Document Detail


Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase.
MedLine Citation:
PMID:  17292865     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The CMP-sialic acid synthetase (CSS) catalyzes the activation of sialic acid (Sia) to CMP-Sia which is a donor substrate of sialyltransferases. The vertebrate CSSs are usually localized in nucleus due to the nuclear localization signal (NLS) on the molecule. In this study, we first point out that a small, but significant population of the mouse CMP-sialic acid synthetase (mCSS) is also present in cytoplasm, though mostly in nucleus. As a mechanism for the localization in cytoplasm, we first identified two nuclear export signals (NESs) in mCSS, based on the localization studies of the potential NES-deleted mCSS mutants as well as the potential NES-tagged eGFP proteins. These two NESs are conserved among mammalian and fish CSSs, but not present in the bacterial or insect CSS. These results suggest that the intracellular localization of vertebrate CSSs is regulated by not only the NLS, but also the NES sequences.
Authors:
Akiko Fujita; Chihiro Sato; Ken Kitajima
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-02-02
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  355     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2007 Mar 
Date Detail:
Created Date:  2007-02-23     Completed Date:  2007-04-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  174-80     Citation Subset:  IM    
Affiliation:
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Cell Nucleus / enzymology*
Mice
Molecular Sequence Data
N-Acylneuraminate Cytidylyltransferase / chemistry,  genetics,  metabolism*
Peptide Fragments / chemistry
Plasmids
Polydeoxyribonucleotides / chemistry
Polymerase Chain Reaction
Protein Transport
Recombinant Proteins / metabolism
Sequence Deletion
Chemical
Reg. No./Substance:
0/Peptide Fragments; 0/Polydeoxyribonucleotides; 0/Recombinant Proteins; EC 2.7.7.43/N-Acylneuraminate Cytidylyltransferase

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


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