Cancer Institute A national cancer institute
designated cancer center

Howard Y. Chang

Publication Details

  • Essential role of CED-4 oligomerization in CED-3 activation and apoptosis SCIENCE Yang, X. L., Chang, H. Y., Baltimore, D. 1998; 281 (5381): 1355-1357

    Abstract:

    Control of the activation of apoptosis is important both in development and in protection against cancer. In the classic genetic model Caenorhabditis elegans, the pro-apoptotic protein CED-4 activates the CED-3 caspase and is inhibited by the Bcl-2-like protein CED-9. Both processes are mediated by protein-protein interaction. Facilitating the proximity of CED-3 zymogen molecules was found to induce caspase activation and cell death. CED-4 protein oligomerized in cells and in vitro. This oligomerization induced CED-3 proximity and competed with CED-4:CED-9 interaction. Mutations that abolished CED-4 oligomerization inactivated its ability to activate CED-3. Thus, the mechanism of control is that CED-3 in CED-3:CED-4 complexes is activated by CED-4 oligomerization, which is inhibited by binding of CED-9 to CED-4.

    View details for Web of Science ID 000075666800051

    View details for PubMedID 9721101

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