CLK is degraded by the 26S proteasome

Stable Identifier
R-DME-432510
Type
Reaction [omitted]
Species
Drosophila melanogaster
Compartment
nucleoplasm
ReviewStatus
5/5
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CLK is degraded by the 26S proteasome
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Hyperphosphorylated Clock (CLK) is degraded by the 26S proteasome via an unknown intermediate mechanism.
Literature References
PubMed ID Title Journal Year
16139204 The circadian timekeeping system of Drosophila

Hardin, PE

Curr Biol 2005
16543224 PER-dependent rhythms in CLK phosphorylation and E-box binding regulate circadian transcription

Dauwalder, B, Hardin, PE, Zheng, H, Houl, JH, Yu, W

Genes Dev 2006
16603629 Balance between DBT/CKIepsilon kinase and protein phosphatase activities regulate phosphorylation and stability of Drosophila CLOCK protein

Kim, EY, Edery, I

Proc Natl Acad Sci U S A 2006
Participants
Input
Output
Participates
as an event of
Catalyst Activity

endopeptidase activity of 26S proteasome [nucleoplasm]

Physical Entity
26S proteasome [nucleoplasm] (Drosophila melanogaster)
Activity
endopeptidase activity (GO:0004175)
Authored
Williams, MG  (2009-08-13)
Reviewed
Edery, I  (2010-07-06)
Created
Williams, MG  (2009-08-14)
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