The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ced-9  -  Protein CED-9

Caenorhabditis elegans

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ced-9

  • These results support the hypothesis that viral infection can activate the same cell death pathway as is used during normal development and suggest that baculovirus p35 may act downstream or independently of ced-9 in this pathway [1].
 

High impact information on ced-9

  • The egl-1 gene negatively regulates the ced-9 gene, which protects against cell death and is a member of the bcl-2 family [2].
  • Our results suggest that the dual protective and killer functions of the C. elegans bcl-2-like gene ced-9 are mediated by inhibition of the killer and protective ced-4 functions, respectively [3].
  • The activity of the C. elegans gene ced-9 is required to protect cells that normally survive from undergoing programmed cell death [4].
  • Overexpression of bcl-2 can mimic the protective effect of ced-9 on C. elegans cell death and can prevent the ectopic cell deaths that occur in ced-9 loss-of-function mutants [4].
  • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2 [4].
 

Biological context of ced-9

 

Anatomical context of ced-9

 

Associations of ced-9 with chemical compounds

  • We conclude that this glycine has an important function in ced-9 regulation, and we suggest that alteration of this glycine in other members of the ced-9/bcl-2 family might lead to oncogenic activation [5].
  • We show here that an unusual gain-of-function mutation in ced-9 (substitution of glycine 169 to glutamate) that results in potent inhibition of most nematode cell deaths impairs the binding of EGL-1 to CED-9 and EGL-1-induced release of CED-4 from CED-4/CED-9 complexes [8].
  • Vertebrate homologues of both ced-3 and ced-9 have been identified as the genes encoding the caspase cysteine proteases and the Bcl-2 family, respectively [7].
  • Mitochondrial fragmentation is induced by the BH3-only protein EGL-1 and can be blocked by mutations in the bcl-2-like gene ced-9, indicating that members of the Bcl-2 family might function in the regulation of mitochondrial fragmentation in apoptotic cells [9].
 

Regulatory relationships of ced-9

 

Other interactions of ced-9

References

  1. Baculovirus p35 prevents developmentally programmed cell death and rescues a ced-9 mutant in the nematode Caenorhabditis elegans. Sugimoto, A., Friesen, P.D., Rothman, J.H. EMBO J. (1994) [Pubmed]
  2. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Conradt, B., Horvitz, H.R. Cell (1998) [Pubmed]
  3. An alternatively spliced C. elegans ced-4 RNA encodes a novel cell death inhibitor. Shaham, S., Horvitz, H.R. Cell (1996) [Pubmed]
  4. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Hengartner, M.O., Horvitz, H.R. Cell (1994) [Pubmed]
  5. Activation of C. elegans cell death protein CED-9 by an amino-acid substitution in a domain conserved in Bcl-2. Hengartner, M.O., Horvitz, H.R. Nature (1994) [Pubmed]
  6. Mechanisms of apoptosis: integration of genetic, biochemical, and cellular indicators. Stewart, B.W. J. Natl. Cancer Inst. (1994) [Pubmed]
  7. CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9. James, C., Gschmeissner, S., Fraser, A., Evan, G.I. Curr. Biol. (1997) [Pubmed]
  8. Demonstration of the in vivo interaction of key cell death regulators by structure-based design of second-site suppressors. Parrish, J., Metters, H., Chen, L., Xue, D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  9. DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Jagasia, R., Grote, P., Westermann, B., Conradt, B. Nature (2005) [Pubmed]
  10. Interaction and regulation of subcellular localization of CED-4 by CED-9. Wu, D., Wallen, H.D., Nuñez, G. Science (1997) [Pubmed]
  11. Bcl-2 overexpression blocks activation of the death protease CPP32/Yama/apopain. Monney, L., Otter, I., Olivier, R., Ravn, U., Mirzasaleh, H., Fellay, I., Poirier, G.G., Borner, C. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  12. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Yan, N., Chai, J., Lee, E.S., Gu, L., Liu, Q., He, J., Wu, J.W., Kokel, D., Li, H., Hao, Q., Xue, D., Shi, Y. Nature (2005) [Pubmed]
  13. Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death. Chen, F., Hersh, B.M., Conradt, B., Zhou, Z., Riemer, D., Gruenbaum, Y., Horvitz, H.R. Science (2000) [Pubmed]
 
WikiGenes - Universities