TY - JOUR
AU - Baltimore, D
AB - 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.
TI - Essential role of CED-4 oligomerization in CED-3 activation and apoptosis.
JF - Science (New York, N.Y.)
DO - 10.1126/science.281.5381.1355
DA - 1998-09-09
UR - https://www.deepdyve.com/lp/pubmed/essential-role-of-ced-4-oligomerization-in-ced-3-activation-and-1cf06pgCJV
SP - 1355
EP - 7
VL - 281
IS - 5381
DP - DeepDyve
ER -