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Science 21 February 1997: Vol. 275. no. 5303, pp. 1122 - 1126 DOI: 10.1126/science.275.5303.1122
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Reports
Interaction of CED-4 with CED-3 and CED-9: A Molecular Framework for Cell Death
Arul M. Chinnaiyan,
Karen O'Rourke,
Brian
R. Lane,
Vishva M. Dixit
*
Previous genetic studies of the nematode Caenorhabditis
elegans identified three important components of the cell death
machinery. CED-3 and CED-4 function to kill cells, whereas CED-9
protects cells from death. Here CED-9 and its mammalian homolog
Bcl-xL (a member of the Bcl-2 family of cell death
regulators) were both found to interact with and inhibit
the function of CED-4. In addition, analysis revealed that CED-4 can
simultaneously interact with CED-3 and its mammalian counterparts
interleukin-1 -converting enzyme (ICE) and FLICE. Thus, CED-4
plays a central role in the cell death pathway, biochemically linking
CED-9 and the Bcl-2 family to CED-3 and the ICE family of pro-apoptotic
cysteine proteases.
University of Michigan Medical School, Department of Pathology,
Ann Arbor, MI 48109, USA.
*
To whom correspondence should be addressed.
Read the Full Text
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- E1B 19K Inhibits Fas-mediated Apoptosis through FADD-dependent Sequestration of FLICE.
- D. Perez and E. White (1998)
J. Cell Biol.
141, 1255-1266
| Abstract »
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- Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger Apoptosis.
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J. Cell Biol.
141, 1243-1253
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- Proteases to die for.
- V. Cryns and J. Yuan (1998)
Genes & Dev.
12, 1551-1570
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- Potassium Leakage During the Apoptotic Degradation Phase.
- B. Dallaporta, T. Hirsch, S. A. Susin, N. Zamzami, N. Larochette, C. Brenner, I. Marzo, and G. Kroemer (1998)
J. Immunol.
160, 5605-5615
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- Bax directly induces release of cytochrome c from isolated mitochondria.
- J. M. Jurgensmeier, Z. Xie, Q. Deveraux, L. Ellerby, D. Bredesen, and J. C. Reed (1998)
PNAS
95, 4997-5002
| Abstract »
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- ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases.
- T. Koseki, N. Inohara, S. Chen, and G. Nunez (1998)
PNAS
95, 5156-5160
| Abstract »
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- Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation.
- Y. Hu, M. A. Benedict, D. Wu, N. Inohara, and G. Nunez (1998)
PNAS
95, 4386-4391
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- Mtd, a Novel Bcl-2 Family Member Activates Apoptosis in the Absence of Heterodimerization with Bcl-2 and Bcl-XL.
- N. Inohara, D. Ekhterae, I. Garcia, R. Carrio, J. Merino, A. Merry, S. Chen, and G. Nunez (1998)
J. Biol. Chem.
273, 8705-8710
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- Systemic Overexpression of BCL-2 in the Hematopoietic System Protects Transgenic Mice From the Consequences of Lethal Irradiation.
- J. Domen, K. L. Gandy, and I. L. Weissman (1998)
Blood
91, 2272-2282
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- Synthetic activation of caspases: Artificial death switches.
- R. A. MacCorkle, K. W. Freeman, and D. M. Spencer (1998)
PNAS
95, 3655-3660
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- Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell-type-dependent manner.
- V. Galvan and B. Roizman (1998)
PNAS
95, 3931-3936
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- The Caspase-3 Precursor Has a Cytosolic and Mitochondrial Distribution: Implications for Apoptotic Signaling.
- M. Mancini, D. W. Nicholson, S. Roy, N. A. Thornberry, E. P. Peterson, L. A. Casciola-Rosen, and A. Rosen (1998)
J. Cell Biol.
140, 1485-1495
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- The Binding Properties and Biological Activities of Bcl-2 and Bax in Cells Exposed to Apoptotic Stimuli.
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J. Biol. Chem.
273, 6110-6120
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- Defects in the Ubiquitin Pathway Induce Caspase-independent Apoptosis Blocked by Bcl-2.
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J. Biol. Chem.
273, 6121-6131
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- Caspase-9, Bcl-XL, and Apaf-1 Form a Ternary Complex.
- G. Pan, K. O'Rourke, and V. M. Dixit (1998)
J. Biol. Chem.
273, 5841-5845
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