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DWARF14, A Receptor Covalently Linked with the Active Form of Strigolactones, Undergoes Strigolactone-Dependent Degradation in Rice
The Dwarf14 Receptor Linked to Active Strigolactones Breaks Down in Rice When Strigolactones Are Present
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Abstract
D14, an enzyme-receptor, is ubiquitinated and degraded after strigolactone treatment in rice.
- Strigolactones regulate shoot branching by inhibiting bud outgrowth in higher plants.
- The enzyme-receptor D14 hydrolyzes strigolactones and undergoes covalent modification.
- Ubiquitination of D14 occurs following strigolactone treatment and is processed by the 26S proteasome system.
- The Lys280 site in the D14 amino acid sequence is crucial for its degradation but does not affect its localization or interactions with D3 and D53.
- D14 degradation is dependent on D3 and closely linked to the protein levels of D53.
- D14 degradation follows D53 degradation, indicating a feedback regulation mechanism for strigolactone perception in rice.
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