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Structural plasticity of D3–D14 ubiquitin ligase in strigolactone signalling
The plant F-box protein D3 has a C-terminal α-helix that switches between two conformational states, allowing the α/β hydrolase D14 to recruit the transcription repressor D53 for strigolactone-dependent degradation.
- Nitzan Shabek
- , Fabrizio Ticchiarelli
- & Ning Zheng
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Article |
D14–SCFD3-dependent degradation of D53 regulates strigolactone signalling
Strigolactones (SLs), key regulators of plant growth, are believed to mediate their responses through a proposed receptor (D14) that interacts with an F-box protein (D3) to form a D14–SCFD3 protein complex; here the perception of SLs by the D14–SCFD3 complex and the control of gene expression are linked by the finding that DWARF 53, a repressor protein of SL function, interacts with the D14–SCFD3 complex and is ubiquitinated and degraded in a SL-dependent manner.
- Feng Zhou
- , Qibing Lin
- & Jianmin Wan