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The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast.

Publication ,  Journal Article
Jabbour, AM; Ho, P-K; Puryer, MA; Ashley, DM; Ekert, PG; Hawkins, CJ
Published in: Cell Death Differ
December 2004

A genetically defined pathway orchestrates the removal of 131 of the 1090 somatic cells generated during the development of the hermaphrodite nematode Caenorhabditis elegans. Regulation of apoptosis is highly evolutionarily conserved and the nematode cell death pathway is a valuable model for studying mammalian apoptotic pathways, the dysregulation of which can contribute to numerous diseases. The nematode caspase CED-3 is ultimately responsible for the destruction of worm cells in response to apoptotic signals, but it must first be activated by CED-4. CED-9 inhibits programmed cell death and considerable data have demonstrated that CED-9 can directly bind and inhibit CED-4. However, it has been suggested that CED-9 may also directly inhibit CED-3. In this study, we used a yeast-based system and biochemical approaches to explore this second potential mechanism of action. While we confirmed the ability of CED-9 to inhibit CED-4, our data argue that CED-9 can not directly inhibit CED-3.

Duke Scholars

Published In

Cell Death Differ

DOI

ISSN

1350-9047

Publication Date

December 2004

Volume

11

Issue

12

Start / End Page

1309 / 1316

Location

England

Related Subject Headings

  • Signal Transduction
  • Saccharomyces cerevisiae
  • Proto-Oncogene Proteins c-bcl-2
  • Proto-Oncogene Proteins
  • In Vitro Techniques
  • Gene Expression Regulation, Fungal
  • Feedback, Physiological
  • Enzyme Activation
  • Caspases
  • Calcium-Binding Proteins
 

Citation

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MLA
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Jabbour, A. M., Ho, P.-K., Puryer, M. A., Ashley, D. M., Ekert, P. G., & Hawkins, C. J. (2004). The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast. Cell Death Differ, 11(12), 1309–1316. https://doi.org/10.1038/sj.cdd.4401501
Jabbour, A. M., P. -. K. Ho, M. A. Puryer, D. M. Ashley, P. G. Ekert, and C. J. Hawkins. “The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast.Cell Death Differ 11, no. 12 (December 2004): 1309–16. https://doi.org/10.1038/sj.cdd.4401501.
Jabbour AM, Ho P-K, Puryer MA, Ashley DM, Ekert PG, Hawkins CJ. The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast. Cell Death Differ. 2004 Dec;11(12):1309–16.
Jabbour, A. M., et al. “The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast.Cell Death Differ, vol. 11, no. 12, Dec. 2004, pp. 1309–16. Pubmed, doi:10.1038/sj.cdd.4401501.
Jabbour AM, Ho P-K, Puryer MA, Ashley DM, Ekert PG, Hawkins CJ. The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast. Cell Death Differ. 2004 Dec;11(12):1309–1316.

Published In

Cell Death Differ

DOI

ISSN

1350-9047

Publication Date

December 2004

Volume

11

Issue

12

Start / End Page

1309 / 1316

Location

England

Related Subject Headings

  • Signal Transduction
  • Saccharomyces cerevisiae
  • Proto-Oncogene Proteins c-bcl-2
  • Proto-Oncogene Proteins
  • In Vitro Techniques
  • Gene Expression Regulation, Fungal
  • Feedback, Physiological
  • Enzyme Activation
  • Caspases
  • Calcium-Binding Proteins