Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 27, Issue 13, Pages 5002-5013Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.02338-06
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Funding
- NINDS NIH HHS [P01 NS044232, NS44232] Funding Source: Medline
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We identify in this study a 27-amino-acid motif which is conserved between the Drosophila melanogaster period protein (PER) and the three mammalian PERs. Characterization of PER lacking this motif (PERD) shows that it is important for phosphorylation of Drosophila PER by casein kinase IF, (CKIE; doubletime protein or DBT) and CKII. S2 cell assays indicate that the domain also contributes significantly to PER nuclear localization as well as to PER transcriptional repressor activity. These two phenomena appear linked, since PERD transcriptional repressor activity in S2 cells was restored when nuclear localization was facilitated. Two less direct assays of PERO activity in flies can be interpreted similarly. The separate assay of nuclear import and export suggests that the domain functions in part to facilitate PER phosphorylation within the cytoplasm, which in turn promotes nuclear entry. As there is evidence that the kinases also function within the nucleus to promote transcriptional repression, we suggest that there is a subsequent collaboration between phosphorylated PER and the kinases to repress CLK-CYC activity, probably through the phosphorylation of CLK. This is then followed by additional PER phosphorylation, which occurs within the nucleus and leads to PER degradation.
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