Protein-protein interaction in the mammalian circadian system

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Circadian clocks are endogenous oscillators that regulate daily rhythms in physiology and behaviour. In almost every cell a gene-regulatory network generates molecular circadian oscillations with protein phosphorylation and complex formation playing a crucial role for their dynamics. Here, we will analyze these interactions (with PER2 as paradigmatic protein) both on the molecular and the functional level. To this end, we aim to identify kinases phosphorylating PER2, characterize its interactions with CRY1 and CKIε/δ as well as pharmacologically perturb these interactions in an established dynamical cell-culture model with subsequent analysis of the effect on circadian rhythms.