ArticleJournal of experimental botany2019
Protein phosphatase 2A regulates the nuclear accumulation of the Arabidopsis bZIP protein VIP1 under hypo-osmotic stress.
Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- The transcription factor AtVIP1 promotes sorghum root development by interacting with the SbARF7 promoter.Plant cell reports · 2026Article
- Functional 14-3-3 Proteins: Master Regulators in Plant Responses to Salt Stress.Plants (Basel, Switzerland) · 2025Review
- Unveiling the evolution of VIP1 subgroup bZIP transcription factors in plants and the positive effects of BdiVIP1A on heat stress response in Brachypodium distachyon.Plant cell reports · 2025Article
- Overexpression of a pearl millet WRKY transcription factor gene, PgWRKY74, in Arabidopsis retards shoot growth under dehydration and salinity-stressed conditions.Biotechnology letters · 2024Article
- Should I stay or should I go? Trafficking of plant extra-nuclear transcription factors.The Plant cell · 2024Review
- Article
- Walnut phosphatase 2A proteins interact with basic leucine zipper protein JrVIP1 to regulate osmotic stress responseForestry research · 2024Article
- Calcium signaling-mediated transcriptional reprogramming during abiotic stress response in plants.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Review
- "B" Regulatory Subunits of PP2A: Their Roles in Plant Development and Stress Reactions.International journal of molecular sciences · 2023Review
- The baseless mutant links protein phosphatase 2A with basal cell identity in the brown alga Ectocarpus.Development (Cambridge, England) · 2023Article
- Article
- SWO1 modulates cell wall integrity under salt stress by interacting with importin ɑ in Arabidopsis.Stress biology · 2021Article
- NDR/LATS-family protein kinase genes are indispensable for embryogenesis in Arabidopsis.FEBS open bio · 2021Article
- Article
- Genomic Analysis of Soybean PP2A-BFrontiers in plant science · 2021Article
- Regulation Mechanisms of Plant Basic Leucine Zippers to Various Abiotic Stresses.Frontiers in plant science · 2020Review
- Gene co-expression network analysis to identify critical modules and candidate genes of drought-resistance in wheat.PloS one · 2020Article
- VIP1, a bZIP protein, interacts with the catalytic subunit of protein phosphatase 2A in Arabidopsis thaliana.Plant signaling & behavior · 2020Article
- Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VIP1 is a bZIP transcription factor in Arabidopsis thaliana. When cells are exposed to mechanical stress, VIP1 transiently accumulates in the nucleus, where it regulates the expression of its target genes and suppresses mechanical stress-induced root waving. The nuclear-cytoplasmic shuttling of VIP1 is regulated by phosphorylation and calcium-dependent signaling, but specific regulators of these processes remain to be identified. Here, inhibitors of protein phosphatase 2A (PP2A) are shown to inhibit both the mechanical stress-induced dephosphorylation and nuclear accumulation of VIP1. The PP2A B subunit, which recruits substrates of PP2A holoenzyme, is classified into B, B', B'', and B''' families. Using bimolecular fluorescence complementation, in vitro pull-down, and yeast two-hybrid assays, we show that VIP1 interacts with at least two of the six members of the Arabidopsis PP2A B''-family subunit, which have calcium-binding EF-hand motifs. VIP1AAA, a constitutively nuclear-localized VIP1 variant with substitutions in putative phosphorylation sites of VIP1, suppressed the root waving induced by VIP1-SRDX (a repression domain-fused variant of VIP1). These results support the idea that VIP1 is dephosphorylated by PP2A and that the dephosphorylation suppresses the root waving. The phosphorylation sites of VIP1 and its homologs were narrowed down by in vitro phosphorylation, yeast two-hybrid, and protein subcellular localization assays.
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