Document Detail


Serine 714 might be implicated in the regulation of the phosphorylation in other areas of mPer1 protein.
MedLine Citation:
PMID:  16750171     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The phosphorylation of mPer proteins may play important roles in the mechanism of the circadian clock via changes in subcellular localization and degradation. However, the mechanism has remained unclear. Previously, we identified three putative casein kinase (CK)1epsilon phosphorylation motif clusters in mPer1. In this work, we examined the role of the phosphorylation of serine residue, Ser(S)714, in mPer1. mPer1 S[714-726]A mutant, in which potential phosphorylation serine residues replaced by alanine residues, is rapidly phosphorylated compared with wild-type mPer1 by CK1epsilon. Coexpression with S[714]G mutant of mPer1 advanced phase of circadian expression of mPer2-luc expression, which was monitored by in vitro bioluminescence system. This result showed that the mPER1 S[714]G mutation affects circadian core oscillator. Considering these, it seems that Ser 714 might be involved in the regulation of the phosphorylation of other sites in mPer1 by CK1epsilon.
Authors:
Atsuko Takano; Katsuya Nagai
Publication Detail:
Type:  Journal Article     Date:  2006-05-24
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  346     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-06-19     Completed Date:  2006-08-28     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  95-101     Citation Subset:  IM    
Affiliation:
Institute for Protein Research, Osaka University, 3-2 Yamada-Oka, Suita, Osaka 565-0871, Japan. takano@obi.or.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites
COS Cells
Casein Kinase Iepsilon / metabolism
Cell Cycle Proteins
Cercopithecus aethiops
Mice
Nuclear Proteins / genetics,  metabolism*
Period Circadian Proteins
Phosphorylation / drug effects
Serine / physiology*
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Nuclear Proteins; 0/Per1 protein, mouse; 0/Period Circadian Proteins; 56-45-1/Serine; EC 2.7.11.1/Casein Kinase Iepsilon

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


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