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Proteasome activity determines pupation timing through the degradation speed of timer molecule Blimp‐1
Author(s) -
Aly Hamdy,
Akagi Kazutaka,
Ueda Hitoshi
Publication year - 2018
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/dgd.12569
Subject(s) - proteasome , ubiquitin ligase , gene knockdown , mg132 , microbiology and biotechnology , ubiquitin , repressor , chemistry , biology , proteasome inhibitor , biochemistry , gene expression , gene
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 β ftz‐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 MG 132. Pupation timing was delayed in mutants of 26S proteasome subunits as well as FBXO 11, 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 FBXO 11 mutant was suppressed by the induction of β FTZ ‐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 FBXO 11 in the fat body, which is important for determining pupation timing.