Strigolactone esterase DWARF14 (AtD14) (AtD14)

AtD14 (Strigolactone esterase DWARF14) is a primary receptor in Arabidopsis thaliana that mediates the perception of strigolactones, a class of plant hormones essential for regulating plant architecture and development (UniProt Q9SST0; Hamiaux et al., 2012). It belongs to the alpha/beta-hydrolase superfamily and functions uniquely as both a receptor and an enzyme that hydrolyzes its ligand (Yao et al., 2016). Upon binding strigolactone, AtD14 catalyzes the cleavage of the hormone, leading to the formation of a covalently linked intermediate molecule (CLIM) that triggers a significant conformational change in the protein (Zhao et al., 2013). This structural shift enables AtD14 to interact with the F-box protein MAX2 (More Axillary Growth 2), facilitating the ubiquitination and subsequent proteasomal degradation of SMXL (Suppressor of MAX2-Like) repressor proteins (Yao et al., 2016). This degradation relieves the inhibition of downstream genes, thereby controlling biological processes such as shoot branching, root growth, and the plant's response to nutrient availability (Waters et al., 2017). While AtD14 is a plant-specific protein, it is a significant target in agricultural biotechnology for the development of synthetic strigolactone analogs to manage crop architecture and combat parasitic weeds (Waters et al., 2017).

Other names

DWARF14D14At3g03990PRY2Decreased apical dominance 2 homolog

AtD14 acts as a covalent receptor that hydrolyzes strigolactones to form a covalent adduct, inducing a conformational change that recruits the MAX2-SCF ubiquitin ligase complex to degrade SMXL repressor proteins (Yao et al., 2016; Nature).