (Basel, Switzerland) · 2025Review
- The cytokinin receptor OHK4/OsHK4 regulates inflorescence architecture in rice via an IDEAL PLANT ARCHITECTURE1/WEALTHY FARMER'S PANICLE-mediated positive feedback circuit.The Plant cell · 2023Article
- Genome-wide identification and expression profiling of two-component system (TCS) genes inFrontiers in genetics · 2023Article
- The origin and early evolution of cytokinin signaling.Frontiers in plant science · 2023Review
- The LONELY GUY gene family: from mosses to wheat, the key to the formation of active cytokinins in plants.Plant biotechnology journal · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal transduction of the plant hormone cytokinin is mediated by a His-to-Asp phosphorelay. The canonical cytokinin receptor consists of an extra cytoplasmic hormone binding domain named cyclase/histidine kinase associated sensory extracellular (CHASE) and cytoplasmic histidine kinase and receiver domains. In addition to classical cytokinin receptors, a different type receptor-named CHASE domain receptor serine/threonine kinase (CHARK)-is also present in rice. It contains the same ligand binding domain as other cytokinin receptors but has a predicted Ser/Thr-instead of a His-kinase domain. Bioinformatic analysis indicates that CHARK is a retrogene and a product of trans-splicing. Here, we analyzed whether CHARK can function as a bona fide cytokinin receptor. A biochemical assay demonstrated its ability to bind cytokinin. Transient expression of CHARK in protoplasts increased their response to cytokinin. Expression of CHARK in an Arabidopsis receptor double mutant complemented its growth defects and restored the ability to activate cytokinin response genes, clearly demonstrating that CHARK functions as a cytokinin receptor. We propose that the CHARK gene presents an evolutionary novelty in the cytokinin signaling system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.