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Open Access Research article

Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signalling

Barbara Pauly14, Margherita Lasi1, Carol MacKintosh2, Nick Morrice2, Axel Imhof1, Jörg Regula1, Stephen Rudd3, Charles N David1 and Angelika Böttger1*

Author Affiliations

1 Ludwig-Maximilians-University Munich, Germany

2 Department of Biochemistry, Dundee University, Dundee, UK

3 Joint Bioinformatics Laboratory, Turku Centre for Biotechnology, Turku, Finland

4 Department of Molecular and Cell Biology, University of California, Berkeley, USA

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BMC Cell Biology 2007, 8:31  doi:10.1186/1471-2121-8-31

Published: 25 July 2007

Abstract

Background

14-3-3 proteins have been implicated in many signalling mechanisms due to their interaction with Ser/Thr phosphorylated target proteins. They are evolutionarily well conserved in eukaryotic organisms from single celled protozoans and unicellular algae to plants and humans. A diverse array of target proteins has been found in higher plants and in human cell lines including proteins involved in cellular metabolism, apoptosis, cytoskeletal organisation, secretion and Ca2+ signalling.

Results

We found that the simple metazoan Hydra has four 14-3-3 isoforms. In order to investigate whether the diversity of 14-3-3 target proteins is also conserved over the whole animal kingdom we isolated 14-3-3 binding proteins from Hydra vulgaris using a 14-3-3-affinity column. We identified 23 proteins that covered most of the above-mentioned groups. We also isolated several novel 14-3-3 binding proteins and the Hydra specific secreted fascin-domain-containing protein PPOD. In addition, we demonstrated that one of the 14-3-3 isoforms, 14-3-3 HyA, interacts with one Hydra-Bcl-2 like protein in vitro.

Conclusion

Our results indicate that 14-3-3 proteins have been ubiquitous signalling components since the start of metazoan evolution. We also discuss the possibility that they are involved in the regulation of cell numbers in response to food supply in Hydra.