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. 1998 May 15;93(4):519-29.
doi: 10.1016/s0092-8674(00)81182-4.

The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9

B Conradt  1 , H R Horvitz
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Free article

The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9

B Conradt et al. Cell. .
Free article

Abstract

Gain-of-function mutations in the Caenorhabditis elegans gene egl-1 cause the HSN neurons to undergo programmed cell death. By contrast, a loss-of-function egl-1 mutation prevents most if not all somatic programmed cell deaths. The egl-1 gene negatively regulates the ced-9 gene, which protects against cell death and is a member of the bcl-2 family. The EGL-1 protein contains a nine amino acid region similar to the Bcl-2 homology region 3 (BH3) domain but does not contain a BH1, BH2, or BH4 domain, suggesting that EGL-1 may be a member of a family of cell death activators that includes the mammalian proteins Bik, Bid, Harakiri, and Bad. The EGL-1 and CED-9 proteins interact physically. We propose that EGL-1 activates programmed cell death by binding to and directly inhibiting the activity of CED-9, perhaps by releasing the cell death activator CED-4 from a CED-9/CED-4-containing protein complex.

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