Recent Advances in the Regulation of Brassinosteroid Signaling and Biosynthesis Pathways<sup>F</sup>

Ye, Huaxun; Li, Lei; Yin, Yanhai

doi:10.1111/j.1744-7909.2011.01046.x

Cited by 117 publications

(105 citation statements)

References 157 publications

Supporting

Mentioning

103

Contrasting

Order By: Relevance

“…Brassinosteroids (BRs) are crucial plant phytohormones that affect a wide range of developmental and physiological processes in plants, such as stem elongation and vascular differentiation (Clouse, 2011;Ye et al, 2011). BRs function through the BRI1 receptor-like kinase and a well-defined signal transduction pathway to activate two key transcription factors, BRASSI-NAZOLE-RESISTANT1 (BZR1) and BRINSENSITIVE1 (BRI1)-EMS-SUPPRESSOR1(BES1)/BZR2 (Li, 2010;Kim and Wang, 2010;Clouse, 2011;Gudesblat and Russinova, 2011).…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

et al. 2012

View full text Add to dashboard Cite

The brassinosteroid (BR) phytohormones play crucial roles in regulating plant cell growth and morphogenesis, particularly in hypocotyl cell elongation. The microtubule cytoskeleton is also known to participate in the regulation of hypocotyl elongation. However, it is unclear if BR regulation of hypocotyl elongation involves the microtubule cytoskeleton. In this study, we demonstrate that BRs mediate hypocotyl cell elongation by influencing the orientation and stability of cortical microtubules. Further analysis identified the previously undiscovered Arabidopsis thaliana MICROTUBULE DESTABILIZING PROTEIN40 (MDP40) as a positive regulator of hypocotyl cell elongation. BRASSINAZOLE-RESISTANT1, a key transcription factor in the BR signaling pathway, directly targets and upregulates MDP40. Overexpression of MDP40 partially rescued the shorter hypocotyl phenotype in BR-deficient mutant de-etiolated-2 seedlings. Reorientation of the cortical microtubules in the cells of MDP40 RNA interference transgenic lines was less sensitive to BR. These findings demonstrate that MDP40 is a key regulator in BR regulation of cortical microtubule reorientation and mediates hypocotyl growth. This study reveals a mechanism involving BR regulation of microtubules through MDP40 to mediate hypocotyl cell elongation.

show abstract

Section: Introductionmentioning

confidence: 99%

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

et al. 2012

View full text Add to dashboard Cite

show abstract

“…Modeling oligomeric receptor complexes. In the left panel, a brief scheme of the BRI1 pathway is shown (redrawn after Ye et al, 2011). In the absence of BL, the kinase activity of unbound BRI1 receptor is restricted by negative regulators such as BRI1 KINASE INHIBI-TOR1 (BKI1).…”

mentioning

confidence: 99%

“…BR signaling is one of the best-understood signal transduction cascades in Arabidopsis with respect to biochemical interactions and downstream responses (Ye et al, 2011;van Esse et al, 2013;Fig. 1).…”

mentioning

confidence: 99%

A Mathematical Model for the Coreceptors SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 and SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE3 in BRASSINOSTEROID INSENSITIVE1-Mediated Signaling

et al. 2013

View full text Add to dashboard Cite

Brassinosteroids (BRs) are key regulators in plant growth and development. The main BR-perceiving receptor in Arabidopsis (Arabidopsis thaliana) is BRASSINOSTEROID INSENSITIVE1 (BRI1). Seedling root growth and hypocotyl elongation can be accurately predicted using a model for BRI1 receptor activity. Genetic evidence shows that non-ligand-binding coreceptors of the SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) family are essential for BRI1 signal transduction. A relatively simple biochemical model based on the properties of SERK loss-of-function alleles explains complex physiological responses of the BRI1-mediated BR pathway. The model uses BRI1-BR occupancy as the central estimated parameter and includes BRI1-SERK interaction based on mass action kinetics and accurately describes wild-type root growth and hypocotyl elongation. Simulation studies suggest that the SERK coreceptors primarily act to increase the magnitude of the BRI1 signal. The model predicts that only a small number of active BRI1-SERK complexes are required to carry out BR signaling at physiological ligand concentration. Finally, when calibrated with single mutants, the model predicts that roots of the serk1serk3 double mutant are almost completely brassinolide (BL) insensitive, while the double mutant hypocotyls remain sensitive. This points to residual BRI1 signaling or to a different coreceptor requirement in shoots.

