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Circadian clock control of eIF2α phosphorylation is necessary for rhythmic translation initiation
Daily body clock control of eIF2α phosphorylation is needed for regular protein production cycles
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Abstract
Inhibitory phosphorylation of eIF2α peaks during the subjective day, indicating a clock-controlled mechanism for regulating translation initiation.
- Phosphorylation levels of eIF2α are regulated by the circadian clock.
- The eIF2α kinase is rhythmically activated, which is essential for the cycling of P-eIF2α.
- Alterations in charged tRNA levels disrupt the rhythmic activation of CPC-3.
- In vitro studies show that clock-controlled P-eIF2α levels lead to reduced translation during the day.
- In vivo, rhythmic P-eIF2α levels are necessary for the synthesis of specific proteins.
- Loss of rhythmic P-eIF2α levels is associated with reduced linear growth rates in Neurospora crassa.
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Key numbers
2×
Increase in P-eIF2α Levels
P-eIF2α levels were twofold higher in untreated WT cells at DD40 compared to DD28.
30%
Decrease in Growth Rate
Growth rate was reduced to a level comparable to Δ cells when P-eIF2α levels were disrupted.