ArticleGenes & development2004
Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis.
Article in Genes & development, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 196 papers.
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Who cites it
196 citing papers in PubMed, 408 citations in OpenAlex.
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- Arabidopsis microtubule-BRI1-associated proteins negatively regulate hypocotyl elongation by controlling brassinosteroid-dependent cortical microtubule reorientation.Plant communications · 2026Article
- Two Phytophthora effectors mitigate plant immunity by manipulating intracellular pH through interaction with V-ATPase in potato.Molecular horticulture · 2026Article
- The Arabidopsis phosphatase PP2C12 negatively regulates LRX-RALF-FER-mediated cell wall integrity sensing.The EMBO journal · 2026Article
- Mitotic entry is controlled by the plant-specific phosphatase BSL1 and cyclin-dependent kinase B.Nature plants · 2025Article
- Specificity of brassinosteroid perception and its integration at signaling crossroads in vascular development.The Plant journal : for cell and molecular biology · 2025Review
- A BRASSINOSTEROID INSENSISTIVE 1 receptor kinase ortholog is required for sex determination in Ceratopteris richardii.The Plant cell · 2025Article
- Studies on the Japanese soil-borne wheat mosaic virus movement protein highlight its ability to bind plant RNA.Virology journal · 2025Article
- OsMAPKKK5 affects brassinosteroid signal transduction via phosphorylating OsBSK1-1 and regulates rice plant architecture and yield.Plant biotechnology journal · 2025Article
- Genome Identification, Expression Profile Analysis, and Abiotic Stress Response Mechanism of LonganInternational journal of molecular sciences · 2025Article
- Transcriptome Analysis Reveals Sugar and Hormone Signaling Pathways Mediating Flower Induction in Pitaya (International journal of molecular sciences · 2025Article
- Dressed Up to the Nines: The Interplay of Phytohormones Signaling and Redox Metabolism During Plant Response to Drought.Plants (Basel, Switzerland) · 2025Review
- BIL7 enhances plant growth by regulating the transcription factor BIL1/BZR1 during brassinosteroid signaling.The Plant journal : for cell and molecular biology · 2025Article
- Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.Plant & cell physiology · 2024Article
- Molecular cloning and characterization of a brassinosteriod biosynthesis-related gene PtoCYP90D1 from Populus tomentosa.BMC genomics · 2024Article
- Brassinosteroid biosynthesis and signaling: Conserved and diversified functions of core genes across multiple plant species.Plant communications · 2024Review
- Evolution, classification, structure, and functional diversification of steroid 5α-reductase family in eukaryotes.Heliyon · 2024Review
- Molecular Lesions in BRI1 and Its Orthologs in the Plant Kingdom.International journal of molecular sciences · 2024Review
136 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in A abidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counter acting the action of the glycogen synthase kinase-3 BIN2, and leading to inc eased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.
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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.