Submitted Successfully!
To reward your contribution, here is a gift for you: A free trial for our video production service.
Thank you for your contribution! You can also upload a video entry or images related to this topic.
Version Summary Created by Modification Content Size Created at Operation
1
Koushik Halder
 -- 2262 2022-12-08 20:40:52 |
2 format correct
Vivi Li
 Meta information modification 2262 2022-12-09 04:15:37 |

Video Upload Options

Do you have a full video?
Send video materials Upload full video

Confirm

Are you sure to Delete?
Yes No
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Chaudhuri, A.;  Halder, K.;  Abdin, M.Z.;  Majee, M.;  Datta, A. Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants. Encyclopedia. Available online: https://encyclopedia.pub/entry/38366 (accessed on 27 July 2024).
Chaudhuri A,  Halder K,  Abdin MZ,  Majee M,  Datta A. Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants. Encyclopedia. Available at: https://encyclopedia.pub/entry/38366. Accessed July 27, 2024.
Chaudhuri, Abira, Koushik Halder, Malik Z. Abdin, Manoj Majee, Asis Datta. "Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants" Encyclopedia, https://encyclopedia.pub/entry/38366 (accessed July 27, 2024).
Chaudhuri, A.,  Halder, K.,  Abdin, M.Z.,  Majee, M., & Datta, A. (2022, December 08). Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants. In Encyclopedia. https://encyclopedia.pub/entry/38366
Chaudhuri, Abira, et al. "Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants." Encyclopedia. Web. 08 December, 2022.
Brassinosteroid Hormones and Abiotic Stress Tolerance in Plants
Edit
This entry is adapted from the peer-reviewed paper 10.3390/ijms232314577

Brassinosteroid hormones (BRs) multitask to smoothly regulate a broad spectrum of vital physiological processes in plants, such as cell division, cell expansion, differentiation, seed germination, xylem differentiation, reproductive development and light responses (photomorphogenesis and skotomorphogenesis). Their importance is inferred when visible abnormalities arise in plant phenotypes due to suboptimal or supraoptimal hormone levels. This group of steroidal hormones are major growth regulators, having pleiotropic effects and conferring abiotic stress resistance to plants. Numerous abiotic stresses are the cause of significant loss in agricultural yield globally. However, plants are well equipped with efficient stress combat machinery. Scavenging reactive oxygen species (ROS) is a unique mechanism to combat the deleterious effects of abiotic stresses.

brassinosteroid abiotic stress signaling transcription factors

1. Introduction

Plants are sessile organisms and are invariably exposed to a plethora of environmental stress factors, both biotic and abiotic, the rapidly changing climatic conditions being a leading cause. Primarily, heat, cold, drought, flood, salinity and heavy metals/metalloids have posed potential threats to agriculture through generations, as they hamper the basic life mechanisms, both at a physiological and molecular level [1][2]. Numerous phytohormones interact with various factors such as reactive oxygen species (ROS), metabolites, etc., to expedite the plant’s response to any stressful stimuli [3][4]. Lately, BRs have taken a center stage in the phytohormone family, since they have displayed diverse roles in plant growth and development [5][6].
Rigorous research over the past few decades has proved with numerous supporting pieces of evidence that BRs possess significant power in mitigating the stress impact when plants are exposed to the above categories of stresses [7]. The plant-specific ligands of BRs directly bind to the cell surface receptors called leucine-rich repeat receptor kinases BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-associated receptor kinase (BAK1). The signaling happens via phosphorylation triggered inside the cytoplasm, involving phosphorylation of the BSU1 protein and the proteasome-mediated pulling down of BRASSINOSTEROID-INSENSITIVE 2 (BIN2) proteins. This deactivation of BIN2 paves the way for BRI1 EMS SUPPRESSOR/Brassinozole-resistant 1 (BES1/BZR1) to gain access to the target genes inside the nucleus [8]. This signaling cascade involves cross-talk with multiple phytohormones which have been duly established [9][10][11]. BRs participate in an active manner in plants to regulate diverse developmental processes [5], and a graphical representation is provided in Figure 1. Physiological abnormalities triggered by stress can be overcome by the exogenous application of BRs, and this phenomenon has gained considerable importance among scientists [12][13]. Research is continuing at the physiological and molecular level in different laboratories worldwide, yet the role of BRs in nullifying the adverse effects of stress is still an enigma. The reason for this haze in the signaling network is assumed to be not only the presence but also the cross-talk among them to eventually mitigate stress [14][15]. Here, researchers discuss in detail some of the potential abiotic stress factors and how their deleterious effects are modulated by BRs. The inferences gained here might be extrapolated for stress management in the case of many important food and cash crops.
Ijms 23 14577 g001 550
Figure 1. Active regulation of a wide array of developmental processes in plants by Brassinosteroids (BRs).

