ArticleThe New phytologist2022
Phosphorylation status of Bβ subunit acts as a switch to regulate the function of phosphatase PP2A in ethylene-mediated root growth inhibition.
Article in The New phytologist, 2022. 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.
- A current view on the involvement of protein phosphatase PP2A subunits in the responses of plants to abiotic stress at the subcellular level.Plant cell reports · 2026Review
- Histone acetyltransferase HAF2 associates with pyruvate dehydrogenase complex to control H3K14ac and H3K23ac in ethylene response.Cell reports · 2025Article
- Hyperosmolarity-induced suppression of group B1 Raf-like protein kinases modulates drought-growth trade-off inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- LHP1 and INO80 cooperate with ethylene signaling for warm ambient temperature response by activating specific bivalent genes.Cell reports · 2024Article
- Nuclear pyruvate dehydrogenase complex regulates histone acetylation and transcriptional regulation in the ethylene response.Science advances · 2024Article
- Distinct Clades of Protein Phosphatase 2A Regulatory B'/B56 Subunits Engage in Different Physiological Processes.International journal of molecular sciences · 2023Review
- "B" Regulatory Subunits of PP2A: Their Roles in Plant Development and Stress Reactions.International journal of molecular sciences · 2023Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The various combinations and regulations of different subunits of phosphatase PP2A holoenzymes underlie their functional complexity and importance. However, molecular mechanisms governing the assembly of PP2A complex in response to external or internal signals remain largely unknown, especially in Arabidopsis thaliana. We found that the phosphorylation status of Bβ of PP2A acts as a switch to regulate the activity of PP2A. In the absence of ethylene, phosphorylated Bβ leads to an inactivation of PP2A; the substrate EIR1 remains to be phosphorylated, preventing the EIR1-mediated auxin transport in epidermis, leading to normal root growth. Upon ethylene treatment, the dephosphorylated Bβ mediates the formation of the A2-C4-Bβ protein complex to activate PP2A, resulting in the dephosphorylation of EIR1 to promote auxin transport in epidermis of elongation zone, leading to root growth inhibition. Altogether, our research revealed a novel molecular mechanism by which the dephosphorylation of Bβ subunit switches on PP2A activity to dephosphorylate EIR1 to establish EIR1-mediated auxin transport in the epidermis in elongation zone for root growth inhibition in response to ethylene.
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