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CLOCK deubiquitylation by USP8 inhibits CLK/CYC transcription in Drosophila
USP8 reverses CLOCK protein changes to reduce CLK/CYC gene activity in fruit flies
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Abstract
Loss of function of ubiquitin-specific protease 8 (USP8) enhances CLK/CYC transcriptional activity in Drosophila.
- USP8 interacts with the CLOCK (CLK) protein, suggesting a regulatory role in circadian transcription.
- In flies with reduced USP8 function, the molecular oscillations of clock proteins and mRNAs are nearly absent in circadian neurons.
- CLK ubiquitylation is found to cycle in wild-type flies, peaking when CLK/CYC transcription is at its highest.
- The absence of USP8 leads to increased ubiquitylation of CLK, which may enhance CLK/CYC transcriptional activity.
- USP8 mRNA levels cycle and are directly activated by CLK/CYC, indicating its involvement in the circadian feedback loop.
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