2. Brassinosteroid Signaling Cascade

Cell signaling via the cell-surface embedded receptors are the key to the survival and development of plants. In plants, signaling via cell surface receptors take place through ‘Receptor-Like-Kinases’ (RLKs) and they are considered to be the major type of receptors [16]. The structure of the RLKs is quite simple, consisting of three domains: an extracellular domain whose function is to attach to ligands, one transmembrane domain, and finally a cytoplasmic kinase domain which triggers all intracellular signal transmission. RLKs are the key participants of the signaling cascades that act during the defense responses in plants [17]. In case of BRs, the RLK which acts as the potential receptor for this steroid hormone is BRASSINOSTEROID INSENSITIVE 1 (BRI1). This receptor is the key regulator for a broad range of physiological and developmental processes in plants. Any type of mutation of BRI1 might have far-reaching negative consequences in plant development. Advanced research has identified many additional components of the BR signaling cascade, e.g., the co-receptor BRI1-Associated Receptor Kinase 1 (BAK1), GSK-3 like kinase BRASSINOSTEROID-INSENSITIVE 2 (BIN2), Bri1-suppressor 1 phosphatase (BSU1) and the Brassinozole-resistant (BZR) family of transcription factors [18].
Some very significant proteomic studies have also given helpful insights to researchers, as they established BR signaling kinases (BSKs) to act as substrate for the BRI1 kinase that acts as a connecting link between the receptor kinases present on the plasma membrane and the downstream cytoplasmic elements [19][20]. Further phosphoproteomic studies, especially detailed mass-spectrometry analysis, clearly established the presence and involvement of phosphorylation sites in the BR signaling cascade [21][22][23]. The BR signaling cascade can be divided into a stepwise process, as outlined below.

2.1. Jump-Start of BRI1 Receptor Kinase by Brassinosteroid

The BRI1 protein belongs to the leucine-rich repeat RLK (LRR-RLK) family. BRI1 is constructed of an extracellular domain consisting of 24 LRRs and a small island (ID) juxtaposed in between LRR20 and 21. BRs attach directly to the ID domain (ID-LRR21) which leads to the activation of the BRI1 kinase [24], which performs its assigned task of phosphorylating target proteins located in the cytoplasm and thus commences intracellular signal transmission. A plethora of mechanisms are interconnected in the whole process of ligand-triggered activation of BRI1. BRI1 kinase remains in a dormant state in the absence of BRs due to two partial hindrances: one being the unphosphorylated condition of the CT domain [25] and the other being attachment to the inhibitory protein BKI1 [26]. The attachment of BRs instantly triggers a series of molecular events that eventually leads to kinase activation. These molecular events include homodimerization and autophosphorylation of BRI1 [25][27], uncoupling of the BRI1 Kinase Inhibitor [26] and finally the attachment/transphosphorylation with the BAK1 co-receptor kinase [22][23].

2.2. Interaction of BRI1 with Receptor Complex Associates

BAK1 is an RLK that interplays with BRI1. BRI1 kinase is the key player that is kicked into action the moment BRs come into the scenario, linking BRI1 with BAK1, which can be vouched by numerous evidence. Firstly, it was proved that mutant BRI1 sans kinase activity betrayed a remarkable decline in binding with BAK1 both during in vitro and in vivo conditions. However, in case of mutated BAK1 kinase there was only a negligible decline in interaction [28][29]. The second piece of evidence is that BR is capable of triggering linkage between a wild-type BRI1 with a ‘kinase-dead’ mutant BAK1 but not vice versa [22]. In another line of evidence, it was seen that BR fails to hike up the phosphorylation of BAK1 in the bri1-1 mutant but can perform the exact opposite during BRI1 phosphorylation in the bak1, bakk1 double mutant. The observation and inferences obtained from the in vitro kinase assays gave a picture that BAK1 actively transphosphorylates BRI1, which bestows extreme power to BRI1 kinase activity towards its substrate peptide. Therefore, to sum up it can be stated that the phosphorylation of BAK1, which is totally BR induced, is controlled by BRI1 kinase activity, whereas in another line of action, the transphosphorylation of the substrate peptide by BRI1 is severely boosted by phosphorylation of BAK1 [22]. However, studies by two prominent research groups [28][29] paved the way to concluding that the overexpression of a dominant negative mutant bak1 resulted in a significant dwarf phenotype, and this points clearly to that the presence of BAK1 is mandatory in the BR signaling cascade.