show abstract

“…BR-related mutants of the brassinosteroid biosynthesis pathway and signal transduction exhibited a short hypocotyl, opened cotyledons, and de-etiolation in the dark. Under light conditions, they exhibited severe dwarfism, aggregated and dark-green rosette leaves with epinasty, decreased elongation of the petiole, defects in the fertility of pollens, apical dominance, and senescence [9,69]. Therefore, brassinosteroids have pivotal roles in plant growth and differentiation [11,18].…”

mentioning

confidence: 99%

“…1 shows a model of the phosphorylation-mediated brassinosteroid signal transduction pathway based on published reports from the initial discovery of BRI1 to BR-dependent gene expression. CDG1 and SBI1 were added to the most recent model published by Ye et al [69] and Clouse [9]. More mechanisms need to be elucidated regarding the endocytosis of BRI1 and the action of PP2A on BRI1.…”

mentioning

confidence: 99%

Update on Phosphorylation-Mediated Brassinosteroid Signaling Pathways

Lee¹,

Kim

2012

Journal of Life Science

View full text Add to dashboard Cite

Protein phosphorylation is a universal mechanism that regulates cellular activities. The brassinosteroid (BR) signal transduction pathway is a relay of phosphorylation and dephosphorylation cascades. It starts with the BR-induced activation of the membrane receptor kinase brassinosteroid insensitive 1 (BRI1), resulting in the dephosphorylation of transcription factors such as BZR1/BES2 and BZR2/BES1 followed by BR-induced gene expression. Brassinosteroid signal transduction research has progressed rapidly by identifying the phosphorylation/dephosphorylation site(s) of the BR-regulated kinase and phosphatase substrates with a simultaneous pursuit of mutant phenotypes. Autophosphorylation, transphosphorylation, and serine/threonine and tyrosine phosphorylation of the receptor protein kinases BRI1 and BRI1-associated kinase (BAK1) have increased the understanding of the regulatory role of those kinases during physiological and developmental processes in plants. The phosphorylation event initiated by BR is also found in the regulation of receptor-mediated endocytosis and the subsequent degradation of the receptor. However, the basic molecular links of the BR signal transduction pathway are not well understood regarding this phosphorylation/dephosphorylation event. This review summarizes the current state of BR signal transduction research to uncover the phosphorylation/dephosphorylation networks and suggests directions for future research on steroid signal transduction to gain a more comprehensive understanding of the process. IntroductionBrassinosteroids are the only group of steroid hormones discovered in plants, which are different from steroid hormones in the animal system that has several different steroid hormones. Brassinosteroids regulate plant growth and development such as cell elongation, vascular development, senescence, stress responses, and photomorphogenesis [10,11,68]. BR-related mutants of the brassinosteroid biosynthesis pathway and signal transduction exhibited a short hypocotyl, opened cotyledons, and de-etiolation in the dark. Under light conditions, they exhibited severe dwarfism, aggregated and dark-green rosette leaves with epinasty, decreased elongation of the petiole, defects in the fertility of pollens, apical dominance, and senescence [9,69]. Therefore, brassinosteroids have pivotal roles in plant growth and differentiation [11,18]. In animal systems, steroid ligands bind to nuclear binding receptors that act as transcriptional regulators [65]. However, in plant systems, BRs bind to BRI1, an LRR-RLK on the plasma membrane, and this binding induces a signal, which is transduced to the nucleus through several signaling components in the cytoplasm [33,63].For the past few years, information on brassinosteroid-mediated phosphorylation has increased enormously. Not only serine/threonine phosphorylation but also tyrosine phosphorylation have been found, and the significance of autophosphorylation and transphosphorylation became known. Recently, many phosphorylation sites on protein kinases in ...

show abstract

Recent Advances in the Regulation of Brassinosteroid Signaling and Biosynthesis Pathways^F

Cited by 117 publications

References 157 publications

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

A Mathematical Model for the Coreceptors SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 and SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE3 in BRASSINOSTEROID INSENSITIVE1-Mediated Signaling

Update on Phosphorylation-Mediated Brassinosteroid Signaling Pathways

Contact Info

Product

Resources

About

Recent Advances in the Regulation of Brassinosteroid Signaling and Biosynthesis PathwaysF

Cited by 117 publications

References 157 publications

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

Arabidopsis MICROTUBULE DESTABILIZING PROTEIN40 Is Involved in Brassinosteroid Regulation of Hypocotyl Elongation

A Mathematical Model for the Coreceptors SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 and SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE3 in BRASSINOSTEROID INSENSITIVE1-Mediated Signaling

Update on Phosphorylation-Mediated Brassinosteroid Signaling Pathways

Contact Info

Product

Resources

About

Recent Advances in the Regulation of Brassinosteroid Signaling and Biosynthesis Pathways^F