Document Detail


A small conserved domain of Drosophila PERIOD is important for circadian phosphorylation, nuclear localization, and transcriptional repressor activity.
MedLine Citation:
PMID:  17452453     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 (PER Delta) shows that it is important for phosphorylation of Drosophila PER by casein kinase I epsilon (CKI epsilon; 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 PER Delta transcriptional repressor activity in S2 cells was restored when nuclear localization was facilitated. Two less direct assays of PER Delta 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.
Authors:
Pipat Nawathean; Dan Stoleru; Michael Rosbash
Related Documents :
16683253 - Protein kinase cepsilon and development of squamous cell carcinoma, the nonmelanoma hum...
9285643 - Ischemic preconditioning induces selective translocation of protein kinase c isoforms e...
14744853 - A threshold mechanism governing activation of the developmental regulatory protein sigm...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-04-23
Journal Detail:
Title:  Molecular and cellular biology     Volume:  27     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-06-18     Completed Date:  2007-08-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5002-13     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute and Department of Biology, Brandeis University, Waltham, MA 02454, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
Cell Nucleus / metabolism*
Circadian Rhythm / physiology*
Conserved Sequence
Drosophila Proteins
Drosophila melanogaster / genetics*,  physiology
Models, Biological
Molecular Sequence Data
Motor Activity
Mutagenesis
Mutant Proteins / metabolism
Nuclear Proteins / chemistry*,  metabolism*
Period Circadian Proteins
Phenotype
Phosphorylation
Protein Processing, Post-Translational
Protein Structure, Tertiary
Protein Transport
Repressor Proteins / metabolism*
Structure-Activity Relationship
Transcription, Genetic*
Grant Support
ID/Acronym/Agency:
NS44232/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/Mutant Proteins; 0/Nuclear Proteins; 0/PER protein, Drosophila; 0/Period Circadian Proteins; 0/Repressor Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Epigenetic programming of the rRNA promoter by MBD3.
Next Document:  Unique requirement for Rb/E2F3 in neuronal migration: evidence for cell cycle-independent functions.