2.3. Joining the Dots to Complete the BR Signaling Cascade

The downstream components of the BR signaling cascade are numerous and significant. To start, there is BIN2, which is a GSK3/SHAGGY-like protein kinase; BSU1, a phosphate with Kelch repeats; and finally, the transcription factors BZR1 and BZR2, which are also called by the name BES1 [16]. When BR is not present in the scene, the BR signaling cascade faces a negative command by BIN2, which phosphorylates BZR1 and BES1/BZR2 to carry out this hindrance [30][31]. BZR1 and BES1/BZR2 are disabled from functioning due to phosphorylation by BIN2, and this process takes place in diverse ways: the first being by hindering DNA binding and nuclear localization and the second being by advocating degradation by the proteasome [30][31][32][33][34]. The S173 residue of BZR1 is phosphorylated and this leads to a potential association with the 14-3-3 proteins, which transport and maintain BZR1 and BZR2/BES1 inside the cytoplasm [33][34]. The exact opposite activity of BIN2 is performed by BSU1 phosphatase, which facilitates dephosphorylation of BES1/BZR2 in plants [35].
Many research groups were in a dilemma in the past about the exact function of BSU1, which was presumed to participate in the dephosphorylation process of BES1/BZR2. However, extensive research [20] has shed light on the biochemical and genetic aspects of the BR signaling cascade. This has given a vivid picture that BSU1 has a direct downstream location from BSK1 and upstream of BIN2. BSU1 functions in a very interesting way by disabling BIN2, rather than directly dephosphorylating BES1/BZR2 or BZR1, which in turn stops phosphorylation, and this disabling happens by dephosphorylation of a phospho-tyrosine residue (pY200) of BIN2. Once again, [20] pinpointed that BSU11 has some versatile traits, such as interacting with BIN2 as well as BSK1 directly, both in vitro and in vivo. BSU1 strongly binds with BSK1, and the condition for this happens to be BSK1 being phosphorylated by BRI1 and almost annihilated by a mutation at the BRI1 phosphorylation site (S230A). The activation of BSU1 happens by phosphorylation, and this is carried out by BSK1. In addition, was inferred that BR treatment causes a spike in BSU1′s inhibiting capacity of BIN2. Finally, researchers can draw a conclusion about the complete BR signaling pathway, which comprises a line of chronological events starting from the kick-start of BRI1, BSK1 and BSU1, deactivation of BIN2 and accretion of unphosphorylated BZR1 along with BZR2/BES1 inside the nucleus. This entire mechanism deciphered by research provides a concrete basis of a ligand’s grasp by RLK and links it with the downstream transcription factors in a plant body. However, one missing link still remains to be found, and that is the identity crisis of the protein phosphatase responsible for the dephosphorylation of the BZR transcription factor. Further genetic studies using mutants clearly point out that the pathway linking BRI1 to BZR1/BES1 is the main signaling route for the majority of BR-induced responses. A summary of the BR signaling pathway is shown in Figure 2.
Ijms 23 14577 g002 550
Figure 2. A comprehensive diagram depicting the brassinosteroid signaling pathway in plants.

