受体激酶介导的油菜素内酯信号转导途径

油菜素内酯（brassinosteroids,BRs）是一类重要的类固醇激素,参与调控植物生长发育的许多过程。结合应用遗传学、生物化学以及蛋白质组学等研究手段现已基本阐明了BR信号转导的主要过程。BRI1作为受体在细胞表面感知BR,BRI1抑制子BKI1从质膜上解离下来,使BRI1与其共受体BAK1结合。BRI1和BAK1通过顺序磷酸化将BR信号完全激活。活化的BRI1将BSK磷酸化激活,BSK活化BSU1,BSU1将BIN2去磷酸化使其失活,解除BIN2对BES1/BZR1的抑制功能。PP2A可以将BES1/BZR1去磷酸化激活,又可以将受体BRI1去磷酸化促使其降解。BR信号的传递最终使去磷酸化状态的BES1/BZR1在细胞内累积,激活BR信号通路下游的转录调控。     

Brassinosteroid signaling and application in rice

Combined approaches with genetics, biochemistry, and proteomics studies have greatly advanced our understanding of brassinosteroid (BR) signaling in Arabidopsis. However, in rice, a model plant of monocot and as well an important crop plant, BR signaling is not as well characterized as in Arabidopsis. Recent studies by forward and reverse genetics have identified a number of either conserved or specific components of rice BR signaling pathway, bringing new ideas into BR signaling regulation mechanisms. Genetic manipulation of BR level or BR sensitivity to improve rice yield has established the great significance of BR research achievements.     

Brassinosteroid Signal Transduction: A Mix of Conservation and Novelty

Brassinosteroids (BRs) are a unique class of plant steroids that are structurally similar to animal steroid hormones and play important roles in plant growth and development. Unlike the animal steroids, which bind to classical intracellular steroid receptors that directly modulate gene activities after translocation into the nucleus, the plant steroids rely on transmembrane receptor kinases to activate a phosphorylation cascade to regulate gene expression. Recent genetic and biochemical studies have identified several critical BR signaling components and revealed a striking mechanistic similarity between the plant steroid signaling pathway and several well-studied animal signaling cascades involving a receptor kinase and glycogen synthase kinase 3 (GSK3). A working model for BR signal transduction proposes that BR initiates its signaling pathway by promoting heterodimerization of two transmembrane receptor-like kinases at the cell surface, leading to inhibition of a GSK3 kinase and subsequent stabilization and nuclear accumulation of two GSK3 substrates that regulate BR-responsive genes. Such a simple model provides a framework for continued investigation of molecular mechanism(s) of plant steroid signaling.     

On the Origin and Evolution of Plant Brassinosteroid Receptor Kinases

Brassinosteroid (BR) signaling pathway is so far the best-understood receptor-kinase signaling pathway in plants. In Arabidopsis, the activation of this pathway requires binding of BRs to the receptor kinase BRASSINOSTEROID-INSENSITIVE I (AtBRI1). Although the function of AtBRI1 has been extensively studied, it is not known when the binding function emerged and how this important component of BR signaling pathway and related genes (the BRI1–BRL gene family) have evolved in plants. We define BRI1–BRL genes in sequenced plant genomes, construct profiles for critical protein domains, scan them against all accessible plant gene/EST resources, and reveal the evolution of domain configuration of this family. We also investigate its evolutionary pattern through phylogenetic analysis. The complete BR receptor domain configuration originates through two domain gain events in the ancestral receptor-like kinase: first juxtamembrane domain gained during the early diversification of land plants, and then island domain (ID) acquired in the common ancestor of angiosperms and gymnosperms after its divergence from spike moss. The 70 amino acid ID has characteristic sequences of BRI1–BRL family and this family keeps relative stable copy numbers during the history of angiosperms and the majority of duplications and losses have occurred in terminal taxa in current taxon sampling. This study reveals important events shaping structural and functional characteristics of plant BR receptors. It answers the question of how and when BR receptors originates, which provide insights into the origin and evolution of the BR signaling pathway.     

Autophagy: A critical regulator of cellular metabolism and homeostasis

Plants possess a variety of extracellular leucine-rich repeats receptor-like kinases (LRR-RLKs) to coordinate developmental programs with responses to environmental changes. Out of sixteen families of LRR-RLKs in Arabidopsis, the LRR-RLKII family consists of fourteen individual members, including five Arabidopsis thaliana somatic embryogenesis receptor kinases (AtSERKs). BAK1/AtSERK3 was first identified as a dual co-receptor of BRI1 and FLS2, mediating BR signaling and pathogen-associated molecular pattern (PAMP) triggered immunity (PTI), respectively. Since its identification, many researchers have attempted to elucidate the phosphorylation mechanisms between receptor complexes and identify additional components that interact with receptor complexes to transduce the signaling downstream. Relatively detailed early events in complex formation, phosphorylation sites on the BRI1/BAK1 complex and BAK1-interacting proteins, such as BIK1 and PUB13, have been identified. Small receptor complexes consisting of BAK1 and BIR1 or BAK1 and AtSERK4 regulate cell death during steady state conditions. Moreover, the redundant and distinct functions of AtSERK proteins and other members of the LRR-RLKII family have been revealed. This review focuses on the integration of the information from the most recent studies concerning BAK1 and its homologs.