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 |
|---|---|
| Pages (from-to) | 502-508 |
| Number of pages | 7 |
| Journal | Development Growth and Differentiation |
| Volume | 60 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Oct 1 2018 |
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Keywords
- Blimp-1
- developmental timer
- Drosophila
- FBXO11
- proteasome
- pupation timing
ASJC Scopus subject areas
- Developmental Biology
- Cell Biology
Cite this
Proteasome activity determines pupation timing through the degradation speed of timer molecule Blimp-1. / Aly, Hamdy; Akagi, Kazutaka; Ueda, Hitoshi.
In: Development Growth and Differentiation, Vol. 60, No. 8, 01.10.2018, p. 502-508.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteasome activity determines pupation timing through the degradation speed of timer molecule Blimp-1
AU - Aly, Hamdy
AU - Akagi, Kazutaka
AU - Ueda, Hitoshi
PY - 2018/10/1
Y1 - 2018/10/1
N2 - 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.
AB - 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.
KW - Blimp-1
KW - developmental timer
KW - Drosophila
KW - FBXO11
KW - proteasome
KW - pupation timing
UR - http://www.scopus.com/inward/record.url?scp=85055424141&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85055424141&partnerID=8YFLogxK
U2 - 10.1111/dgd.12569
DO - 10.1111/dgd.12569
M3 - Article
C2 - 30368781
AN - SCOPUS:85055424141
VL - 60
SP - 502
EP - 508
JO - Development Growth and Differentiation
JF - Development Growth and Differentiation
SN - 0012-1592
IS - 8
ER -