3. Signaling and Regulation by BRs (Endogenous and Exogenous) in Plants under Abiotic Stress

It has already been established by various research groups that BRs control some crucial physiological and biochemical processes such as cell differentiation, cell division, elongation, etc. The model plant Arabidopsis thaliana is a potential platform for experimentation on BRs and has been a source of many recent findings. Plants have a labyrinth of extraordinary signaling networks that sense and respond appropriately to the ever-changing environment. In the present day, the nature of stress is also rather complex, therefore the active participation of a multitude of sensors for signal perception and transmission are preempted. The signaling cascades are activated spontaneously after the stress trigger, which eventually activates the stress-responsive genes. According to established results, the membrane-based steroid receptor BRI1 binds with BR, and this triggers a chain reaction of cytoplasmic signaling that leads to the expression of BR-associated genes. It was well observed in this context that in Arabidopsis thaliana the primary roots have shown precise stress-responsive signals as an adaptive response to stress [10]. More and more scientists are working presently on BR-associated stress-responsive signaling mechanisms which are potential routes to decode the plant’s adjusting capacity to biotic and abiotic stress [36][37]. BRs balance environmental assaults and the normal growth process by operating through several signaling routes, e.g., acting independently by engaging in cross-talk with other phytohormones [10]. The machineries that are activated by BR signaling to bring about adaptive response are the elevated production of osmoprotectants [38], the triggering of antioxidant production machinery [39] and the arousal of stress-responsive transcription factors [40]. BRs have a considerably significant interaction with a variety of stress-related transcription factors (TFs), directly or indirectly. This operation takes place through the pathway involving the negative regulator BIN2 and prominent TFs BZR1/BES1 that eventually trigger stress-adaptive signaling pathways. Other potential transcription factors that take part in this entire operation of synchronizing abiotic stress response are DREB, WRKY, MYB/MYC, GRAS, bZIP, NAC, NPR, etc. [41]. Figure 3 gives a graphic detail of the mechanisms adopted by BRs in positively controlling abiotic stresses in plants through signaling at various levels by actively interacting with TFs.
Ijms 23 14577 g003 550
Figure 3. A vivid picture of the numerous mechanisms endorsed by the Brassinosteroids at different levels in plants to mitigate a plethora of potentially fatal abiotic stresses with close association with transcription factors.
Ref. [42] showed that BRs are associated with nitrogen (N) starvation in plants and the responses are via the modulation of autophagy, which is a self-destructive process as known to all and followed by plants to mediate stress response. Next comes the entry of the exogenous application of BRs. Exogenous BRs elevate the transcript levels of autophagy-associated genes and the generation of autophagosomes [43]. Various pharmacological approaches give researchers an idea about the effects of exogenous application of BRs on plants to infer the stress-responsive/stress-protective role of BRs. Different pharmacological techniques of application such as foliar spray, pre-sowing seed treatment, pre-planting, dipping of cuttings, post-emergence root treatment, etc., have been applied to a vast range of plant species [44][45][46][47][48]. Many scientist groups [47][49] have established that the effects of exogenously applied BRs depend on quite a number of parameters, such as plants, dose, growth stage, conditions of growth, viz., with/without stress, signaling molecules, growth regulators, cross-talk with other hormones, etc.

