Literature DB >> 9109415

Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4.

M Irmler1, K Hofmann, D Vaux, J Tschopp.   

Abstract

The two genes CED-4 and CED-3 (the nematode homologue of interleukin-1beta converting enzyme, ICE) of Caenorhabditis elegans are implicated in the control of cell death, but the mechanism by which this occurs is unknown. Here we provide evidence that CED-3 and CED-4 both contain sequences with homology to a domain present in RAIDD and the prodomain of certain ICE-like proteases (caspases). This domain is known to establish an interaction between RAIDD and these caspases. Similarly, CED-4 was found to interact with CED-3. Thus, the activity of the death protease CED-3 appears to be controlled by CED-4 through a direct physical interaction.

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Year:  1997        PMID: 9109415     DOI: 10.1016/s0014-5793(97)00271-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  14 in total

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4.  The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4.

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5.  Modulation of cell death by Bcl-XL through caspase interaction.

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Review 6.  Immunopathology of apoptosis--introduction and overview.

Authors:  D L Vaux
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Review 7.  Cell Death in C. elegans Development.

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8.  Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing.

Authors:  A Aballay; F M Ausubel
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-13       Impact factor: 11.205

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Review 10.  Cell death specification in C. elegans.

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