Abstract
The transcriptional repressor Blimp-1 is a labile protein. This characteristic is key for determining pupation timing because the timing of the disappearance of Blimp-1 affects pupation timing by regulating the expression of its target βftz-f1. However, the molecular mechanisms that regulate the protein turnover of Blimp-1 are still unclear. Here, we demonstrate that Blimp-1 is regulated by the ubiquitin proteasome system. We show that Blimp-1 degradation is inhibited by proteasome inhibitor MG132. Pupation timing was delayed in mutants of 26S proteasome subunits as well as FBXO11, which recruits target proteins to the 26S proteasome as a component of the SCF ubiquitin ligase complex by slowing down the degradation speed of Blimp-1. Delay in pupation timing in the FBXO11 mutant was suppressed by the induction of βFTZ-F1. Furthermore, fat-body-specific knockdown of proteasomal activity was sufficient to induce a delay in pupation timing. These results suggest that Blimp-1 is degraded by the 26S proteasome and is recruited by FBXO11 in the fat body, which is important for determining pupation timing.
Original language | English |
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Pages (from-to) | 502-508 |
Number of pages | 7 |
Journal | Development Growth and Differentiation |
Volume | 60 |
Issue number | 8 |
DOIs | |
Publication status | Published - Oct 2018 |
Keywords
- Blimp-1
- Drosophila
- FBXO11
- developmental timer
- proteasome
- pupation timing
ASJC Scopus subject areas
- Developmental Biology
- Cell Biology