ArticleThe Journal of biological chemistry2010
A direct docking mechanism for a plant GSK3-like kinase to phosphorylate its substrates.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 64 citations in OpenAlex.
- Structural insights into AVR-Rmg8 recognition mechanisms by the wheat blast resistance gene Rmg8.Scientific reports · 2025Article
- Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.Plant & cell physiology · 2024Article
- StSN2 interacts with the brassinosteroid signaling suppressor StBIN2 to maintain tuber dormancy.Horticulture research · 2023Article
- Mining of long non-coding RNAs with target genes in response to rust based on full-length transcriptome in Kentucky bluegrass.Frontiers in plant science · 2023Article
- BES1/BZR1 Family Transcription Factors Regulate Plant Development via Brassinosteroid-Dependent and Independent Pathways.International journal of molecular sciences · 2022Review
- Genome-wide identification and expression analysis of the GSK gene family in wheat (Triticum aestivum L.).Molecular biology reports · 2022Article
- Triticale Improvement: Mining of Genes Related to Yellow Rust Resistance in Triticale Based on Transcriptome Sequencing.Frontiers in plant science · 2022Article
- Sugar inhibits brassinosteroid signaling by enhancing BIN2 phosphorylation of BZR1.PLoS genetics · 2021Article
- Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020Review
- Updates on BES1/BZR1 Regulatory Networks Coordinating Plant Growth and Stress Responses.Frontiers in plant science · 2020Review
- PIF4-induced BR synthesis is critical to diurnal and thermomorphogenic growth.The EMBO journal · 2018Article
- Crosstalk of the Brassinosteroid Signalosome with Phytohormonal and Stress Signaling Components Maintains a Balance between the Processes of Growth and Stress Tolerance.International journal of molecular sciences · 2018Review
- Hydrogen peroxide positively regulates brassinosteroid signaling through oxidation of the BRASSINAZOLE-RESISTANT1 transcription factor.Nature communications · 2018Article
- Tomato leaf curl Yunnan virus-encoded C4 induces cell division through enhancing stability of Cyclin D 1.1 via impairing NbSKη -mediated phosphorylation in Nicotiana benthamiana.PLoS pathogens · 2018Article
- The F-box Protein KIB1 Mediates Brassinosteroid-Induced Inactivation and Degradation of GSK3-like Kinases in Arabidopsis.Molecular cell · 2017Article
- BRASSINOSTEROID INSENSITIVE2 negatively regulates cellulose synthesis inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Histone deacetylase HDA6 enhances brassinosteroid signaling by inhibiting the BIN2 kinase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- BR-dependent phosphorylation modulates PIF4 transcriptional activity and shapes diurnal hypocotyl growth.Genes & development · 2014Article
- TOPLESS mediates brassinosteroid-induced transcriptional repression through interaction with BZR1.Nature communications · 2014Article
- Mechanisms of signaling crosstalk between brassinosteroids and gibberellins.Plant signaling & behavior · 2013Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycogen synthase kinase 3 (GSK3) is a highly conserved serine/threonine protein kinase that plays important roles in a variety of physiological and developmental processes in animals. It is well known that the GSK3 kinase-catalyzed protein phosphorylation often requires a stable kinase-substrate docking interaction, which is achieved mainly by two mechanisms as follows: priming phosphorylation of a substrate by a distinct kinase to create a docking phosphate group and scaffold protein-mediated protein complex formation. Brassinosteroid-INsensitive 2 (BIN2) is an Arabidopsis GSK3-like kinase that negatively regulates brassinosteroid (BR) signaling by phosphorylating BES1 (bri1 EMS suppressor 1) and BZR1 (brassinazole-resistant 1), two highly similar transcription factors critical for bringing about characteristic BR responses. However, little is known about the biochemical mechanism by which BIN2 phosphorylates its substrates. Here, we show that BIN2 interacts directly with BZR1 through a 12-amino acid BIN2-docking motif adjacent to the C terminus of BZR1. Interestingly, this 12-amino acid motif is sufficient to allow a Drosophila GSK3 substrate Armadillo to be phosphorylated by BIN2 in vitro. Deletion of this motif inhibits the phosphorylation and subsequent degradation of BZR1 in vivo, resulting in phenotypic suppression of a hypermorphic bin2 mutation and enhanced resistance to a BR biosynthesis inhibitor. We thus concluded that BIN2 utilizes a direct kinase-substrate docking mechanism to phosphorylate BZR1 and regulate its protein stability.
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