ArticleThe Plant cell2011
Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A reductase by protein phosphatase 2A.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 117 citations in OpenAlex.
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- The potential of metabolic engineering for sustainable phytosterol production.Advanced biotechnology · 2026Review
- Targeted Gene Modification ofInternational journal of molecular sciences · 2026Article
- Postharvest warm conditioning associates with HMGR abundance, squalene accumulation, and MAPK/phosphatase transcriptional responses inFrontiers in plant science · 2026Article
- PP1-associated responses linked to HMGR-related changes during postharvest squalene accumulation inFrontiers in plant science · 2026Article
- Metabolic Engineering of Terpenoid Biosynthesis in Medicinal Plants: From Genomic Insights to Biotechnological Applications.Current issues in molecular biology · 2025Review
- Functional Identification and Transcriptional Activity Analysis ofPlants (Basel, Switzerland) · 2025Article
- HMGR Modulates Strawberry Fruit Coloration and Aroma Through Regulating Terpenoid and Anthocyanin Pathways.Foods (Basel, Switzerland) · 2025Article
- An3 Biotech · 2025Article
- PHOSPHATASE 2A dephosphorylates PHYTOCHROME-INTERACTING FACTOR3 to modulate photomorphogenesis in Arabidopsis.The Plant cell · 2024Article
- Genome-Wide Identification and Characterization of thePlants (Basel, Switzerland) · 2024Article
- An insight into the roles of ubiquitin-specific proteases in plants: development and growth, morphogenesis, and stress response.Frontiers in plant science · 2024Review
- Genome-Wide Comparison and Functional Characterization ofInternational journal of molecular sciences · 2023Article
- 3-Hydroxy-3-methylglutaryl coenzyme A reductase genes from Glycine max regulate plant growth and isoprenoid biosynthesis.Scientific reports · 2023Article
- "B" Regulatory Subunits of PP2A: Their Roles in Plant Development and Stress Reactions.International journal of molecular sciences · 2023Review
- Isolation and Comprehensive in Silico Characterisation of a NewPlants (Basel, Switzerland) · 2022Article
- The Expression Profiles of the Salvia miltiorrhiza 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase 4 Gene and Its Influence on the Biosynthesis of TanshinonesMolecules (Basel, Switzerland) · 2022Article
- Methyl Jasmonate Activates theMolecules (Basel, Switzerland) · 2022Article
- Genome-wide identification and transcriptional profiling analysis ofChinese herbal medicines · 2022Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants synthesize a myriad of isoprenoid products that are required both for essential constitutive processes and for adaptive responses to the environment. The enzyme 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes a key regulatory step of the mevalonate pathway for isoprenoid biosynthesis and is modulated by many endogenous and external stimuli. In spite of that, no protein factor interacting with and regulating plant HMGR in vivo has been described so far. Here, we report the identification of two B'' regulatory subunits of protein phosphatase 2A (PP2A), designated B''α and B''β, that interact with HMGR1S and HMGR1L, the major isoforms of Arabidopsis thaliana HMGR. B''α and B''β are Ca²⁺ binding proteins of the EF-hand type. We show that HMGR transcript, protein, and activity levels are modulated by PP2A in Arabidopsis. When seedlings are transferred to salt-containing medium, B''α and PP2A mediate the decrease and subsequent increase of HMGR activity, which results from a steady rise of HMGR1-encoding transcript levels and an initial sharper reduction of HMGR protein level. In unchallenged plants, PP2A is a posttranslational negative regulator of HMGR activity with the participation of B''β. Our data indicate that PP2A exerts multilevel control on HMGR through the five-member B'' protein family during normal development and in response to a variety of stress conditions.
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