
In mammals, transcriptional autorepression by Period (PER) and Cryptochrome (CRY) protein complexes is essential for the generation of circadian rhythms. We have identified CAVIN-3 as a new, cytoplasmic PER2-interacting protein influencing circadian clock properties. Thus, CAVIN-3 loss- and gain-of-function shortened and lengthened, respectively, the circadian period in fibroblasts and affected PER:CRY protein abundance and interaction. While depletion of protein kinase Cδ (PKCδ), a known partner of CAVIN-3, had little effect on circadian gene expression, CAVIN-3 required the PKCδ-binding site to exert its effect on period length. This suggests the involvement of yet uncharacterized protein kinases. Finally, CAVIN-3 activity in circadian gene expression was independent of caveolae.
Intracellular Signaling Peptides and Proteins, Membrane Proteins, RNA-Binding Proteins, Period Circadian Proteins, Caveolae, Cryptochromes, Mice, Protein Kinase C-delta, Protein Transport, Gene Expression Regulation, Circadian Clocks, NIH 3T3 Cells, Animals, Protein Binding
Intracellular Signaling Peptides and Proteins, Membrane Proteins, RNA-Binding Proteins, Period Circadian Proteins, Caveolae, Cryptochromes, Mice, Protein Kinase C-delta, Protein Transport, Gene Expression Regulation, Circadian Clocks, NIH 3T3 Cells, Animals, Protein Binding
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