ArticleProceedings of the National Academy of Sciences of the United States of America2016
PP2A-3 interacts with ACR4 and regulates formative cell division in the Arabidopsis root.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- Association mapping for root system architecture under varying levels of phosphorus application in Brassica juncea L. Czern & Coss.BMC genomics · 2025Article
- An update on evolutionary, structural, and functional studies of receptor-like kinases in plants.Frontiers in plant science · 2024Review
- Time-Dependent Proteomic Signatures Associated with Embryogenic Callus Induction inPlants (Basel, Switzerland) · 2023Article
- Application of an Improved 2-Dimensional High-Throughput Soybean Root Phenotyping Platform to Identify Novel Genetic Variants Regulating Root Architecture Traits.Plant phenomics (Washington, D.C.) · 2023Article
- Phosphorylation status of Bβ subunit acts as a switch to regulate the function of phosphatase PP2A in ethylene-mediated root growth inhibition.The New phytologist · 2022Article
- ZmTE1 promotes plant height by regulating intercalary meristem formation and internode cell elongation in maize.Plant biotechnology journal · 2022Article
- Interactome of Arabidopsis Thaliana.Plants (Basel, Switzerland) · 2022Article
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- The protein phosphatase 2A catalytic subunit StPP2Ac2b enhances susceptibility to Phytophthora infestans and senescence in potato.PloS one · 2022Article
- MAG2 and MAL Regulate Vesicle Trafficking and Auxin Homeostasis With Functional Redundancy.Frontiers in plant science · 2022Article
- Specific PP2A Catalytic Subunits Are a Prerequisite for Positive Growth Effects in Arabidopsis Co-Cultivated withPlants (Basel, Switzerland) · 2020Article
- Receptor-like protein kinase-mediated signaling in controlling root meristem homeostasis.aBIOTECH · 2020Review
- Salicylic Acid Targets Protein Phosphatase 2A to Attenuate Growth in Plants.Current biology : CB · 2020Article
- Redox-Mediated Endocytosis of a Receptor-Like Kinase during Distal Stem Cell Differentiation Depends on Its Tumor Necrosis Factor Receptor Domain.Plant physiology · 2019Article
- Mutual Regulation of Receptor-Like Kinase SIT1 and B'κ-PP2A Shapes the Early Response of Rice to Salt Stress.The Plant cell · 2019Article
- Genome-wide association study of inflorescence length of cultivated soybean based on the high-throughout single-nucleotide markers.Molecular genetics and genomics : MGG · 2019Article
- PROTEIN PHOSHATASE 2A B'Plant physiology · 2018Article
- Article
- Sirtinol, a Sir2 protein inhibitor, affects stem cell maintenance and root development in Arabidopsis thaliana by modulating auxin-cytokinin signaling components.Scientific reports · 2017Article
- The protein phosphatase 2A catalytic subunit StPP2Ac2b acts as a positive regulator of tuberization induction in Solanum tuberosum L.Plant molecular biology · 2017Article
Corrections and comments
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Authors and funding
25 authors at 7 institutions in 3 countries.
Funding
Abstract
In plants, the generation of new cell types and tissues depends on coordinated and oriented formative cell divisions. The plasma membrane-localized receptor kinase ARABIDOPSIS CRINKLY 4 (ACR4) is part of a mechanism controlling formative cell divisions in the Arabidopsis root. Despite its important role in plant development, very little is known about the molecular mechanism with which ACR4 is affiliated and its network of interactions. Here, we used various complementary proteomic approaches to identify ACR4-interacting protein candidates that are likely regulators of formative cell divisions and that could pave the way to unraveling the molecular basis behind ACR4-mediated signaling. We identified PROTEIN PHOSPHATASE 2A-3 (PP2A-3), a catalytic subunit of PP2A holoenzymes, as a previously unidentified regulator of formative cell divisions and as one of the first described substrates of ACR4. Our in vitro data argue for the existence of a tight posttranslational regulation in the associated biochemical network through reciprocal regulation between ACR4 and PP2A-3 at the phosphorylation level.
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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.