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  The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins.

Lasi, M., Pauly, B., Schmidt, N., Cikala, M., Stiening, B., Kaesbauer, T., et al. (2010). The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins. Cell Research, 20(7), 812-825. doi:10.1038/cr.2010.66.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0017-9636-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DB82-5
Genre: Journal Article

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 Creators:
Lasi, M.1, Author
Pauly, B.1, Author
Schmidt, N.1, Author
Cikala, M.1, Author
Stiening, B.1, Author
Kaesbauer, Tina1, Author
Zenner, G.1, Author
Popp, T.1, Author
Wagner, A.1, Author
Knapp, R. T.1, Author
Huber, A. H.1, Author
Grunert, M.1, Author
Söding, J.2, Author              
David, C. N.1, Author
Boettger, A.1, Author
Affiliations:
1external, ou_persistent22              
2Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

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 Abstract: The fresh water polyp Hydra belongs to the phylum Cnidaria, which diverged from the metazoan lineage before the appearance of bilaterians. In order to understand the evolution of apoptosis in metazoans, we have begun to elucidate the molecular cell death machinery in this model organism. Based on ESTs and the whole Hydra genome assembly, we have identified 15 caspases. We show that one is activated during apoptosis, four have characteristics of initiator caspases with N-terminal DED, CARD or DD domain and two undergo autoprocessing in vitro. In addition, we describe seven Bcl-2-like and two Bak-like proteins. For most of the Bcl-2 family proteins, we have observed mitochondrial localization. When expressed in mammalian cells, HyBak-like 1 and 2 strongly induced apoptosis. Six of the Bcl-2 family members inhibited apoptosis induced by camptothecin in mammalian cells with HyBcl-2-like 4 showing an especially strong protective effect. This protein also interacted with HyBak-like 1 in a yeast two-hybrid assay. Mutation of the conserved leucine in its BH3 domain abolished both the interaction with HyBak-like 1 and the anti-apoptotic effect. Moreover, we describe novel Hydra BH-3-only proteins. One of these interacted with Bcl-2-like 4 and induced apoptosis in mammalian cells. Our data indicate that the evolution of a complex network for cell death regulation arose at the earliest and simplest level of multicellular organization, where it exhibited a substantially higher level of complexity than in the protostome model organisms Caenorhabditis and Drosophila.

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Language(s): eng - English
 Dates: 2010-05-182010
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/cr.2010.66
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Title: Cell Research
Source Genre: Journal
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Publ. Info: Beijing, China : Science Press
Pages: - Volume / Issue: 20 (7) Sequence Number: - Start / End Page: 812 - 825 Identifier: ISSN: 1001-0602
CoNE: /journals/resource/954927710256