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Casein kinase 1 and disordered clock proteins form functionally equivalent, phospho-based circadian modules in fungi and mammals
Similar phosphate-based daily timing modules made by casein kinase 1 and unstable clock proteins in fungi and mammals
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Abstract
CK1 promotes of FRQ and mouse PER2 on a circadian timescale.
- CK1 targets numerous low-affinity phosphorylation sites on FRQ and mPER2.
- The process of phosphorylation is influenced by the recruitment of CK1 to specific sites.
- Phosphorylation kinetics are affected by the accessibility of disordered segments of FRQ and mPER2.
- Compromising CK1 activity disrupts circadian rhythms in both fungal and mammalian cells.
- CK1 and clock proteins FRQ and PER may function as equivalent timing mechanisms in various organisms.
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Key numbers
2 h
Circadian Period Shortening
CK1δ overexpression shortened the circadian period in T-REx-U2OS cells.
7 h
CK1δ-R178Q Effect on Circadian Period
CK1δ-R178Q expression shortened the circadian period even more than wild-type CK1δ.