ArticleThe Plant cell2025
PROTEIN PHOSPHATASE 2A B'η drives spliceosome subunit dephosphorylation to mediate alternative splicing following heat stress.
Article in The Plant cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- 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
- Alternative Splicing in Plant Development and Abiotic Stress Responses: A Multifunctional Regulatory Mechanism.International journal of molecular sciences · 2026Review
- Nitrate Reductase GenesBiomolecules · 2026Article
- Postharvest warm conditioning associates with HMGR abundance, squalene accumulation, and MAPK/phosphatase transcriptional responses inFrontiers in plant science · 2026Article
- Thermal priming enhances heat tolerance in alfalfa (Medicago sativa L.) through activation of multiple metabolic pathways.BMC plant biology · 2025Article
- Transcription fidelity and control of alternative splicing contribute to heat stress survival in Arabidopsis.The Plant cell · 2025Article
- Two-layer quality control protects Arabidopsis from transcriptional errors under heat stress.The Plant cell · 2025Article
- The Role of Alternative Splicing in Polyploids in Response to Abiotic Stress.International journal of molecular sciences · 2025Review
- Splice it hot: How nuclear PP2A B'η regulates splicing fidelity by targeting the heat-stressed spliceosome.The Plant cell · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Dephosphorylation of spliceosome components is an essential regulatory step for intron removal from pre-mRNA, thereby controlling gene expression. However, the specific phosphatase responsible for this dephosphorylation step has not been identified. Here, we show that Arabidopsis thaliana (Arabidopsis) PROTEIN PHOSPHATASE 2A B'η (PP2A B'η), a B subunit of PP2A, interacts with the splicing factors PRP18a, PRP16, and RH2 and facilitates their dephosphorylation by recognizing substrates through a conserved binding motif. This dephosphorylation is crucial for proper splicing of retained introns in heat stress-responsive genes, which is mediated by the PP2A interactor PRE-MRNA PROCESSING FACTOR 18a. Genetic inactivation of PP2A B'η abolished thermotolerance during seed germination and resulted in widespread intron retention in heat stress-responsive genes. Conversely, overexpression of PP2A B'η conferred enhanced thermotolerance, accompanied by the efficient removal of retained introns under heat stress. We demonstrate that a B regulatory subunit of PP2A plays a central role in dephosphorylating spliceosome components, regulating alternative splicing, facilitating acclimation to heat stress, and targeting specific spliceosome subunits that activate pre-mRNA splicing.
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