25 Years of thermomorphogenesis research: milestones and perspectives

In 1998, Bill Gray and colleagues showed that warm temperatures trigger arabidopsis hypocotyl elongation in an auxin-dependent manner. This laid the foundation for a vibrant research discipline. With several active members of the 'thermomorphogenesis' community, we here reflect on 25 years of elevated ambient temperature research and look to the future

A current perspective on the role of AGCVIII kinases in PIN-mediated apical hook development

Despite their sessile lifestyle, seed plants are able to utilize differential growth rates to move their organs in response to their environment. Asymmetrical growth is the cause for the formation and maintenance of the apical hook – a structure of dicotyledonous plants shaped by the bended hypocotyl that eases the penetration through the covering soil. As predicted by the Cholodny-Went theory, the cause for differential growth is the unequal distribution of the phytohormone auxin. The PIN-FORMED proteins transport auxin from cell-to-cell and control the distribution of auxin in the plant. Their localization and activity are regulated by two subfamilies of AGCVIII protein kinases: the D6 PROTEIN KINASEs as well as PINOID and its two closely related WAG kinases. This review focuses on the regulatory mechanism of these AGCVIII kinases as well as their role in apical hook development of Arabidopsis thaliana

A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors

A subset of α/β hydrolases is known to suppress the pathogen-triggered hypersensitive response (HR) in plants, but their mechanism of action remains unclear. The authors present two crystal structures and functional analyses of these enzymes, showing that HR is suppressed by a previously unknown family of deacetylases

Gibberellin Regulates PIN-FORMED Abundance and Is Required for Auxin Transport–Dependent Growth and Development in Arabidopsis thaliana[C][W]

This work presents physiological, cell biological, and developmental data that establish that gibberellins (GA) is required for proper polar auxin transport in Arabidopsis thaliana. It shows that the GA pathway interacts with PIN protein-dependent auxin transport and development, suggesting that at least some of the growth defects of GA biosynthesis and signaling mutants are a result of altered auxin transport

The DELLA Domain of GA INSENSITIVE Mediates the Interaction with the GA INSENSITIVE DWARF1A Gibberellin Receptor of Arabidopsis[W]

Gibberellic acid (GA) promotes seed germination, elongation growth, and flowering time in plants. GA responses are repressed by DELLA proteins, which contain an N-terminal DELLA domain essential for GA-dependent proteasomal degradation of DELLA repressors. Mutations of or within the DELLA domain of DELLA repressors have been described for species including Arabidopsis thaliana, wheat (Triticum aestivum), maize (Zea mays), and barley (Hordeum vulgare), and we show that these mutations confer GA insensitivity when introduced into the Arabidopsis GA INSENSITIVE (GAI) DELLA repressor. We also demonstrate that Arabidopsis mutants lacking the three GA INSENSITIVE DWARF1 (GID1) GA receptor genes are GA insensitive with respect to GA-promoted growth responses, GA-promoted DELLA repressor degradation, and GA-regulated gene expression. Our genetic interaction studies indicate that GAI and its close homolog REPRESSOR OF ga1-3 are the major growth repressors in a GA receptor mutant background. We further demonstrate that the GA insensitivity of the GAI DELLA domain mutants is explained in all cases by the inability of the mutant proteins to interact with the GID1A GA receptor. Since we found that the GAI DELLA domain alone can mediate GA-dependent GID1A interactions, we propose that the DELLA domain functions as a receiver domain for activated GA receptors

BRASSINOSTEROID-SIGNALING KINASE 3, a plasma membrane-associated scaffold protein involved in early brassinosteroid signaling

<div><p>Brassinosteroids (BRs) are steroid hormones essential for plant growth and development. The BR signaling pathway has been studied in some detail, however, the functions of the BRASSINOSTEROID-SIGNALING KINASE (BSK) family proteins in the pathway have remained elusive. Through forward genetics, we identified five semi-dominant mutations in the <i>BSK3</i> gene causing <i>BSK3</i> loss-of-function and decreased BR responses. We therefore investigated the function of BSK3, a receptor-like cytoplasmic kinase, in BR signaling and plant growth and development. We find that BSK3 is anchored to the plasma membrane via N-myristoylation, which is required for its function in BR signaling. The N-terminal kinase domain is crucial for BSK3 function, and the C-terminal three tandem TPR motifs contribute to BSK3/BSK3 homodimer and BSK3/BSK1 heterodimer formation. Interestingly, the effects of BSK3 on BR responses are dose-dependent, depending on its protein levels. Our genetic studies indicate that kinase dead BSK3^K86R protein partially rescues the <i>bsk3-1</i> mutant phenotypes. BSK3 directly interacts with the BSK family proteins (BSK3 and BSK1), BRI1 receptor kinase, BSU1 phosphatase, and BIN2 kinase. BIN2 phosphorylation of BSK3 enhances BSK3/BSK3 homodimer and BSK3/BSK1 heterodimer formation, BSK3/BRI1 interaction, and BSK3/BSU1 interaction. Furthermore, we find that BSK3 upregulates <i>BSU1</i> transcript and protein levels to activate BR signaling. <i>BSK3</i> is broadly expressed and plays an important role in BR-mediated root growth, shoot growth, and organ separation. Together, our findings suggest that BSK3 may function as a scaffold protein to regulate BR signaling. The results of our studies provide new insights into early BR signaling mechanisms.</p></div