References

  1. Hasanuzzaman, M. Plant Ecophysiology and Adaptation under Climate Change: Mechanisms and Perspectives I: General Consequences and Plant Responses. In Plant Ecophysiology and Adaptation under Climate Change: Mechanisms and Perspectives I: General Consequences and Plant Responses; Springer Nature: Berlin/Heidelberg, Germany, 2020; pp. 1–859. ISBN 9789811521560.
  2. Saddiq, M.S.; Afzal, I.; Iqbal, S.; Hafeez, M.B.; Raza, A. Low Leaf Sodium Content Improves the Grain Yield and Physiological Performance of Wheat Genotypes in Saline-Sodic Soil. Pesqui. Agropecu. Trop. 2021, 51.
  3. Zahra, N.; Mahmood, S.; Raza, Z.A. Salinity Stress on Various Physiological and Biochemical Attributes of Two Distinct Maize (Zea mays L.) Genotypes. J. Plant Nutr. 2018, 41, 1368–1380.
  4. Zahra, N.; Wahid, A.; Shaukat, K.; Rasheed, T. Role of Seed Priming and Foliar Spray of Calcium in Improving Flag Leaf Growth, Grain Filling and Yield Characteristics in Wheat (Triticum aestivum)—A Field Appraisal. Int. J. Agric. Biol. 2020, 24, 1591–1600.
  5. Wei, Z.; Li, J. Brassinosteroids Regulate Root Growth, Development, and Symbiosis. Mol. Plant 2016, 9, 86–100.
  6. Nazir, F.; Hussain, A.; Fariduddin, Q. Interactive Role of Epibrassinolide and Hydrogen Peroxide in Regulating Stomatal Physiology, Root Morphology, Photosynthetic and Growth Traits in Solanum lycopersicum L. under Nickel Stress. Environ. Exp. Bot. 2019, 162, 479–495.
  7. Vardhini, B.V.; Anjum, N.A. Brassinosteroids Make Plant Life Easier under Abiotic Stresses Mainly by Modulating Major Components of Antioxidant Defense System. Front. Environ. Sci. 2015, 2, 67.
  8. Hafeez, M.B.; Zahra, N.; Zahra, K.; Raza, A.; Khan, A.; Shaukat, K.; Khan, S. Brassinosteroids: Molecular and Physiological Responses in Plant Growth and Abiotic Stresses. Plant Stress 2021, 2, 100029.
  9. Mubarik, M.S.; Khan, S.H.; Sajjad, M.; Raza, A.; Hafeez, M.B.; Yasmeen, T.; Rizwan, M.; Ali, S.; Ali, S.; Arif, M.S. A Manipulative Interplay between Positive and Negative Regulators of Phytohormones: A Way Forward for Improving Drought Tolerance in Plants. Physiol. Plant 2021, 172, 1269–1290.
  10. Planas-Riverola, A.; Gupta, A.; Betegoń-Putze, I.; Bosch, N.; Ibañes, M.; Cano-Delgado, A.I. Brassinosteroid Signaling in Plant Development and Adaptation to Stress. Development 2019, 146, dev151894.
  11. Kour, J.; Kohli, S.K.; Khanna, K.; Bakshi, P.; Sharma, P.; Singh, A.D.; Ibrahim, M.; Devi, K.; Sharma, N.; Ohri, P.; et al. Brassinosteroid Signaling, Crosstalk and, Physiological Functions in Plants under Heavy Metal Stress. Front. Plant Sci. 2021, 12, 608061.
  12. Zhang, C.; Bai, M.; Chong, K. Brassinosteroid-Mediated Regulation of Agronomic Traits in Rice. Plant Cell Rep. 2014, 33, 683–696.
  13. Ahanger, M.A.; Mir, R.A.; Alyemeni, M.N.; Ahmad, P. Combined Effects of Brassinosteroid and Kinetin Mitigates Salinity Stress in Tomato through the Modulation of Antioxidant and Osmolyte Metabolism. Plant Physiol. Biochem. 2020, 147, 31–42.
  14. Ahammed, G.J.; Li, X.; Xia, X.J.; Shi, K.; Zhou, Y.H.; Yu, J.Q. Enhanced Photosynthetic Capacity and Antioxidant Potential Mediate Brassinosteriod-Induced Phenanthrene Stress Tolerance in Tomato. Environ. Pollut. 2015, 201, 58–66.
  15. Divi, U.K.; Rahman, T.; Krishna, P. Gene Expression and Functional Analyses in Brassinosteroid-Mediated Stress Tolerance. Plant Biotechnol. J. 2016, 14, 419–432.
  16. Tang, W.; Deng, Z.; Wang, Z.Y. Proteomics shed light on the brassinosteroid signaling mechanisms. Curr. Opin. Plant Biol. 2010, 13, 27–33.
  17. Johnson, K.L.; Ingram, G.C. Sending the Right Signals: Regulating Receptor Kinase Activity. Curr. Opin. Plant Biol. 2005, 8, 648–656.
