IntroductionBrassinosteroids (BRs) are a group of plant steroidal hormones that are structurally related to animal and insect steroid hormones. BRs regulate a wide range of physiological responses in plants, including cell elongation, photomorphogenesis, xylem differentiation, seed germination [1], and stress responses [2,3]. Although the growth-promoting properties of BRs were recognized in the early 1970s, the first genetic evidence to suggest that BRs are essential for proper plant development came with the isolation of the BR-deficient mutants det2 (de-etiolated2) and cpd (constitutive photomorphogenic dwarf ) [4,5]. Isolation and sequence analysis of DET2 and CPD genes revealed that the encoded proteins share sequence similarities with steroid 5a-reductases and steroid hydroxylases, respectively, indicating a role for these proteins in steroid metabolism. Indeed, feeding det2 and cpd mutant seedlings with BRs rescued their mutant phenotypes to wild-type in a dose-dependent manner, clearly establishing the roles of DET2 and CPD in BR biosynthesis. Numerous other Arabidopsis BR-deficient and BR-insensitive mutants, displaying phenotypic alterations such as dwarfism, small dark-green leaves, a compact rosette structure, delayed flowering and senescence, and reduced fertility [1], were instrumental in the identification of BR signaling components and in understanding to some extent how BR regulates gene expression [6,7]. Numerous reviews detailing BR effects on plant growth and development and BR signaling mechanisms have surfaced in the recent literature [6-10]; these aspects have therefore been discussed only briefly here. The present chapter is focused on the relatively less explored topic of BR-mediated stress responses in plants [3] and highlights the progress made towards understanding the molecular basis of BRmediated plant stress tolerance.Plant Stress Biology. Edited by H. Hirt BR is perceived at the cell surface by BRI1 (BR-INSENSITIVE1), a plasma membrane-localized leucine-rich repeat (LRR) receptor-like kinase (RLK) [11,12]. BR binding to BRI1 induces a series of biochemical events, such as autophosphorylation of BRI1 in its C-terminal domain, dissociation of an inhibitory protein, BKI1 (BRI1 KINASE INHIBITOR1), and association of BRI1 with another LRR RLK, BAK1 (BRI1-ASSOCIATED RECEPTOR KINASE1) [13,14]. The recent demonstration that BR-dependent activation of BRI1 precedes association with BAK1 has led to a model in which BAK1 enhances signaling output through reciprocal BRI1 transphosphorylation [15]. However, whether the main function of BAK1 is to enhance signaling output of BRI1, promote endocytosis of BRI1, or to help link BRI1 with a downstream signaling protein remains to be determined [7]. Other known components of the BR signaling pathway include GSK3 (GLYCO-GEN SYNTHASE KINASE3), BIN2 (BR-INSENSITIVE2), which negatively regulates the transcription factors BZR1 (BRASSINAZOLE-RESISTANT1) and BES1 (BRI1-EMS SUPPRESSOR1) by phosphorylating them [16,17], while the phosphatase BSU1 (BRI1 SUPPRE...