Document Detail


Molecular cloning and cellular distribution of two 14-3-3 isoforms from Hydra: 14-3-3 proteins respond to starvation and bind to phosphorylated targets.
MedLine Citation:
PMID:  12681283     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In the simple metazoan Hydra a clear link between food supply and cell survival has been established. Whilst in plants 14-3-3 proteins are found to be involved in signalling cascades that regulate metabolism, in animals they have been shown to participate in cell survival pathways. In order to explore the possibility that 14-3-3 proteins in Hydra could be involved in regulating metabolism under different conditions of food supply, we have cloned two isoforms of 14-3-3 proteins. We show here that 14-3-3 proteins bind to phosphorylated targets in Hydra and form homo- and heterodimers in vitro. 14-3-3 proteins are localised in the cytoplasm of all cells and also in the nuclei of some epithelial cells. This nuclear localisation becomes more prominent during starvation. Moreover, 14-3-3 protein is present in large amounts in food granules and from this we conclude that it performs functions which are associated with metabolism and food storage in Hydra.
Authors:
Barbara Pauly; Beate Stiening; Marsha Schade; Olga Alexandrova; Robert Zoubek; Charles N David; Angelika Böttger
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Experimental cell research     Volume:  285     ISSN:  0014-4827     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2003 Apr 
Date Detail:
Created Date:  2003-04-08     Completed Date:  2003-06-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15-26     Citation Subset:  IM    
Affiliation:
Zoological Institute, Ludwig-Maximilians-University Munich, D-80333 14, Munich, Luisenstrasse, Germany.
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MeSH Terms
Descriptor/Qualifier:
14-3-3 Proteins
Amino Acid Sequence
Animals
Cell Fractionation
Cell Nucleus / metabolism
Cloning, Molecular
Dimerization
Humans
Hydra / cytology,  metabolism*
Molecular Sequence Data
Phosphorylation
Phylogeny
Protein Binding
Protein Isoforms / classification,  genetics,  metabolism*
Sequence Alignment
Starvation*
Tyrosine 3-Monooxygenase / classification,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/14-3-3 Proteins; 0/Protein Isoforms; EC 1.14.16.2/Tyrosine 3-Monooxygenase

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


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