  18. Vert, G.; Nemhauser, J.L.; Geldner, N.; Hong, F.; Chory, J. Molecular Mechanisms of Steroid Hormone Signaling in Plants. Annu. Rev. Cell Dev. Biol. 2005, 21, 177–201.
  19. Tang, W.; Tae-Wuk, K.; Oses-Prieto, J.A.; Yu, S.; Deng, Z.; Zhu, S.; Wang, R.; Burlingame, A.L.; Wang, Z.-Y. BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis. Science 2008, 321, 557–560.
  20. Kim, T.W.; Guan, S.; Sun, Y.; Deng, Z.; Tang, W.; Shang, J.X.; Sun, Y.; Burlingame, A.L.; Wang, Z.Y. Brassinosteroid Signal Transduction from Cell-Surface Receptor Kinases to Nuclear Transcription Factors. Nat. Cell Biol. 2009, 11, 1254–1260.
  21. Karlova, R.; Boeren, S.; Van Dongen, W.; Kwaaitaal, M.; Aker, J.; Vervoort, J.; De Vries, S. Identification of in Vitro Phosphorylation Sites in the Arabidopsis Thaliana Somatic Embryogenesis Receptor-like Kinases. Proteomics 2009, 9, 368–379.
  22. Wang, X.; Kota, U.; He, K.; Blackburn, K.; Li, J.; Goshe, M.B.; Huber, S.C.; Clouse, S.D. Sequential Transphosphorylation of the BRI1/BAK1 Receptor Kinase Complex Impacts Early Events in Brassinosteroid Signaling. Dev. Cell 2008, 15, 220–235.
  23. Wang, X.; Goshe, M.B.; Soderblom, E.J.; Phinney, B.S.; Kuchar, A.; Li, J.; Asami, T.; Yoshida, S.; Huber, S.C.; Clouse, S.D.; et al. Identification and Functional Analysis of in Vivo Phosphorylation Sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 Receptor Kinase. Plant Cell 2005, 17, 1685–1703.
  24. Kinoshita, T.; Caño-Delgado, A.; Seto, H.; Hiranuma, S.; Fujioka, S.; Yoshida, S.; Chory, J. Binding of Brassinosteroids to the Extracellular Domain of Plant Receptor Kinase BRI1. Nature 2005, 433, 167–171.
  25. Wang, X.; Li, X.; Meisenhelder, J.; Hunter, T.; Yoshida, S.; Asami, T.; Chory, J. Autoregulation and Homodimerization Are Involved in the Activation of the Plant Steroid Receptor BRI1. Dev. Cell 2005, 8, 855–865.
  26. Wang, X.; Chory, J. Brassinoteroids Regulate Dissociation of BKI1, a Negative Regulator of BRI1 Signaling, from the Plasma Membrane. Science 2006, 313, 1118–1122.
  27. Wang, Z.-Y.; Seto, H.; Fujioka, S.; Yoshida, S.; Chory, J. BRI1 Is a Critical Component of a Plasma-Membrane Receptor for Plants Steroids. Nature 2001, 410, 380–383.
  28. Nam, K.H.; Li, J. BRI1/BAK1, a Receptor Kinase Pair Mediating Brassinosteroid Signaling. Cell 2002, 110, 203–212.
  29. Li, J.; Wen, J.; Lease, K.A.; Doke, J.T.; Tax, F.E.; Walker, J.C. BAK1, an Arabidopsis LRR Receptor-like Protein Kinase, Interacts with BRI1 and Modulates Brassinosteroid Signaling. Cell 2002, 110, 213–222.
  30. He, J.X.; Gendron, J.M.; Yang, Y.; Li, J.; Wang, Z.Y. The GSK3-like Kinase BIN2 Phosphorylates and Destabilizes BZR1, a Positive Regulator of the Brassinosteroid Signaling Pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 2002, 99, 10185–10190.
  31. Yin, Y.; Wang, Z.Y.; Mora-Garcia, S.; Li, J.; Yoshida, S.; Asami, T.; Chory, J. BES1 Accumulates in the Nucleus in Response to Brassinosteroids to Regulate Gene Expression and Promote Stem Elongation. Cell 2002, 109, 181–191.
  32. Vert, G.; Chory, J. Downstream Nuclear Events in Brassinosteroid Signalling. Nature 2006, 441, 96–100.
  33. Gampala, S.S.; Kim, T.W.; He, J.X.; Tang, W.; Deng, Z.; Bai, M.Y.; Guan, S.; Lalonde, S.; Sun, Y.; Gendron, J.M.; et al. An Essential Role for 14-3-3 Proteins in Brassinosteroid Signal Transduction in Arabidopsis. Dev. Cell 2007, 13, 177–189.
  34. Ryu, H.; Kim, K.; Cho, H.; Park, J.; Choe, S.; Hwang, I. Nucleocytoplasmic Shuttling of BZR1 Mediated by Phosphorylation Is Essential in Arabidopsis Brassinosteroid Signaling. Plant Cell 2007, 19, 2749–2762.
  35. Mora-García, S.; Vert, G.; Yin, Y.; Caño-Delgado, A.; Cheong, H.; Chory, J. Nuclear Protein Phosphatases with Kelch-Repeat Domains Modulate the Response to Brassinosteroids in Arabidopsis. Genes Dev. 2004, 18, 448–460.
