SLMB binds phosphorylated nuclear PER, facilitating its ubiquitination

Stable Identifier
R-DME-432483
Type
Reaction [uncertain]
Species
Drosophila melanogaster
Compartment
ReviewStatus
5/5
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During the day, with levels of its stabilising partner Timeless (TIM) drastically reduced by light, hyperphosphorylated Period (PER) becomes a target for the F-box containing protein, supernumerary limbs (SLMB). Ser47 phosphorylation of Period (PER) appears to be the trigger for SLMB to bind phosphorylated PER, facilitating its ubiquitination and marking it for processing by the 26S proteasome. In this model for the Circadian Clock pathway we are assuming that the cytoplasmic and nuclear mechanisms for PER degradation are the same.
Literature References
PubMed ID Title Journal Year
12432393 The F-box protein slimb controls the levels of clock proteins period and timeless

Grima, B, Lamouroux, A, Limbourg-Bouchon, B, Papin, C, Rouyer, F, Chélot, E

Nature 2002
12442174 Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime

Jiang, J, Edery, I, Ko, HW

Nature 2002
18593878 The phospho-occupancy of an atypical SLIMB-binding site on PERIOD that is phosphorylated by DOUBLETIME controls the pace of the clock

Vanselow, JT, Edery, I, Kramer, A, Chiu, JC

Genes Dev 2008
Participants
Participates
Catalyst Activity

ubiquitin ligase-substrate adaptor activity of SLMB [nucleoplasm]

Authored
Reviewed
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