Proteasome activity determines pupation timing through the degradation speed of timer molecule Blimp-1

Hamdy Aly, Kazutaka Akagi, Hitoshi Ueda

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)502-508
Number of pages7
JournalDevelopment Growth and Differentiation
Volume60
Issue number8
DOIs
Publication statusPublished - Oct 1 2018

Keywords

  • Blimp-1
  • developmental timer
  • Drosophila
  • FBXO11
  • proteasome
  • pupation timing

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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