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Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling

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 arra...

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Autores principales: Pauly, Barbara, Lasi, Margherita, MacKintosh, Carol, Morrice, Nick, Imhof, Axel, Regula, Jörg, Rudd, Stephen, David, Charles N, Böttger, Angelika
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1964759/
https://www.ncbi.nlm.nih.gov/pubmed/17651497
http://dx.doi.org/10.1186/1471-2121-8-31
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author Pauly, Barbara
Lasi, Margherita
MacKintosh, Carol
Morrice, Nick
Imhof, Axel
Regula, Jörg
Rudd, Stephen
David, Charles N
Böttger, Angelika
author_facet Pauly, Barbara
Lasi, Margherita
MacKintosh, Carol
Morrice, Nick
Imhof, Axel
Regula, Jörg
Rudd, Stephen
David, Charles N
Böttger, Angelika
author_sort Pauly, Barbara
collection PubMed
description 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 Ca(2+ )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.
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spelling pubmed-19647592007-09-05 Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling Pauly, Barbara Lasi, Margherita MacKintosh, Carol Morrice, Nick Imhof, Axel Regula, Jörg Rudd, Stephen David, Charles N Böttger, Angelika BMC Cell Biol Research Article 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 Ca(2+ )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. BioMed Central 2007-07-25 /pmc/articles/PMC1964759/ /pubmed/17651497 http://dx.doi.org/10.1186/1471-2121-8-31 Text en Copyright © 2007 Pauly et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Pauly, Barbara
Lasi, Margherita
MacKintosh, Carol
Morrice, Nick
Imhof, Axel
Regula, Jörg
Rudd, Stephen
David, Charles N
Böttger, Angelika
Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title_full Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title_fullStr Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title_full_unstemmed Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title_short Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca(2+ )signalling
title_sort proteomic screen in the simple metazoan hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and ca(2+ )signalling
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1964759/
https://www.ncbi.nlm.nih.gov/pubmed/17651497
http://dx.doi.org/10.1186/1471-2121-8-31
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