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Mutation in a PER2 protein region disrupts the daily timing switch
Updated
Abstract
Knock-in mice with the PER2-Ser478Ala mutation exhibited a longer in behavioral analysis.
- The mutation caused accumulation of PER2 protein in both the nucleus and cytoplasm of the liver.
- Messenger RNA levels of PER2 were minimally affected by the mutation.
- Increased levels of nuclear PER1, CRY1, and CRY2 proteins were observed, likely due to stabilization of PER2-containing complexes.
- Circadian period and temperature compensation were disrupted in mouse embryonic fibroblasts derived from the mutant mice.
- These findings provide direct in vivo evidence for the role of phosphorylation in regulating PER2 stability and its influence on the circadian clock.
Simplified
Key numbers
1 h
Increase in Length
length in PER2-S478A mice vs. wild-type mice.
2×
Peak PER2 Protein Level Increase
Peak levels of PER2 protein in PER2-S478A mice vs. wild-type mice.
0.92
Temperature Compensation Q Value
Q value in PER2-S478A mice vs. control mice.