Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling

<p>Abstract</p> <p>Background</p> <p>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...

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Main Authors: Imhof Axel, Morrice Nick, MacKintosh Carol, Lasi Margherita, Pauly Barbara, Regula Jörg, Rudd Stephen, David Charles N, Böttger Angelika
Format: Article
Language:English
Published: BMC 2007-07-01
Series:BMC Cell Biology
Online Access:http://www.biomedcentral.com/1471-2121/8/31
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spelling doaj-ba16f432515c44b5a6c625be48aace692020-11-24T22:11:20ZengBMCBMC Cell Biology1471-21212007-07-01813110.1186/1471-2121-8-31Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signallingImhof AxelMorrice NickMacKintosh CarolLasi MargheritaPauly BarbaraRegula JörgRudd StephenDavid Charles NBöttger Angelika<p>Abstract</p> <p>Background</p> <p>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<sup>2+ </sup>signalling.</p> <p>Results</p> <p>We found that the simple metazoan <it>Hydra </it>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 <it>Hydra vulgaris </it>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 <it>Hydra </it>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 <it>Hydra</it>-Bcl-2 like protein in vitro.</p> <p>Conclusion</p> <p>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 <it>Hydra</it>.</p> http://www.biomedcentral.com/1471-2121/8/31
collection DOAJ
language English
format Article
sources DOAJ
author Imhof Axel
Morrice Nick
MacKintosh Carol
Lasi Margherita
Pauly Barbara
Regula Jörg
Rudd Stephen
David Charles N
Böttger Angelika
spellingShingle Imhof Axel
Morrice Nick
MacKintosh Carol
Lasi Margherita
Pauly Barbara
Regula Jörg
Rudd Stephen
David Charles N
Böttger Angelika
Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
BMC Cell Biology
author_facet Imhof Axel
Morrice Nick
MacKintosh Carol
Lasi Margherita
Pauly Barbara
Regula Jörg
Rudd Stephen
David Charles N
Böttger Angelika
author_sort Imhof Axel
title Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
title_short Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
title_full Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
title_fullStr Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
title_full_unstemmed Proteomic screen in the simple metazoan <it>Hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca<sup>2+ </sup>signalling
title_sort proteomic screen in the simple metazoan <it>hydra </it>identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and ca<sup>2+ </sup>signalling
publisher BMC
series BMC Cell Biology
issn 1471-2121
publishDate 2007-07-01
description <p>Abstract</p> <p>Background</p> <p>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<sup>2+ </sup>signalling.</p> <p>Results</p> <p>We found that the simple metazoan <it>Hydra </it>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 <it>Hydra vulgaris </it>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 <it>Hydra </it>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 <it>Hydra</it>-Bcl-2 like protein in vitro.</p> <p>Conclusion</p> <p>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 <it>Hydra</it>.</p>
url http://www.biomedcentral.com/1471-2121/8/31
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