  36. Anwar, A.; Liu, Y.; Dong, R.; Bai, L.; Yu, X.; Li, Y. The Physiological and Molecular Mechanism of Brassinosteroid in Response to Stress: A Review. Biol. Res. 2018, 51, 1–15.
  37. Nolan, T.; Chen, J.; Yin, Y. Cross-Talk of Brassinosteroid Signaling in Controlling Growth and Stress Responses. Biochem. J. 2017, 474, 2461–2661.
  38. Fàbregas, N.; Lozano-Elena, F.; Blasco-Escámez, D.; Tohge, T.; Martínez-Andújar, C.; Albacete, A.; Osorio, S.; Bustamante, M.; Riechmann, J.L.; Nomura, T.; et al. Overexpression of the Vascular Brassinosteroid Receptor BRL3 Confers Drought Resistance without Penalizing Plant Growth. Nat. Commun. 2018, 9, 1–13.
  39. Zou, L.J.; Deng, X.G.; Zhang, L.E.; Zhu, T.; Tan, W.R.; Muhammad, A.; Zhu, L.J.; Zhang, C.; Zhang, D.W.; Lin, H.H. Nitric Oxide as a Signaling Molecule in Brassinosteroid-Mediated Virus Resistance to Cucumber Mosaic Virus in Arabidopsis thaliana. Physiol. Plant 2018, 163, 196–210.
  40. Ye, H.; Liu, S.; Tang, B.; Chen, J.; Xie, Z.; Nolan, T.M.; Jiang, H.; Guo, H.; Lin, H.Y.; Li, L.; et al. RD26 Mediates Crosstalk between Drought and Brassinosteroid Signalling Pathways. Nat. Commun. 2017, 8, 14573.
  41. Sharma, I.; Kaur, N.; Pati, P.K. Brassinosteroids: A Promising Option in Deciphering Remedial Strategies for Abiotic Stress Tolerance in Rice. Front. Plant Sci. 2017, 8, 2151.
  42. Wang, Y.; Cao, J.J.; Wang, K.X.; Xia, X.J.; Shi, K.; Zhou, Y.H.; Yu, J.Q.; Zhoua, J. BZR1 Mediates Brassinosteroid-Induced Autophagy and Nitrogen Starvation in Tomato. Plant Physiol. 2019, 179, 671–685.
  43. Ahammed, G.J.; Li, X.; Liu, A.; Chen, S. Brassinosteroids in Plant Tolerance to Abiotic Stress. J. Plant Growth Regul. 2020, 39, 1451–1464.
  44. Amraee, L.; Rahmani, F.; Abdollahi Mandoulakani, B. 24-Epibrassinolide Alters DNA Cytosine Methylation of Linum Usitatissimum L. under Salinity Stress. Plant Physiol. Biochem. 2019, 139, 478–484.
  45. Sharma, A.; Thakur, S.; Kumar, V.; Kanwar, M.K.; Kesavan, A.K.; Thukral, A.K.; Bhardwaj, R.; Alam, P.; Ahmad, P. Pre-Sowing Seed Treatment with 24-Epibrassinolide Ameliorates Pesticide Stress in Brassica juncea L. through the Modulation of Stress Markers. Front. Plant Sci. 2016, 7, 1569.
  46. Sharma, A.; Yuan, H.; Kumar, V.; Ramakrishnan, M.; Kohli, S.K.; Kaur, R.; Thukral, A.K.; Bhardwaj, R.; Zheng, B. Castasterone Attenuates Insecticide Induced Phytotoxicity in Mustard. Ecotoxicol. Environ. Saf. 2019, 179, 50–61.
  47. Yin, W.; Dong, N.; Niu, M.; Zhang, X.; Li, L.; Liu, J.; Liu, B.; Tong, H. Brassinosteroid-Regulated Plant Growth and Development and Gene Expression in Soybean. Crop J. 2019, 7, 411–418.
  48. Yue, J.; You, Y.; Zhang, L.; Fu, Z.; Wang, J.; Zhang, J.; Guy, R.D. Exogenous 24-Epibrassinolide Alleviates Effects of Salt Stress on Chloroplasts and Photosynthesis in Robinia Pseudoacacia L. Seedlings. J. Plant Growth Regul. 2019, 38, 669–682.
  49. Nolan, T.M.; Vukasinović, N.; Liu, D.; Russinova, E.; Yin, Y. Brassinosteroids: Multidimensional Regulators of Plant Growth, Development, and Stress Responses. Plant Cell 2020, 32, 298–318.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license; additional terms may apply. By using this site, you agree to the Terms and Conditions and Privacy Policy.
Upload a video for this entry
Information
Subjects: Plant Sciences
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Abira Chaudhuri
,
Koushik Halder
,
Malik Z. Abdin
,
Manoj Majee
,
Asis Datta
View Times: 461
Revisions: 2 times (View History)
Update Date: 09 Dec 2022
Table of Contents
    1000/1000
    Hot Most Recent
    Video Production Service
    Feedback