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, Tina; Zenner, G.; Popp, T.; Wagner, A.; Knapp, R. T.; Huber, A. H.; Grunert, M.; Söding, J.; David, C. N.; Boettger, A.

doi:10.1038/cr.2010.66

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

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

MPS-Authors

/persons/resource/persons128572

Söding, J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://www.nature.com/cr/journal/v20/n7/pdf/cr201066a.pdf
(出版社版)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

1944228.pdf
(出版社版), 2MB

付随資料 (公開)

There is no public supplementary material available

引用

Lasi, M., Pauly, B., Schmidt, N., Cikala, M., Stiening, B., Kaesbauer, T., Zenner, G., Popp, T., Wagner, A., Knapp, R. T., Huber, A. H., Grunert, M., Söding, J., David, C. N., & Boettger, A. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-0017-9636-5

要旨

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.