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A more recent version of this article appeared on May 1, 2002
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Submitted on September 13, 2001
Revised on December 14, 2001
Accepted on February 1, 2002
1 Department of Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, NY 14263
2 Department of Cancer Genetics, Roswell Park Cancer Institute, Buffalo, NY 14263
3 Department of Diabetes, Endocrinology and Metabolism, City of Hope National Medical Center, 1500 Duarte Rd., Duarte, CA 91010
4 Centro de Biologia Molecular "Severo Ochoa", Consejo Superior de Investigaciones Cientificas and Universidad Autonoma de Madrid, Cantoblanco, 28049 Madrid, Spain
* Corresponding author. E-mail address: heinz.baumann{at}roswellpark.org.
* Corresponding author. E-mail address: wburhans{at}acsu.buffalo.edu.
The highly conserved Cdc6 protein is required for initiation of eukaryotic DNA replication and, in yeast and Xenopus, for the coupling of DNA replication to mitosis. Here we show that human Cdc6 is rapidly destroyed by a p53-independent, proteasome- and ubiquitin-dependent pathway during early stages of programmed cell death induced by the DNA damaging drug adozelesin, or by a separate caspase-dependent pathway in cells undergoing apoptosis through an extrinsic pathway induced by TNF
and cycloheximide. The proteasome-dependent pathway induced by adozelesin is conserved in the budding yeast S. cerevisiae. The destruction of Cdc6 may be a primordial programmed death response that uncouples DNA replication from the cell division cycle, which is reinforced in metazoans by the evolution of caspases and p53.
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