BSKs are partially redundant positive regulators of brassinosteroid signaling in Arabidopsis
Autor: | Shivakumar Sreeramulu, Liat Ben Hayun, Hadas Nahum, Guido Sessa, Yana Mostizky, Christian Gruetter, Dor Salomon, Eilon Shani, Sukumaran Sunitha, Naomi Ori, Daniel Rauh |
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Rok vydání: | 2012 |
Předmět: |
Mutant
Molecular Sequence Data Arabidopsis Plant Science Flowers Protein Serine-Threonine Kinases chemistry.chemical_compound Steroids Heterocyclic Plant Growth Regulators Gene Expression Regulation Plant Two-Hybrid System Techniques Brassinosteroids Genetics Arabidopsis thaliana Brassinosteroid Amino Acid Sequence Phosphorylation biology Kinase Arabidopsis Proteins Cell Biology biology.organism_classification Plants Genetically Modified Phenotype Cell biology Plant Leaves Mutagenesis Insertional chemistry Mutagenesis Site-Directed Signal transduction Protein Kinases Sequence Alignment Signal Transduction |
Zdroj: | The Plant journal : for cell and molecular biology. 74(6) |
ISSN: | 1365-313X |
Popis: | †SUMMARY Arabidopsis thaliana brassinosteroid signaling kinases (BSKs) constitute a receptor-like cytoplasmic kinase sub-family (RLCK-XII) with 12 members. Previous analysis demonstrated a positive role for BSK1 and BSK3 in the initial steps of brassinosteroid (BR) signal transduction. To investigate the function of BSKs in plant growth and BR signaling, we characterized T-DNA insertion lines for eight BSK genes (BSK1–BSK8) and multiple mutant combinations. Simultaneous elimination of three BSK genes caused alterations in growth and the BR response, and the most severe phenotypes were observed in the bsk3,4,7,8 quadruple and bsk3,4,6,7,8 pentuple mutants, which displayed reduced rosette size, leaf curling and enhanced leaf inclination. In addition, upon treatment with 24-epibrassinolide, these mutants showed reduced hypocotyl elongation, enhanced root growth and alteration in the expression of BR-responsive genes. Some mutant combinations also showed antagonistic interactions. In support of a redundant function in BR signaling, multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro. The BIN2 and BIL2 GSK3-like kinases, which are negative regulators of BR signaling, interacted in vivo with BSKs and phosphorylated them in vitro, probably at different sites to BRI1. This study demonstrates redundant biological functions for BSKs, and suggests the existence of a regulatory link between BSKs and GSK3-like kinases. |
Databáze: | OpenAIRE |
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