Proceedings of the National Academy of Sciences of the United States of America

Mutation in a PER2 protein region disrupts the daily timing switch

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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.

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Funding

Competing interests

The authors declare no competing interest.
PubMed

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